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Department of Pharmacology, Monash University, Clayton, VIC 3800, Australia
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Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia
Department of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Melbourne, VIC 3000, Australia
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Correspondence Address: Del Borgo, M.P.; Department of Pharmacology, Australia; email: mark.delborgo@monash.edu
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Small tripeptides composed entirely of beta 3-amino acids have been shown to self-assemble into fibres following acylation of the N-terminus. Given the use of Fmoc as a strategy to initiate self-assembly in alpha-peptides, we hypothesized that the acyl cap can be replaced by an Fmoc without perturbation to the self-assembly and enable simpler synthetic protocols. We therefore replaced the N-acyl cap for an Fmoc group and herein we show that these Fmoc-protected beta 3-peptides produce regular spherical particles, rather than fibrous structures, that are stable and capable of encapsulating cargo. We then demonstrated that these particles were able to deliver cargo to cells without any obvious signs of cytotoxicity. This is the first description of such regular nanoparticles derived from Fmoc-protected beta 3-peptides.Alteration to the N-terminal cap of beta-peptides switches self-assembly from fibrillar to spherical structures.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Chen, Yi-Kai </span> <span class="author-type"> </span> ; <span class="author-name" > Simon, Isabella A. </span> <span class="author-type"> </span> ; <span class="author-name" > Maslov, Ivan </span> <span class="author-type"> </span> ; <span class="author-name" > Oyarce-Pino, Ivan E. </span> <span class="author-type"> </span> ; <span class="author-name" > Kulkarni, Ketav </span> <span class="author-type"> </span> ; <span class="author-name" > Hopper, Denham </span> <span class="author-type"> </span> ; <span class="author-name" > Aguilar, Marie-Isabel </span> <span class="author-type"> </span> ; <span class="author-name" > Vankadari, Naveen </span> <span class="author-type"> </span> ; <span class="author-name" > Broughton, Brad R. S. </span> <span class="author-type"> </span> ; <span class="author-name" > Del Borgo, Mark P. ✉ </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;34250241" mtid="34250241" target="_blank">A switch in N-terminal capping of β-peptides creates novel self-assembled nanoparticles</a></div> <div class="pub-info"> <span class="journal-title">RSC ADVANCES</span> <span class="journal-volume">13</span> : <span class="journal-issue">42</span> <span class="page"> pp. 29401-29407. , 7 p. </span> <span class="year">(2023)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1039/d3ra04514e" target="_blank" href="https://doi.org/10.1039/d3ra04514e"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="001077573300001" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/001077573300001"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85176593856" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85176593856"> Scopus </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:34250241 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;34250241" target="_blank">A switch in N-terminal capping of β-peptides creates novel self-assembled nanoparticles</a></div> <div> <span class="journal-title">RSC ADVANCES</span>
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<div class="lastModified">Utolsó módosítás: 2024.02.27. 14:46 Pécsi Éva (MTMT Közp 3, admin)
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Department of Pharmacology, Monash University, Clayton, VIC 3800, Australia
Department of Biochemistry & Molecular Biology, Monash University, Clayton, VIC 3800, Australia
Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia
Department of Biochemistry and Pharmacology, Bio21 Molecular Science and...</pre>
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Departamento de Química Orgánica, Universidade de Santiago de Compostela, Avda. das Ciencias s/n, Santiago de Compostela, 15782, Spain
Chemistry Research Laboratory, Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, United Kingdom
Export Date: 6 March 2024
CODEN: OBCRA
Correspondence Address: Estévez, J.C.; Centro Singular de Investigación en Química Biolóxica e Materiais Moleculares (CIQUS), c/Jenaro de la Fuente s/n, Spain; email: juancarlos.estevez@usc.es
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We describe the synthesis of trihydroxylated cyclohexane β-amino acids from (−)-shikimic acid, in their cis and trans configuration, and the incorporation of the trans isomer into a trans-2-aminocyclohexanecarboxylic acid peptide chain. Subsequently, the hydroxyl groups were partially or totally deprotected. The structural study of the new peptides by FTIR, CD, solution NMR and DFT calculations revealed that they all fold into a 14-helix secondary structure, similarly to the homooligomer of trans-2-aminocyclohexanecarboxylic acid. This means that the high degree of substitution of the cyclohexane ring of the new residue is compatible with the adoption of a stable helical secondary structure and opens opportunities for the design of more elaborate peptidic foldamers with oriented polar substituents at selected positions of the cycloalkane residues. © 2023 The Royal Society of Chemistry
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Reza, D. </span> <span class="author-type"> </span> ; <span class="author-name" > Balo, R. </span> <span class="author-type"> </span> ; <span class="author-name" > Otero, J.M. </span> <span class="author-type"> </span> ; <span class="author-name" > Fletcher, A.M. </span> <span class="author-type"> </span> ; <span class="author-name" > García-Fandino, R. </span> <span class="author-type"> </span> ; <span class="author-name" > Sánchez-Pedregal, V.M. </span> <span class="author-type"> </span> ; <span class="author-name" > Davies, S.G. </span> <span class="author-type"> </span> ; <span class="author-name" > Estévez, R.J. </span> <span class="author-type"> </span> ; <span class="author-name" > Estévez, J.C. ✉ </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;34318027" mtid="34318027" target="_blank">β-Peptides incorporating polyhydroxylated cyclohexane β-amino acid: synthesis and conformational study</a></div> <div class="pub-info"> <span class="journal-title">ORGANIC & BIOMOLECULAR CHEMISTRY</span> <span class="journal-volume">21</span> <span class="page"> pp. 8535-8547. , 13 p. </span> <span class="year">(2023)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1039/d3ob00906h" target="_blank" href="https://doi.org/10.1039/d3ob00906h"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:black" title="10.26434/chemrxiv-2022-zdb5j" target="_blank" href="https://doi.org/10.26434/chemrxiv-2022-zdb5j"> Preprint DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="001119457500001" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/001119457500001"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85175313142" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85175313142"> Scopus </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:34318027 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Centro Singular de Investigación en Química Biolóxica e Materiais Moleculares (CIQUS), Departamento de Química Orgánica, Universidade de Santiago de Compostela, c/Jenaro de la Fuente s/n, Santiago de Compostela, 15782, Spain
Departamento de Química Orgánica, Universidade de Santiago de Compostela, Avda. das Ciencias s/n, Santiago de Compostela, 15782, Spain
...</pre>
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We explored trans- and cis-2-aminocycloheptanecarboxylic acid (ACHpC) as potential building blocks for helical foldamers. trans-ACHpC does not show sufficient folding propensity in unnatural peptides. cis-ACHpC promotes nontraditional helices of two unnatural peptide backbones: the 11/9-helix for 1:1 alpha/beta-peptides and the 12/10-helix for beta-peptides with interconvertible handedness. The two opposite-handed 12/10-helices rapidly interconvert in solution by pseudorotation of the two twist chair forms of the cycloheptane moiety in each cis-ACHpC residue.
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Department of Chemistry, Yonsei University, Seoul, 03722, South Korea
Department of Chemistry, University of Wisconsin, Madison, WI 53706, United States
Export Date: 6 March 2024
CODEN: ORLEF
Correspondence Address: Choi, S.H.; Department of Chemistry, South Korea; email: sh-choi@yonsei.ac.kr</pre>
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Self-assembly of peptides demonstrates a great potential for designing highly ordered, finely tailored supramolecular arrangements enriched with high specificity, improved efficacy and biological activity. Along with natural peptides, hybrid peptide systems composed of natural and chemically diverse unnatural amino acids have been used in various fields, including drug delivery, wound healing, potent inhibition of diseases, and prevention of biomaterial related diseases to name a few. In this review, we provide a brief outline of various methods that have been utilized for obtaining fascinating structures that create an avenue to reproduce a range of functions resulting from these folds. An overview of different self-assembled structures as well as their applications will also be provided. We believe that this review is very relevant to the current scenario and will cover conformations of hybrid peptides and resulting self-assemblies from the late 20(th) century through 2022. This review aims to be a comprehensive and reliable account of the hybrid peptide-based self-assembly owing to its enormous influence in understanding and mimicking biological processes.
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;33173758" target="_blank">Advances in hybrid peptide-based self-assembly systems and their applications</a></div> <div> <span class="journal-title">BIOMATERIALS SCIENCE</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :4
Export Date: 6 March 2024
Correspondence Address: Roy, A.; Applied Organic Chemistry Group, Pulibor, Assam, India; email: aroy@neist.res.in</pre>
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The α/β-peptide 11/9-helix and the β-peptide 12/10-helix belong to "mixed"helices, in which two types of hydrogen bonds with opposite directionality alternate along the helical axis. cis-2-Aminocyclohexanecarboxylic acid (cis-ACHC) is known to promote these mixed helices and stabilize the helical propensity more than other acyclic β-residues. Application of a mixed-helical backbone still requires sufficient solubility in aqueous solution. In this regard, we chose cis-4-aminopiperidine-3-carboxylic acid (cis-APiC) as a foldamer building block that can provide both sufficient aqueous solubility and mixed-helical propensity. Conformational analyses of α/β- and β-peptides containing a cis-APiC residue by circular dichroism spectroscopy and single-crystal X-ray crystallography suggest that the incorporation of cis-APiC instead of cis-ACHC can enhance the aqueous solubility of the mixed-helical peptides without any adverse effect on helical folding. In addition, the ratio between right- and left-handed 12/10-helices of β-peptides can be rationalized by relative energies between the local conformations of the cis-APiC residue. This journal is © The Royal Society of Chemistry.
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;32696667" target="_blank">Effect of a: Cis -4-aminopiperidine-3-carboxylic acid (cis -APiC) residue on mixed-helical folding of unnatural peptides</a></div> <div> <span class="journal-title">ORGANIC & BIOMOLECULAR CHEMISTRY</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Export Date: 6 March 2024
CODEN: OBCRA
Correspondence Address: Choi, S.; Department of Chemistry, South Korea; email: sh-choi@yonsei.ac.kr</pre>
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Anti-β2,3-amino acids are a class of acyclic β-amino acids that usually stabilize β-sheet-like conformations of unnatural peptides. (2S,3R)-3-amino-2-ethylpentanoic acid (AEPA) is a diethyl-substituted anti-β2,3-amino acid that can be regarded as an acyclic analog of cis-2-aminocyclohexanecarboxylic acid, which is known to promote the α/β-peptide 11/9-helix and the β-peptide 12/10-helix. We report that AEPA can be incorporated into the two unnatural peptide helices without disrupting helical folding. Crystal structure data reveal that the anti-β2,3-residue adopts unconventional gauche (+) conformation in those unnatural peptide helices. © 2021 Korean Chemical Society, Seoul & Wiley-VCH GmbH
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Choi, S. ✉ </span> <span class="author-type"> </span> ; <span class="author-name" > Choi, S.H. ✉ </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;32693883" mtid="32693883" target="_blank">Synthesis and conformational analysis of an anti-β2,3-amino acid as a building block for unnatural peptide helices</a></div> <div class="pub-info"> <span class="journal-title">BULLETIN OF THE KOREAN CHEMICAL SOCIETY</span> <span class="journal-volume">43</span> : <span class="journal-issue">2</span> <span class="page"> pp. 241-245. , 5 p. </span> <span class="year">(2022)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1002/bkcs.12457" target="_blank" href="https://doi.org/10.1002/bkcs.12457"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000732662600001" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000732662600001"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85121556566" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85121556566"> Scopus </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:32693883 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;32693883" target="_blank">Synthesis and conformational analysis of an anti-β2,3-amino acid as a building block for unnatural peptide helices</a></div> <div> <span class="journal-title">BULLETIN OF THE KOREAN CHEMICAL SOCIETY</span>
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<div class="lastModified">Utolsó módosítás: 2024.02.27. 14:28 Pécsi Éva (MTMT Közp 3, admin)
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Export Date: 6 March 2024
CODEN: BKCSD
Correspondence Address: Choi, S.H.; Department of Chemistry, South Korea; email: sh-choi@yonsei.ac.kr</pre>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Export Date: 6 March 2024
Correspondence Address: Kato, T.; Osaka Medical and Pharmaceutical University, Japan</pre>
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CSIR-Indian Institute of Chemical Biology (CSIR-IICB), Kolkata, 700032, India
Export Date: 6 March 2024
Correspondence Address: Rai, R.; Natural Products & Medicinal Chemistry Division (NPMC), India; email: raj@iiim.res.in
Correspondence Address: Singh, U.P.; Academy of Scientific and Innovative Research (AcSIR)India; email: umesh.singh@iicb.res.in
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Conformation of Achiral alpha/beta Hybrid Peptides Containing Glycine and 1-Aminocyclohexaneacetic Acid
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The present work describes the conformation of achiral alpha/beta hybrid peptides, Boc-Gly-beta(3,3)-Ac(6)c-NHMe (P1), Boc-Gly-beta(3,3)-Ac(6)c-Gly-OMe (P2), and Boc-Gly-beta(3,3)-Ac(6)c-Gly-beta(3,3)-Ac(6)c-OMe, (P3) using X-ray crystallography. Peptides P1 and P2 adopt C-11 and C-12 folded conformations, respectively. The directionality of the hydrogen bond observed in P1 is opposite to that observed in peptide P2. In case of tetrapeptide P3, no such hydrogen bond is observed. Further, the solvent titration experiment establishes the similar intramolecular hydrogen bonding as observed in the crystals. In P1 and P2, the amino group of beta(3,3)-Ac(6)c occupies equatorial orientations, while in the case of peptide P3, it occupies axial and equatorial orientations for residues beta(3,3)-Ac(6)c(2) and beta(3,3)-Ac(6)c(4), respectively. The average (phi,theta,psi) torsional preferences of beta(3,3)-Ac(6)c in achiral alpha/beta peptides are somewhat different from that of chiral alpha/beta peptides.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Shankar, Sudha </span> <span class="author-type"> </span> ; <span class="author-name" > Jyothi, Deeti </span> <span class="author-type"> </span> ; <span class="author-name" > Rahim, Junaid Ur </span> <span class="author-type"> </span> ; <span class="author-name" > Pal, Purna Chandra </span> <span class="author-type"> </span> ; <span class="author-name" > Singh, Umesh Prasad ✉ </span> <span class="author-type"> </span> ; <span class="author-name" > Rai, Rajkishor ✉ </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;32955370" mtid="32955370" target="_blank">Conformation of Achiral alpha/beta Hybrid Peptides Containing Glycine and 1-Aminocyclohexaneacetic Acid</a></div> <div class="pub-info"> <span class="journal-title">CHEMISTRYSELECT</span> <span class="journal-volume">7</span> : <span class="journal-issue">10</span> <span class="page"> Paper: e202104453 , 6 p. </span> <span class="year">(2022)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1002/slct.202104453" target="_blank" href="https://doi.org/10.1002/slct.202104453"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000771395600033" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000771395600033"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85126858761" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85126858761"> Scopus </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:32955370 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;32955370" target="_blank">Conformation of Achiral alpha/beta Hybrid Peptides Containing Glycine and 1-Aminocyclohexaneacetic Acid</a></div> <div> <span class="journal-title">CHEMISTRYSELECT</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Natural Products & Medicinal Chemistry Division (NPMC), CSIR-Indian Institute of Integrative Medicine (CSIR-IIIM), Jammu, 180001, India
Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, 201002, India
CSIR-Indian Institute of Chemical Biology (CSIR-IICB), Kolkata, 700032, India
Export Date: 6 March 2024 ...</pre>
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Export Date: 6 March 2024
Correspondence Address: Szefczyk, M.; Department of Bioorganic Chemistry, Wybrzeże Wyspiańskiego 27, Poland; email: monika.szefczyk@pwr.edu.pl
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Peptide soft materials belong to an emerging branch of materials sciences due to their growing importance as responsive materials in diagnostics, therapeutics, and biomedical applications. The diversity provided by easily modifiable peptide sequences can be further increased by introducing nonnatural amino acids such as cyclic beta-amino acids, leading to the formation of foldamers. Moreover, it is possible to combine peptide chains with other polymers, aromatic compounds, etc. to create hybrids with completely new properties and applications. In this review, we focus on the cis/trans enantiomers of three cyclic beta-amino acids: 2-aminocyclobutane-1-carboxylic acid (ACBC), 2-aminocyclopentane-1-carboxylic acid (ACPC) and 2-aminocyclohexane-1-carboxylic acid (ACHC). The peptides discussed here either contain exclusively beta-amino acids or are alpha,beta-peptides, and they undergo self-assembly by forming different interactions that lead to the creation of well-defined nanostructures.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Szefczyk, Monika ✉ </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;32234723" mtid="32234723" target="_blank">Peptide foldamer-based self-assembled nanostructures containing cyclic beta-amino acids</a></div> <div class="pub-info"> <span class="journal-title">NANOSCALE</span> <span class="journal-volume">13</span> : <span class="journal-issue">26</span> <span class="page"> pp. 11325-11333. , 9 p. </span> <span class="year">(2021)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1039/d1nr02220b" target="_blank" href="https://doi.org/10.1039/d1nr02220b"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000667790300001" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000667790300001"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85110047315" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85110047315"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="34190303" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=34190303&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:32234723 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Összefoglaló cikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :9
Export Date: 6 March 2024
Correspondence Address: Szefczyk, M.; Department of Bioorganic Chemistry, Wybrzeże Wyspiańskiego 27, Poland; email: monika.szefczyk@pwr.edu.pl</pre>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: CNRS, Immunology, Immunopathology and Therapeutic Chemistry, ISIS, University of Strasbourg, UPR 3572, Strasbourg, 67000, France
Department of Chemistry, University of Copenhagen, Thorvaldsensvej 40, Frederiksberg, 1871, Denmark
Export Date: 6 March 2024
CODEN: EJOCF
Correspondence Address: Jensen, K...</pre>
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The inherent conformational preferences of the neutral beta-peptide foldamer series, Ac-(ACHC)(n)-NHBn, n = 2-4, are studied in the gas phase using conformation-specific IR-UV double resonance methods. The cyclically constrained chiral beta-amino acid cis-2-aminocyclohexane carboxylic acid (ACHC) is designed to bring both right- and left-handed helices into close energetic proximity. Comparison of the infrared spectra in the NH stretch and amide I/II regions with the predictions of DFT calculations lead to the unambiguous assignment of four out of the six observed conformations of the molecules in this series, while corroborating computational and spectral evidence, affords tentative assignments of the remaining two conformers for which IR data were not recorded. The observed structures fall into one of two conformational families: a right-handed 12/10-mixed helix or its "cap-disrupted" left-handed helical analogue, which coexist with significant populations. Site-specific and stereospecific methylation on the cyclohexane backbone at the dipeptide (n = 2) level is also tested as a means to sterically lock in a predetermined cyclohexane chair conformation. These substitutions are proven to be a means of selectively driving formation of one helical screw sense or the other. Calculated relative energies and free energies of all possible structures for the molecules provide strong supporting evidence that the rigid nature of the ACHC residue confers unusual stability to the 12/10-mixed helix conformation, regardless of local environment, temperature, or C-terminal capping unit. The simultaneous presence of both handed helices offers unique opportunities for future studies of their interconversion.
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Department of Chemistry, Purdue University, West Lafayette, IN 47907-2084, United States
Department of Chemistry, Yonsei University, Seoul, 03722, South Korea
Cited By :4
Export Date: 6 March 2024
CODEN: JPCAF</pre>
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;31385379" target="_blank">Structural insight into hybrid peptide ε-helices</a></div> <div> <span class="journal-title">CHEMICAL COMMUNICATIONS</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Department of Chemistry, Indian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pune, 411021, India
NMR Research Center, Indian Institute of Science, Bangalore, 560012, India
Cited By :3
Export Date: 6 March 2024
CODEN: CHCOF
Correspondence Address: Raghotha...</pre>
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Funding text: Momentum programme of the Hungarian Academy of Sciences [LP2016-2]; National Competitiveness and Excellence Program [NVKP 16-1-2016-0007]; BIONANO GINOP-2.3.2-15-2016-00017b. Funding for open access charge: Momentum programme of the Hungarian Academy of Sciences [LP2016-2].
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Nizami, Bilal ✉ </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10067795"> <a href="/gui2/?type=authors&mode=browse&sel=10067795" target="_blank">Bereczki-Szakál, Dorottya</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10065032"> <a href="/gui2/?type=authors&mode=browse&sel=10065032" target="_blank">Varró, Nikolett</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10093721"> <a href="/gui2/?type=authors&mode=browse&sel=10093721" target="_blank">el Battioui, Kamal</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10078635"> <a href="/gui2/?type=authors&mode=browse&sel=10078635" target="_blank">Nagaraj, Vignesh U</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10012939"> <a href="/gui2/?type=authors&mode=browse&sel=10012939" target="_blank">Szigyártó, Imola Cs</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10022837"> <a href="/gui2/?type=authors&mode=browse&sel=10022837" target="_blank">Mándity, István</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10027455"> <a href="/gui2/?type=authors&mode=browse&sel=10027455" target="_blank">Beke-Somfai, Tamás ✉</a> </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;30933404" mtid="30933404" target="_blank">FoldamerDB: a database of peptidic foldamers</a></div> <div class="pub-info"> <span class="journal-title">NUCLEIC ACIDS RESEARCH</span> <span class="journal-volume">48</span> : <span class="journal-issue">D1</span> <span class="page"> pp. D1122-D1128. </span> <span class="year">(2020)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:blue" title="10.1093/nar/gkz993" target="_blank" href="https://doi.org/10.1093/nar/gkz993"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000525956700143" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000525956700143"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85077664234" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85077664234"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="31686102" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=31686102&dopt=Abstract"> PubMed </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:black" title="https://academic.oup.com/nar/advance-article/doi/10.1093/nar/gkz993/5612547" target="_blank" href="https://academic.oup.com/nar/advance-article/doi/10.1093/nar/gkz993/5612547"> Egyéb URL </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:30933404 </span> <span class="status-holder"><span class="status-data status-ADMIN_APPROVED"> Admin láttamozott </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 10</span> | Független: 7 | Függő: 3 | Nem jelölt: 0 | WoS jelölt: 10 | Scopus jelölt: 8 | WoS/Scopus jelölt: 10 | DOI jelölt: 9 </div> </div> </div> </div><div class="JournalArticle Publication long-list">
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<img title="Forrásközlemény" style="float: left" src="/frontend/resources/grid/publication-core-icon.png">
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<div class="autype autype0"> <span class="author-name" >Nizami Bilal ✉
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<span class="author-name" mtid="10067795"><a
href="/gui2/?type=authors&mode=browse&sel=10067795" target="_blank">Bereczki-Szakál Dorottya
(<span class="authorship-author-name">Bereczki-Szakál Dorottya</span>
<span class="authorAux-mtmt"> Mesterséges transzporterek kutatócsoport</span>)
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</span>
<span class="author-affil">MTA Természettudományi Kutatóközpont; <span title="Természettudományi Kutatóközpont">TTK</span>/<span title="Anyag- és Környezetkémiai Intézet">AKI</span>/Mesterséges Transzporterek Kutatócsoport</span>
;
<span class="author-name" mtid="10065032"><a
href="/gui2/?type=authors&mode=browse&sel=10065032" target="_blank">Varró Nikolett
(<span class="authorship-author-name">Varró Nikolett</span>
<span class="authorAux-mtmt"> Mesterséges transzporterek, szerves kémia</span>)
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<span class="author-affil"><span title="Természettudományi Kutatóközpont">TTK</span>/<span title="Anyag- és Környezetkémiai Intézet">AKI</span>/Mesterséges Transzporterek Kutatócsoport</span>
;
<span class="author-name" mtid="10093721"><a
href="/gui2/?type=authors&mode=browse&sel=10093721" target="_blank">el Battioui Kamal
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<span class="authorAux-mtmt"> Chemistry</span>)
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<span class="author-affil"><span title="Természettudományi Kutatóközpont">TTK</span>/<span title="Anyag- és Környezetkémiai Intézet">AKI</span>/Biomolekuláris Önrendeződés</span>
;
<span class="author-name" mtid="10078635"><a
href="/gui2/?type=authors&mode=browse&sel=10078635" target="_blank">Nagaraj Vignesh U
(<span class="authorship-author-name">Udyavara Nagaraj Vignesh</span>
<span class="authorAux-mtmt"> Peptide chemistry</span>)
</a>
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<span class="author-affil"><span title="Természettudományi Kutatóközpont">TTK</span>/<span title="Anyag- és Környezetkémiai Intézet">AKI</span>/Biomolekuláris Önrendeződés</span>
;
<span class="author-name" mtid="10012939"><a
href="/gui2/?type=authors&mode=browse&sel=10012939" target="_blank">Szigyártó Imola Cs
(<span class="authorship-author-name">Szigyártó Imola Csilla</span>
<span class="authorAux-mtmt"> Bioszervetlen kémia</span>)
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<span class="author-affil"><span title="Természettudományi Kutatóközpont">TTK</span>/Anyag- és Környezetkémiai Intézet; <span title="Természettudományi Kutatóközpont">TTK</span>/<span title="Anyag- és Környezetkémiai Intézet">AKI</span>/Biomolekuláris Önrendeződés</span>
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<span class="authorAux-mtmt"> Gyógyszerkémia, gyógyszerkutatás</span>)
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<span class="author-affil"><span title="Természettudományi Kutatóközpont">TTK</span>/<span title="Anyag- és Környezetkémiai Intézet">AKI</span>/Mesterséges Transzporterek Kutatócsoport</span>
;
<span class="author-name" mtid="10027455"><a
href="/gui2/?type=authors&mode=browse&sel=10027455" target="_blank">Beke-Somfai Tamás ✉
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<span class="author-affil"><span title="Természettudományi Kutatóközpont">TTK</span>/Anyag- és Környezetkémiai Intézet; <span title="Természettudományi Kutatóközpont">TTK</span>/<span title="Anyag- és Környezetkémiai Intézet">AKI</span>/Biomolekuláris Önrendeződés</span>
</div>
</div>
<div class="title"><a href="/gui2/?mode=browse¶ms=publication;30933404" target="_blank">FoldamerDB: a database of peptidic foldamers</a></div> <div> <span class="journal-title">NUCLEIC ACIDS RESEARCH</span>
<span class="journal-issn">(<a target="_blank" href="https://portal.issn.org/resource/ISSN/0305-1048">0305-1048</a> <a target="_blank" href="https://portal.issn.org/resource/ISSN/1362-4962">1362-4962</a>)</span>:
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Funding Agency and Grant Number: Momentum programme of the Hungarian Academy of Sciences [LP2016-2]; National Competitiveness and Excellence Program [NVKP 16-1-2016-0007]; BIONANO [GINOP-2.3.2-15-2016-00017b]
Funding text: Momentum programme of the Hungarian Academy of Sciences [LP2016-2]; National Competitiveness and Excellence Program [NVKP 16-1-2016-0007]; BIONANO GINOP-2.3.2-15-...</pre>
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The Diverse World of Foldamers: Endless Possibilities of Self-Assembly
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Different classes of foldamers, which are synthetic oligomers that adopt well-defined conformations in solution, have been the subject of extensive studies devoted to the elucidation of the forces driving their secondary structures and their potential as bioactive molecules. Regardless of the backbone type (peptidic or abiotic), the most important features of foldamers are the high stability, easy predictability and tunability of their folding, as well as the possibility to endow them with enhanced biological functions, with respect to their natural counterparts, by the correct choice of monomers. Foldamers have also recently started playing a starring role in the self-assembly of higher-order structures. In this review, selected articles will be analyzed to show the striking number of self-assemblies obtained for foldamers with different backbones, which will be analyzed in order of increasing complexity. Starting from the simplest self-associations in solution (e.g., dimers of beta-strands or helices, bundles, interpenetrating double and multiple helices), the formation of monolayers, vesicles, fibers, and eventually nanostructured solid tridimensional morphologies will be subsequently described. The experimental techniques used in the structural investigation, and in the determination of the driving forces and mechanisms underlying the self-assemblies, will be systematically reported. Where applicable, examples of biomimetic self-assembled foldamers and their interactions with biological components will be described.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Rinaldi, Samuele ✉ </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;31417953" mtid="31417953" target="_blank">The Diverse World of Foldamers: Endless Possibilities of Self-Assembly</a></div> <div class="pub-info"> <span class="journal-title">MOLECULES</span> <span class="journal-volume">25</span> : <span class="journal-issue">14</span> <span class="page"> Paper: 3276 , 67 p. </span> <span class="year">(2020)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.3390/molecules25143276" target="_blank" href="https://doi.org/10.3390/molecules25143276"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000556785000001" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000556785000001"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85088682725" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85088682725"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="32708440" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=32708440&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:31417953 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Összefoglaló cikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;31417953" target="_blank">The Diverse World of Foldamers: Endless Possibilities of Self-Assembly</a></div> <div> <span class="journal-title">MOLECULES</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :34
Export Date: 6 March 2024
CODEN: MOLEF
Correspondence Address: Rinaldi, S.; Department of Life and Environmental Sciences, Via Brecce Bianche, Italy; email: s.rinaldi@staff.univpm.it</pre>
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Medicinal Chemistry Division, CSIR-Indian Institute of Integrative Medicine, Canal Road, Jammu, 180001, India
Academy of Scientific and Innovative Research, (AcSIR), Ghaziabad, 201002, India
Cited By :6
Export Date: 6 March 2024
CODEN: CPPSC
Correspondence Address: Rai, R.; Medicinal Chemistry Division, Canal Road, India; email: raj@iiim.ac.in
Correspondence Address: Rai, R.; Academy of Scientific and Innovative Research, India; email: raj@iiim.ac.in
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The peptides containing beta-and gamma-amino acids as building blocks display well-defined secondary structures with unique morphologies. The ability of such peptides to self-assemble into complex structures of controlled geometries has been exploited in biomedical applications. Herein, we have provided an updated overview about the peptides containing beta-and gamma-amino acids considering the significance and advancement in the area of development of peptide-based biomaterials having diverse applications.
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Medicinal Chemistry Division, CSIR-Indian Institute of Integrative Medicine, Canal Road, Jammu, 180001, India
Academy of Scientific and Innovative Research, (AcSIR), Ghaziabad, 201002, India
Cited By :6
Export Date: 6 March 2024
CODEN: CPPSC
Correspondence Address: Rai, R.; Me...</pre>
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The self-assembly of short peptide building blocks into well-ordered nanostructures is a key direction in bionanotechnology. The formation of beta-sheet organizations by short peptides is well explored, leading to the development of a wide range of functional assemblies. Likewise, many natural proteinaceous materials, such as silk and amyloid fibrils, are based on beta-sheet structures. In contrast, collagen, the most abundant protein in mammals, is based on helical arrangement. Similar to 3-sheet structures, short helical peptides have been recently discovered to possess a diverse set of funetionalities with the potential to fabricate artificial self-assembling materials. Here, we outline the functional roles of self-assembled nanostructures fonned by short helical peptides and their potential as artificial materials. We focus on the association between self-assembled mesoscale structures and their material function and demonstrate the way by which this class of building blocks hears the potential for diverse applications, such as the ftiture fabrication of smart devices.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Bera, Santu </span> <span class="author-type"> </span> ; <span class="author-name" > Gazit, Ehud ✉ </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;30956747" mtid="30956747" target="_blank">Self-assembly of Functional Nanostructures by Short Helical Peptide Building Block</a></div> <div class="pub-info"> <span class="journal-title">PROTEIN AND PEPTIDE LETTERS</span> <span class="journal-volume">26</span> : <span class="journal-issue">2</span> <span class="page"> pp. 88-97. , 10 p. </span> <span class="year">(2019)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.2174/0929866525666180917163142" target="_blank" href="https://doi.org/10.2174/0929866525666180917163142"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000459133100003" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000459133100003"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85062413713" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85062413713"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="30227810" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=30227810&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:30956747 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Összefoglaló cikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;30956747" target="_blank">Self-assembly of Functional Nanostructures by Short Helical Peptide Building Block</a></div> <div> <span class="journal-title">PROTEIN AND PEPTIDE LETTERS</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :22
Export Date: 6 March 2024
CODEN: PPELE
Correspondence Address: Gazit, E.; Department of Molecular Microbiology and Biotechnology, Israel; email: ehudg@post.tau.ac.il</pre>
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A series of oligo(ethynylpyridine)-containing alkynylplatinum(II) terpyridine/bzimpy (bzimpy = 2,6-bis(N-alkylbenzimidazol-2'-yl)pyridine) metallofoldamers has been designed and synthesized to investigate the potential applications of metallofoldamers imparted by the rich spectroscopic responses of Pt center dot center dot center dot Pt interactions. Apart from the control of the folding/unfolding processes by solvent compositions and temperatures, this class of metallofoldamers has also been found to exhibit reversible folding/unfolding behaviors mediated by the addition of acids/bases due to the incorporation of the acid-sensitive oligo(ethynylpyridine) derivatives. More importantly, the intramolecular Pt center dot center dot center dot Pt interaction has been found to play a crucial role in governing the folded state conformation. The conformation of this class of metallofoldamers has been investigated by 2D ROESY NMR, electronic absorption, and emission spectroscopy, which provide further insights into the rational molecular design and multidimensional control of metallofoldamers upon the application of various external stimuli, leading to the preparation of multi-stimuli-responsive materials for potential applications in material sciences.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Chan, Michael Ho-Yeung </span> <span class="author-type"> </span> ; <span class="author-name" > Leung, Sammual Yu-Lut </span> <span class="author-type"> </span> ; <span class="author-name" > Yam, Vivian Wing-Wah ✉ </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;30961080" mtid="30961080" target="_blank">Rational Design of Multi-Stimuli-Responsive Scaffolds: Synthesis of Luminescent Oligo(ethynylpyridine)-Containing Alkynylplatinum(II) Polypyridine Foldamers Stabilized by Pt···Pt Interactions</a></div> <div class="pub-info"> <span class="journal-title">JOURNAL OF THE AMERICAN CHEMICAL SOCIETY</span> <span class="journal-volume">141</span> : <span class="journal-issue">31</span> <span class="page"> pp. 12312-12321. , 10 p. </span> <span class="year">(2019)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1021/jacs.9b04447" target="_blank" href="https://doi.org/10.1021/jacs.9b04447"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000480497100023" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000480497100023"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85070536686" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85070536686"> Scopus </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:30961080 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div class="autype autype0"> <span class="author-name" >Chan Michael Ho-Yeung
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;30961080" target="_blank">Rational Design of Multi-Stimuli-Responsive Scaffolds: Synthesis of Luminescent Oligo(ethynylpyridine)-Containing Alkynylplatinum(II) Polypyridine Foldamers Stabilized by Pt···Pt Interactions</a></div> <div> <span class="journal-title">JOURNAL OF THE AMERICAN CHEMICAL SOCIETY</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :47
Export Date: 6 March 2024
CODEN: JACSA
Correspondence Address: Yam, V.W.-W.; Inst. of Molec. Funct. Materials (Areas of Excellence Scheme University Grants Committee (Hong Kong), Pokfulam Road, Hong Kong; email: wwyam@hku.hk</pre>
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Funding Agency and Grant Number: Hungarian Research Foundation (OTKA) [K 115731]; Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences; Bolyai + New National Excellence Program of the Ministry of Human Capacities [UNKP-18-4-SE-121]; [GINOP-2.3.2-15-2016-00014]; [GINOP-2.3.2-15-2016-00034]
Funding text: We are grateful to the Hungarian Research Foundation (OTKA No. K 115731). The financial support of the GINOP-2.3.2-15-2016-00014 and GINOP-2.3.2-15-2016-00034 projects are acknowledged. This work was partially supported by the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences and by the Bolyai + New National Excellence Program (grant number: UNKP-18-4-SE-121) of the Ministry of Human Capacities (S. Beni).
Funding Agency and Grant Number: Hungarian Research Foundation (OTKA)Orszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [K 115731]; Janos Bolyai Research Scholarship of the Hungarian Academy of SciencesHungarian Academy of Sciences; Bolyai + New National Excellence Program of the Ministry of Human Capacities [UNKP-18-4-SE-121]; [GINOP-2.3.2-15-2016-00014]; [GINOP-2.3.2-15-2016-00034]
Funding text: We are grateful to the Hungarian Research Foundation (OTKA No. K 115731). The financial support of the GINOP-2.3.2-15-2016-00014 and GINOP-2.3.2-15-2016-00034 projects are acknowledged. This work was partially supported by the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences and by the Bolyai + New National Excellence Program (grant number: UNKP-18-4-SE-121) of the Ministry of Human Capacities (S. Beni).
Institute of Pharmaceutical Chemistry, University of Szeged, Eötvös u. 7., Szeged, H-6720, Hungary
Department of Organic Chemistry, Faculty of Pharmacy, Semmelweis University Hgyes, Endre u. 7., Budapest, H-1092, Hungary
Servier Research Institute of Medicinal Chemistry (SRIMC), Záhony utca 7., Budapest, H-1031, Hungary
Department of Pharmacognosy, Faculty of Pharmacy, Semmelweis University, Ülli út 26., Budapest, H-1085, Hungary
Institute of Materials and Environmental Chemistry, Research Center for Natural Sciences, Hungarian Academy of Sciences Magyar, Tudósok krt. 2., Budapest, H-1117, Hungary
Department of Medical Chemistry, University of Szeged, Dóm t. 8., Szeged, H-6720, Hungary
MTA SZTE Biomimetic Systems Research Group, Dóm t. 8., Szeged, H-6720, Hungary
MTA TTK Lendület Artificial Transporter Research Group, Institute of Materials and Environmental Chemistry, Research Center for Natural Sciences, Hungarian Academy of Sciences Magyar, Tudósok krt. 2., Budapest, H-1117, Hungary
Cited By :4
Export Date: 25 July 2020
CODEN: CHCOF
Correspondence Address: Fülöp, F.; Institute of Pharmaceutical Chemistry, University of Szeged, Eötvös u. 7., Hungary; email: fulop@pharm.u-szeged.hu
CAplus AN 2019:196581; MEDLINE PMID: 30720807 (Journal; Article);
Institute of Pharmaceutical Chemistry, University of Szeged, Eötvös u. 7., Szeged, H-6720, Hungary
Department of Organic Chemistry, Faculty of Pharmacy, Semmelweis University Hgyes, Endre u. 7., Budapest, H-1092, Hungary
Servier Research Institute of Medicinal Chemistry (SRIMC), Záhony utca 7., Budapest, H-1031, Hungary
Department of Pharmacognosy, Faculty of Pharmacy, Semmelweis University, Ülli út 26., Budapest, H-1085, Hungary
Institute of Materials and Environmental Chemistry, Research Center for Natural Sciences, Hungarian Academy of Sciences Magyar, Tudósok krt. 2., Budapest, H-1117, Hungary
Department of Medical Chemistry, University of Szeged, Dóm t. 8., Szeged, H-6720, Hungary
MTA SZTE Biomimetic Systems Research Group, Dóm t. 8., Szeged, H-6720, Hungary
MTA TTK Lendület Artificial Transporter Research Group, Institute of Materials and Environmental Chemistry, Research Center for Natural Sciences, Hungarian Academy of Sciences Magyar, Tudósok krt. 2., Budapest, H-1117, Hungary
Cited By :7
Export Date: 11 July 2021
CODEN: CHCOF
Correspondence Address: Fülöp, F.; Institute of Pharmaceutical Chemistry, Eötvös u. 7., Hungary; email: fulop@pharm.u-szeged.hu
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<span class="author-affil">Servier Gyógyászati Vegytani Kutatóintézet Zártkörűen Működő Részvénytársaság</span>
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;30535263" target="_blank">Flow-chemistry enabled efficient synthesis of β-peptides: backbone topology vs. helix formation</a></div> <div> <span class="journal-title">CHEMICAL COMMUNICATIONS</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Funding Agency and Grant Number: Hungarian Research Foundation (OTKA) [K 115731]; Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences; Bolyai + New National Excellence Program of the Ministry of Human Capacities [UNKP-18-4-SE-121]; [GINOP-2.3.2-15-2016-00014]; [GINOP-2.3.2-15-2016-00034]
Funding text: We are grateful to the Hungarian Research Foundation (OTKA No...</pre>
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Design of Helical Peptide Foldamers through alpha,beta -> beta,gamma Double-Bond Migration
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The direct transformation of nonhelical alpha,gamma-hybrid peptides composed of alternating alpha- and E-vinylogous amino acids into 12-helical structures through a base-mediated alpha,beta -> beta,gamma double-bond migration is reported. The conformations of double-bond-migrated new 12-helices were studied in single crystals and in solution. Instructively, the 12-helices reported here were found to be acid labile, and they completely break down into the corresponding amino acid derivatives upon treatment with acids.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Veeresh, Kuruva </span> <span class="author-type"> </span> ; <span class="author-name" > Gopi, Hosahudya N. ✉ </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;30961081" mtid="30961081" target="_blank">Design of Helical Peptide Foldamers through alpha,beta -> beta,gamma Double-Bond Migration</a></div> <div class="pub-info"> <span class="journal-title">ORGANIC LETTERS</span> <span class="journal-volume">21</span> : <span class="journal-issue">12</span> <span class="page"> pp. 4500-4504. , 5 p. </span> <span class="year">(2019)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1021/acs.orglett.9b01365" target="_blank" href="https://doi.org/10.1021/acs.orglett.9b01365"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000473116000022" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000473116000022"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85067686550" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85067686550"> Scopus </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:30961081 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;30961081" target="_blank">Design of Helical Peptide Foldamers through alpha,beta -> beta,gamma Double-Bond Migration</a></div> <div> <span class="journal-title">ORGANIC LETTERS</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :9
Export Date: 6 March 2024
CODEN: ORLEF
Correspondence Address: Gopi, H.N.; Department of Chemistry, Dr. Homi Bhabha Road, India; email: hn.gopi@iiserpune.ac.in</pre>
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N1 Funding details: Bose Centre for Advanced Study and Research in Natural Sciences, University of Dhaka
N1 Funding details: BME, Budapesti Műszaki és Gazdaságtudományi Egyetem
N1 Funding details: MTA, Magyar Tudományos Akadémia
N1 Funding details: EGU, European Geosciences Union
N1 Funding details: VEKOP-2.3.2-16-2017-00014, ERDF, European Regional Development Fund
N1 Funding details: VEKOP-2.3.3-15-2017-00018, ERDF, European Regional Development Fund
Funding Agency and Grant Number: European UnionEuropean Commission; State of Hungary; European Regional Development FundEuropean Commission [VEKOP-2.3.2-16-2017-00014, VEKOP-2.3.3-15-2017-00018]; MedInProt Grant Facilitating Access to Instruments from the Hungarian Academy of Sciences
Funding text: These research projects were supported by the European Union and the State of Hungary, and co-financed by the European Regional Development Fund (VEKOP-2.3.2-16-2017-00014 and VEKOP-2.3.3-15-2017-00018). This work was supported by a MedInProt Grant Facilitating Access to Instruments from the Hungarian Academy of Sciences. The authors gratefully acknowledge Gabor Gyorke for his contribution to the preparative work. The authors express their gratitude to agnes Gomory at the Hungarian Academy of Sciences, Research Centre for Natural Sciences, and to and Anita Kapros for carrying out the MS measurements. The authors wish to thank ThalesNano Inc. (Budapest, Hungary) for the H-Cube (R) equipment. The Biostruct Laboratory at the Budapest University of Technology and Economics is acknowledged for collecting X-ray diffraction data. The authors thank Ibolya Leveles for her assistance in X-ray diffraction data collection.
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Approaches to Pyranuronic β-Sugar Amino Acid Building Blocks of Peptidosaccharide Foldamers
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Pyranuronic -sugar amino acids (-SAAs) are biocompatible and tuneable building blocks of foldamers and chimera-peptides. The scalable and economical total synthesis of two building blocks is described here. These C-4 epimers, Fmoc-GlcAPU(Me)-OH (7) and Fmoc-GalAPU(Me)-OH (8), which are suitable for solid phase peptide synthesis, were prepared via a common oxime intermediate 16. The new synthesis uses nine consecutive steps, starting from methyl -d-glucopyranoside (6). The synthesis is fine-tuned, optimized, and ready for large-scale and cost-efficient production.
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Megjegyzés-27132825
N1 Funding details: Bose Centre for Advanced Study and Research in Natural Sciences, University of Dhaka
N1 Funding details: BME, Budapesti Műszaki és Gazdaságtudományi Egyetem
N1 Funding details: MTA, Magyar Tudományos Akadémia
N1 Funding details: EGU, European Geosciences Union
N1 Funding details: VEKOP-2.3.2-16-2017-00014, ERDF, European Regional Development Fund
N1 Fundi...</pre>
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Institut des Biomolécules Max Mousseron (IBMM) UMR 5247, CNRS-Université Montpellier-ENSCM, Montpellier cedex 5, 34093, France
CRM2, UMR 7063 CNRS Université de Lorraine, Boulevard des Aiguilletes, Vandoeuvre-lès-Nancy Cedex, 54506, France
Cited By :1
Export Date: 6 March 2024
CODEN: CEUJE
Correspondence Address: Legrand, B.; Institut des Biomolécules Max Mousseron (IBMM) UMR 5247, France; email: baptiste.legrand@umontpellier.fr
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12/10-Helices constitute suitable templates that can be used to design original structures. Nevertheless, they often suffer from a weak stability in polar solvents because they exhibit a mixed hydrogen-bond network resulting in a small macrodipole. In this work, stable and functionalizable 12/10-helices were developed by alternating a highly constrained beta(2, 3, 3)-trisubstituted bicyclic amino acid (S)-1-aminobicyclo[2.2.2]octane-2-carboxylic acid ((S)-ABOC) and an acyclic substituted beta-homologated proteinogenic amino acid (l-beta(3)-hAA). Based on NMR spectroscopic analysis, it was shown that such mixed beta-peptides display well-defined right-handed 12/10-helices in polar, apolar, and chaotropic solvents; that are, CD3OH, CDCl3, and [D-6]DMSO, respectively. The stability of the hydrogen bonds forming the C-10 and C-12 pseudocycles as well as the benefit provided by the use of the constrained bicyclic ABOC versus typical acyclic beta-amino acids sequences when designing 12/10-helix were investigated using NH/ND NMR exchange experiments and DFT calculations in various solvents. These studies showed that the beta(3)-hAA/(S)-ABOC helix displayed a more stable hydrogen-bond network through specific stabilization of the C-10 pseudocycles involving the bridgehead NH of the ABOC bicyclic scaffold.
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Institut des Biomolécules Max Mousseron (IBMM) UMR 5247, CNRS-Université Montpellier-ENSCM, Montpellier cedex 5, 34093, France
CRM2, UMR 7063 CNRS Université de Lorraine, Boulevard des Aiguilletes, Vandoeuvre-lès-Nancy Cedex, 54506, France
Cited By :1
Export Date: 6 March 2024
CODEN: CEUJE ...</pre>
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Ikerbasque, Basque Foundation for Science, Maria Diaz de Haro 13, Bilbao, 48009, Spain
Department of Organic Chemistry II, Faculty of Science & Technology, University of the Basque Country, Leioa, 48940, Spain
Combinatorial Chemistry Unit, Barcelona Science Park, Baldiri Reixac 10, Barcelona, 08028, Spain
Biomedical Research Networking Center in Bioengineering, Biomaterials and Nanomedicine (CIBER-BBN), Barcelona Science Park, Baldiri Reixac 10, Barcelona, 08028, Spain
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Centro Singular de Investigación en Química Biolóxica e Materiais Moleculares (CiQUS), Departamento de Química Orgánica, Universidade de Santiago de Compostela, Santiago de Compostela, 15782, Spain
Molecular Recognition & Host-Pathogen Interactions Unit, CIC bioGUNE, Bizkaia Technology Park, Building 801A, Derio, 48170, Spain
Ikerbasque, Basque Fo...</pre>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :80
Export Date: 6 March 2024
CODEN: JACSA
Correspondence Address: Yam, V.W.-W.; Institute of Molecular Functional Materials, Pokfulam Road, Hong Kong; email: wwyam@hku.hk</pre>
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Del Borgo, Mark P </span> <span class="author-type"> </span> ; <span class="author-name" > Kulkarni, Ketav </span> <span class="author-type"> </span> ; <span class="author-name" > Aguilar, Marie-Isabel </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;26581834" mtid="26581834" target="_blank">Unique Functional Materials Derived from beta-Amino Acid Oligomers</a></div> <div class="pub-info"> <span class="journal-title">AUSTRALIAN JOURNAL OF CHEMISTRY</span> <span class="journal-volume">70</span> : <span class="journal-issue">2</span> <span class="page"> pp. 126-129. , 4 p. </span> <span class="year">(2017)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1071/CH16511" target="_blank" href="https://doi.org/10.1071/CH16511"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000395050500002" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000395050500002"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85010382727" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85010382727"> Scopus </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:26581834 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :6
Export Date: 6 March 2024
CODEN: AJCHA
Correspondence Address: Del Borgo, M.P.; Department of Biochemistry and Molecular Biology, Australia; email: Mark.Delborgo@monash.edu</pre>
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Department of Chemistry, Indian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pashan, Pune, 411 008, India
Department of Physical Chemistry, School of Chemistry, Madurai Kamaraj University, Madurai, 625 021, India
Institute of Biochemistry, Faculty of Biosciences, Pharmacy and Psychology, Brüderstrasse 34, Leipzig, 04103, Germany
Cited By :7
Export Date: 6 March 2024
CODEN: CEUJE
Correspondence Address: Hofmann, H.-J.; Institute of Biochemistry, Brüderstrasse 34, Germany; email: hofmann@uni-leipzig.de
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;27100837" target="_blank">Modulating the Structural Properties of alpha,gamma-Hybrid Peptides by alpha-Amino Acid Residues: Uniform 12-Helix Versus "Mixed" 12/10-Helix</a></div> <div> <span class="journal-title">CHEMISTRY-A EUROPEAN JOURNAL</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Department of Chemistry, Indian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pashan, Pune, 411 008, India
Department of Physical Chemistry, School of Chemistry, Madurai Kamaraj University, Madurai, 625 021, India
Institute of Biochemistry, Faculty of Biosciences, Pharmacy and Psychology, Brüderstrasse 34, Leipzig, 04103, Germ...</pre>
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Institute of Biochemistry, Faculty of Biosciences, University of Leipzig, Brüderstrasse 34, Leipzig, D-04103, Germany
Cited By :11
Export Date: 6 March 2024
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Thodupunuri, Prashanth </span> <span class="author-type"> </span> ; <span class="author-name" > Katukuri, Sirisha </span> <span class="author-type"> </span> ; <span class="author-name" > Ramakrishna, Kallaganti V S </span> <span class="author-type"> </span> ; <span class="author-name" > Sharma, Gangavaram V M </span> <span class="author-type"> </span> ; <span class="author-name" > Kunwar, Ajit C </span> <span class="author-type"> </span> ; <span class="author-name" > Sarma, Akella V S </span> <span class="author-type"> </span> ; <span class="author-name" > Hofmann, Hans-Joerg </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;26581886" mtid="26581886" target="_blank">Solvent-Directed Switch of a Left-Handed 10/12-Helix into a Right-Handed 12/10-Helix in Mixed β-Peptides</a></div> <div class="pub-info"> <span class="journal-title">JOURNAL OF ORGANIC CHEMISTRY</span> <span class="journal-volume">82</span> : <span class="journal-issue">4</span> <span class="page"> pp. 2018-2031. , 14 p. </span> <span class="year">(2017)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1021/acs.joc.6b02856" target="_blank" href="https://doi.org/10.1021/acs.joc.6b02856"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000394736000019" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000394736000019"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85013194996" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85013194996"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="28094944" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=28094944&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:26581886 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Organic and Biomolecular Chemistry Division, CSIR-Indian Institute of Chemical Technology, Hyderabad, 500 007, India
Nuclear Magnetic Resonance and Structural Chemistry Division, CSIR-Indian Institute of Chemical Technology, Hyderabad, 500 007, India
Institute of Biochemistry, Faculty of Biosciences, University of Leipzig, Brüderstrasse 34, Leipzi...</pre>
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Department of Biomedical Engineering, Boston University, Boston, MA 02215, United States
Division of Materials Science and Engineering, Boston University, Brookline, MA 02446, United States
Department of Physiology and Biophysics, Boston University, School of Medicine, Boston, MA 02118, United States
Department of Medicine, Boston University, School of Medicine, Boston, MA 02118, United States
Cited By :26
Export Date: 6 March 2024
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Department of Chemistry, Boston University, Boston, MA 02215, United States
Department of Biomedical Engineering, Boston University, Boston, MA 02215, United States
Division of Materials Science and Engineering, Boston University, Brookline, MA 02446, United States
Department of Physiology and Biophysics, Boston University,...</pre>
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;26035014" target="_blank">alpha-Helical Structures of Oligopeptides with an Alternating L-Leu-Aib Segment</a></div> <div> <span class="journal-title">EUROPEAN JOURNAL OF ORGANIC CHEMISTRY</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: National Institute of Health Sciences, Setagaya, Tokyo, 158-8501, Japan
Osaka University of Pharmaceutical Sciences, Osaka, 569-1094, Japan
Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, 852-8521, Japan
Cited By :9
Export Date: 6 March 2024
CODEN: EJOCF...</pre>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :41
Export Date: 6 March 2024
CODEN: TELEA
Correspondence Address: Pellegrino, S.; Dipartimento di Scienze Farmaceutiche, Via Venezian 21, Italy; email: sara.pellegrino@unimi.it</pre>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cardiovascular and Metabolic Diseases, Innovative Medicines and Early Development Biotech Unit, AstraZeneca, Pepparedsleden 1, Mölndal, 431 83, Sweden
AstraZeneca MPI Satellite Unit, Department of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, 44202, Germany
Cited By :115
Export Date: 6 March 2024...</pre>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Organic and Bimolecular Chemistry Division, Hyderabad500007, India
NMR and SC Division, CSIR, Indian Institute of Chemical Technology, Hyderabad, 500007, India
Cited By :2
Export Date: 6 March 2024
CODEN: EJOCF
Correspondence Address: Sharma, G.V.M.; Organic and Bimolecular Ch...</pre>
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Cited By :28
Export Date: 6 March 2024
CODEN: JACSA
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Department of Chemistry, Yonsei University, Seoul, 03722, South Korea
Department of Chemistry, University of Wisconsin, Madison, WN 53706, United States
Department of Chemistry, Chungbuk National University, Chungbuk, 28644, South Korea
Cited By :28
Export Date: 6 March 2024
C...</pre>
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School of Chemistry, Monash University, Clayton, VIC 3800, Australia
School of Biological and Chemical Sciences, University of the South PacificSuva, Fiji
Cited By :60
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Gopalan, Romila D </span> <span class="author-type"> </span> ; <span class="author-name" > Del Borgo, Mark P </span> <span class="author-type"> </span> ; <span class="author-name" > Mechler, Adam I </span> <span class="author-type"> </span> ; <span class="author-name" > Perlmutter, Patrick </span> <span class="author-type"> </span> ; <span class="author-name" > Aguilar, Marie-Isabel </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;25371239" mtid="25371239" target="_blank">Geometrically Precise Building Blocks: the Self-Assembly of beta-Peptides</a></div> <div class="pub-info"> <span class="journal-title">CHEMISTRY & BIOLOGY</span> <span class="journal-volume">22</span> : <span class="journal-issue">11</span> <span class="page"> pp. 1417-1423. , 7 p. </span> <span class="year">(2015)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1016/j.chembiol.2015.10.005" target="_blank" href="https://doi.org/10.1016/j.chembiol.2015.10.005"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000366141800002" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000366141800002"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84947901399" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84947901399"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="26584778" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=26584778&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:25371239 </span> <span class="status-holder"><span class="status-data status-ADMIN_APPROVED"> Admin láttamozott </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Összefoglaló cikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;25371239" target="_blank">Geometrically Precise Building Blocks: the Self-Assembly of beta-Peptides</a></div> <div> <span class="journal-title">CHEMISTRY & BIOLOGY</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Department of Biochemistry and Molecular Biology, Monash University, Wellington Road, Clayton, VIC 3800, Australia
Department of Chemistry, School of Molecular Science, La Trobe University, Bundoora, VIC 3083, Australia
School of Chemistry, Monash University, Clayton, VIC 3800, Australia
School of Biological and Chemical Sc...</pre>
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Conformational properties of 1,4- and 1,5-substituted 1,2,3-triazole amino acids-building units for peptidic foldamers
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Peptidic foldamers have recently emerged as a novel class of artificial oligomers with properties and structural diversity similar to that of natural peptides, but possessing additional interesting features granting them great potential for applications in fields from nanotechnology to pharmaceuticals. Among these, foldamers containing 1,4- and 1,5-substitued triazole amino acids are easily prepared via the Cu- and Ru-catalyzed click reactions and may offer increased side chain variation, but their structural capabilities have not yet been widely explored. We here describe a systematic analysis of the conformational space of the two most important basic units, the 1,4-substitued (4Tzl) and the 1,5-substitued (5Tzl) 1,2,3-triazole amino acids, using quantum chemical calculations and NMR spectroscopy. Possible conformations of the two triazoles were scanned and their potential minima were located using several theoretical approaches (B3LYP/6-311++G(2d,2p), ωB97X-D/6-311++G(2d,2p), M06-2X/6-311++G(2d,2p) and MP2/6-311++G(2d,2p)) in different solvents. BOC-protected versions of 4Tzl and 5Tzl were also prepared via one step transformations and analyzed by 2D NOESY NMR. Theoretical results show 9 conformers for 5Tzl derivatives with relative energies lying close to each other, which may lead to a great structural diversity. NMR analysis also indicates that conformers preferring turn, helix and zig-zag secondary structures may coexist in solution. In contrast, 4Tzl has a much lower number of conformers, only 4, and these lack strong intraresidual interactions. This is again supported by NMR suggesting the presence of both extended and bent conformers. The structural information provided on these building units could be employed in future design of triazole foldamers. This journal is © The Royal Society of Chemistry 2015.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Kann, N </span> <span class="author-type"> </span> ; <span class="author-name" > Johansson, JR </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10027455"> <a href="/gui2/?type=authors&mode=browse&sel=10027455" target="_blank">Beke-Somfai, T ✉</a> </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;3016896" mtid="3016896" target="_blank">Conformational properties of 1,4- and 1,5-substituted 1,2,3-triazole amino acids-building units for peptidic foldamers</a></div> <div class="pub-info"> <span class="journal-title">ORGANIC & BIOMOLECULAR CHEMISTRY</span> <span class="journal-volume">13</span> : <span class="journal-issue">9</span> <span class="page"> pp. 2776-2785. , 10 p. </span> <span class="year">(2015)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:blue" title="10.1039/c4ob02359e" target="_blank" href="https://doi.org/10.1039/c4ob02359e"> DOI </a> </span> <span class="id identifier oa_NONE" title=" Nincs "> <span class="isbnOrIssn"> ISSN: </span> <a style="color:blue" title="1477-0539" target="_blank" href="https://portal.issn.org/resource/ISSN/1477-0539"> 1477-0539 </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000350144600037" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000350144600037"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84923366190" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84923366190"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="25605623" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=25605623&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:3016896 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 18</span> | Független: 15 | Függő: 3 | Nem jelölt: 0 | WoS jelölt: 17 | Scopus jelölt: 12 | WoS/Scopus jelölt: 18 | DOI jelölt: 18 (Nem nyilvános: 1) </div> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div class="lastModified">Utolsó módosítás: 2024.02.27. 14:45 Pécsi Éva (MTMT Közp 3, admin)
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :19
Export Date: 6 March 2024
CODEN: OBCRA
Correspondence Address: Kann, N.; Department of Chemical and Biological Engineering, Sweden</pre>
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;24792442" target="_blank">cis-2-Aminocyclohex-4-enecarboxylic acid as a new building block of helical foldamers</a></div> <div> <span class="journal-title">NEW JOURNAL OF CHEMISTRY</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :8
Export Date: 6 March 2024
CODEN: NJCHE
Correspondence Address: Choi, S.H.; Department of Chemistry, South Korea; email: sh-choi@yonsei.ac.kr</pre>
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" mtid="10022837"> <a href="/gui2/?type=authors&mode=browse&sel=10022837" target="_blank">M Mándity, István ✉</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="1381350"> <a href="/gui2/?type=authors&mode=browse&sel=1381350" target="_blank">Fülöp, Ferenc ✉</a> </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;2993085" mtid="2993085" target="_blank">An overview of peptide and peptoid foldamers in medicinal chemistry</a></div> <div class="pub-info"> <span class="journal-title">EXPERT OPINION ON DRUG DISCOVERY</span> <span class="journal-volume">10</span> : <span class="journal-issue">11</span> <span class="page"> pp. 1163-1177. , 15 p. </span> <span class="year">(2015)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_PAY" title=" Fizetős "> <a style="color:blue" title="10.1517/17460441.2015.1076790" target="_blank" href="https://doi.org/10.1517/17460441.2015.1076790"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000369965800001" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000369965800001"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84946500622" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84946500622"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="26289578" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=26289578&dopt=Abstract"> PubMed </a> </span> <span class="id identifier oa_CLOSED" title=" Zárt "> <a style="color:blue" title="6001" target="_blank" href="http://publicatio.bibl.u-szeged.hu/6001"> SZTE Publicatio </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:2993085 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Összefoglaló cikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 55</span> | Független: 52 | Függő: 3 | Nem jelölt: 0 | WoS jelölt: 52 | Scopus jelölt: 50 | WoS/Scopus jelölt: 54 | DOI jelölt: 55 </div> </div> </div> </div><div class="JournalArticle Publication long-list"> <div class="authors"> <img title="Forrásközlemény" style="float: left" src="/frontend/resources/grid/publication-core-icon.png"> <img title="Idézőközlemény" style="float: left" src="/frontend/resources/grid/publication-citation-icon.png"> <div class="autype autype0"> <span class="author-name" mtid="10022837"><a href="/gui2/?type=authors&mode=browse&sel=10022837" target="_blank">M Mándity István ✉ (<span class="authorship-author-name">Mándity István</span> <span class="authorAux-mtmt"> Gyógyszerkémia, gyógyszerkutatás</span>) </a> </span> <span class="author-affil"><span title="Szegedi Tudományegyetem">SZTE</span>/<span title="Gyógyszerésztudományi Kar">GYTK</span>/Gyógyszerkémiai Intézet</span> ; 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Funding Agency and Grant Number: Hungarian Academy of Sciences (Lendulet program) [LP-2011-009]; Gedeon Richter Plc. [TP7-017]; Hungarian Research Foundation [OTKA K112442]\n Funding text: This work was supported by the Hungarian Academy of Sciences (Lendulet program LP-2011-009), Gedeon Richter Plc. (TP7-017), and the Hungarian Research Foundation (OTKA K112442). Computations were carried out at the HPC Center of the University of Szeged (TAMOP-4.2.2.C-11/1/KONV-2012-0010).\n
Funding Agency and Grant Number: Hungarian Academy of Sciences (Lendulet program) [LP-2011-009]; Gedeon Richter Plc. [TP7-017]; Hungarian Research FoundationOrszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [OTKA K112442]
Funding text: This work was supported by the Hungarian Academy of Sciences (Lendulet program LP-2011-009), Gedeon Richter Plc. (TP7-017), and the Hungarian Research Foundation (OTKA K112442). Computations were carried out at the HPC Center of the University of Szeged (TAMOP-4.2.2.C-11/1/KONV-2012-0010).
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Induced Folding of Protein-Sized Foldameric β-Sandwich Models with Core β-Amino Acid Residues
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The mimicry of protein-sized β-sheet structures with unnatural peptidic sequences (foldamers) is a considerable challenge. In this work, the de novo designed betabellin-14 β-sheet has been used as a template, and α→β residue mutations were carried out in the hydrophobic core (positions 12 and 19). β-Residues with diverse structural properties were utilized: Homologous β3-amino acids, (1R,2S)-2-aminocyclopentanecarboxylic acid (ACPC), (1R,2S)-2-aminocyclohexanecarboxylic acid (ACHC), (1R,2S)-2-aminocyclohex-3-enecarboxylic acid (ACEC), and (1S,2S,3R,5S)-2-amino-6,6-dimethylbicyclo[3.1.1]heptane-3-carboxylic acid (ABHC). Six α/β-peptidic chains were constructed in both monomeric and disulfide-linked dimeric forms. Structural studies based on circular dichroism spectroscopy, the analysis of NMR chemical shifts, and molecular dynamics simulations revealed that dimerization induced β-sheet formation in the 64-residue foldameric systems. Core replacement with (1R,2S)-ACHC was found to be unique among the β-amino acid building blocks studied because it was simultaneously able to maintain the interstrand hydrogen-bonding network and to fit sterically into the hydrophobic interior of the β-sandwich. The novel β-sandwich model containing 25% unnatural building blocks afforded protein-like thermal denaturation behavior. Dissolving sandwiches: A water-soluble β-sandwich has been constructed by using cyclic β-amino acids in the hydrophobic core (see figure). The structural stability is highly dependent on the side-chain, and the destructuring effects of the β-residues could be minimized by using (1R,2S)-2-aminocyclohexanecarboxylic acid. The β-sandwich displays protein-like thermal denaturation behavior.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" mtid="10033721"> <a href="/gui2/?type=authors&mode=browse&sel=10033721" target="_blank">Olajos, G</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10001147"> <a href="/gui2/?type=authors&mode=browse&sel=10001147" target="_blank">Hetényi, A</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10027663"> <a href="/gui2/?type=authors&mode=browse&sel=10027663" target="_blank">Wéber, E</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10033720"> <a href="/gui2/?type=authors&mode=browse&sel=10033720" target="_blank">Németh, LJ</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10002784"> <a href="/gui2/?type=authors&mode=browse&sel=10002784" target="_blank">Szakonyi, Z</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="1381350"> <a href="/gui2/?type=authors&mode=browse&sel=1381350" target="_blank">Fülöp, F</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10001168"> <a href="/gui2/?type=authors&mode=browse&sel=10001168" target="_blank">Martinek, TA ✉</a> </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;2868602" mtid="2868602" target="_blank">Induced Folding of Protein-Sized Foldameric β-Sandwich Models with Core β-Amino Acid Residues</a></div> <div class="pub-info"> <span class="journal-title">CHEMISTRY-A EUROPEAN JOURNAL</span> <span class="journal-volume">21</span> : <span class="journal-issue">16</span> <span class="page"> pp. 6173-6180. , 8 p. </span> <span class="year">(2015)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1002/chem.201405581" target="_blank" href="https://doi.org/10.1002/chem.201405581"> DOI </a> </span> <span class="id identifier oa_CLOSED" title=" Zárt "> <a style="color:black" title="60949" target="_blank" href="http://real.mtak.hu/60949"> REAL </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000352508300026" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000352508300026"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84926358041" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84926358041"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="25677195" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=25677195&dopt=Abstract"> PubMed </a> </span> <span class="id identifier oa_RESTRICTED" title=" Korlátozott "> <a style="color:blue" title="5372" target="_blank" href="http://publicatio.bibl.u-szeged.hu/5372"> SZTE Publicatio </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:2868602 </span> <span class="status-holder"><span class="status-data status-VALIDATED"> Egyeztetett </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 15</span> | Független: 9 | Függő: 6 | Nem jelölt: 0 | WoS jelölt: 11 | Scopus jelölt: 13 | WoS/Scopus jelölt: 13 | DOI jelölt: 13 </div> </div> </div> </div><div class="JournalArticle Publication long-list">
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<span class="author-affil"><span title="Szegedi Tudományegyetem">SZTE</span>/<span title="Gyógyszerésztudományi Kar">GYTK</span>/Gyógyszerkémiai Intézet</span>
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;2868602" target="_blank">Induced Folding of Protein-Sized Foldameric β-Sandwich Models with Core β-Amino Acid Residues</a></div> <div> <span class="journal-title">CHEMISTRY-A EUROPEAN JOURNAL</span>
<span class="journal-issn">(<a target="_blank" href="https://portal.issn.org/resource/ISSN/0947-6539">0947-6539</a> <a target="_blank" href="https://portal.issn.org/resource/ISSN/1521-3765">1521-3765</a>)</span>:
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<div class="mtid"><span class="long-pub-mtid">Közlemény: 2868602</span>
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<div class="lastModified">Utolsó módosítás: 2024.02.08. 14:10 Belházyné Szombathelyi Ágnes (SZTE admin5)
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Funding Agency and Grant Number: Hungarian Academy of Sciences (Lendulet program) [LP-2011-009]; Gedeon Richter Plc. [TP7-017]; Hungarian Research Foundation [OTKA K112442]\n Funding text: This work was supported by the Hungarian Academy of Sciences (Lendulet program LP-2011-009), Gedeon Richter Plc. (TP7-017), and the Hungarian Research Foundation (OTKA K112442). Computations were carried out ...</pre>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :14
Export Date: 6 March 2024
CODEN: RSCAC
Correspondence Address: Haldar, D.; Department of Chemical Sciences, Indian Institute of Science Education and Research KolkataIndia</pre>
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Department of Chemistry, University of Wisconsin-Madison, Madison, WI 53706, United States
Department of Chemistry, Yale University, New Haven, CT 06520, United States
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Export Date: 6 March 2024
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Correspondence Address: Gellman, S.H.; Department of Chemistry, University of Wisconsin-MadisonUnited States
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;24327528" target="_blank">A γ-Amino Acid That Favors 12/10-Helical Secondary Structure in α/γ-Peptides</a></div> <div> <span class="journal-title">JOURNAL OF THE AMERICAN CHEMICAL SOCIETY</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Department of Chemistry, University of Wisconsin-Madison, Madison, WI 53706, United States
Department of Chemistry, Yale University, New Haven, CT 06520, United States
Cited By :51
Export Date: 6 March 2024
CODEN: JACSA
Correspondence Address: Gellman, S.H.; Department of Chem...</pre>
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Jadhav, Sandip V </span> <span class="author-type"> </span> ; <span class="author-name" > Misra, Rajkumar </span> <span class="author-type"> </span> ; <span class="author-name" > Gopi, Hosahudya N </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;24777367" mtid="24777367" target="_blank">Foldamers to Nanotubes: Influence of Amino Acid Side Chains in the Hierarchical Assembly of alpha,gamma(4)-Hybrid Peptide Helices</a></div> <div class="pub-info"> <span class="journal-title">CHEMISTRY-A EUROPEAN JOURNAL</span> <span class="journal-volume">20</span> : <span class="journal-issue">50</span> <span class="page"> pp. 16523-16528. , 6 p. </span> <span class="year">(2014)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1002/chem.201404961" target="_blank" href="https://doi.org/10.1002/chem.201404961"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000346055800017" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000346055800017"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84956926315" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84956926315"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="25346477" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=25346477&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:24777367 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :19
Export Date: 6 March 2024
CODEN: CEUJE
Correspondence Address: Gopi, H.N.; Department of Chemistry, Dr. Homi Bhabha Road, India; email: hn.gopi@iiserpune.ac.in</pre>
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Department of Chemical and Biological Engineering, Physical Chemistry, Chalmers University of Technology, 41296 Göteborg, Sweden
Department of Chemical and Biological Engineering, Organic Chemistry, Chalmers University of Technology, 41296 Göteborg, Sweden
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Export Date: 6 March 2024
CODEN: EJOCF
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Non-natural peptides with structures and functions similar to natural peptides have emerged lately in biomedical as well as nanotechnological contexts. They are interesting for pharmaceutical applications since they can adopt structures with new targeting potentials and because they are generally not prone to degradation by proteases. We report here a new set of peptidomimetics derived from δ-peptides, consisting of n units of a 1,5-disubstituted 1,2,3-triazole amino acid (5Tzl). The monomer was prepared using ruthenium-catalyzed azide-alkyne cycloaddition (RuAAC) chemistry using [RuCl2Cp]x as the catalyst, allowing for simpler purification and resulting in excellent yields. This achiral monomer was used to prepare peptide oligomers that are water soluble independent of peptide chain length. Conformational analysis and structural investigations of the oligomers were performed by 2D NOESY NMR experiments, and by quantum chemical calculations using the ωB97X-D functional. These data indicate that several conformations may co-exist with slight energetic differences. Together with their increased hydrophilicity, this feature of homo-5Tzl may prove essential for mimicking natural peptides composed of α-amino acids, where the various secondary structures are achieved by side chain effects and not by the rigidity of the peptide backbone. The improved synthetic method allows for facile variation of the 5Tzl amino acid side chains, further increasing the versatility of these compounds. A new set of non-natural peptides composed of 1,5-disubstituted 1,2,3-triazole amino acids is presented. These peptides benefit from: a) modular synthesis of the monomers, allowing variation of the side chains; b) increased solubility of the oligomers in water, irrespective of peptide length; c) flexibility of the backbone allowing these foldamers to adopt several conformations. Copyright © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Department of Chemical and Biological Engineering, Physical Chemistry, Chalmers University of Technology, 41296 Göteborg, Sweden
Department of Chemical and Biological Engineering, Organic Chemistry, Chalmers University of Technology, 41296 Göteborg, Sweden
Cited By :24
Export Date: 6 March 2024
CODEN...</pre>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Department of Chemistry, Yonsei University, Seoul 120-749, South Korea
Department of Chemistry, University of Wisconsin, Madison WI 53706, United States
Cited By :16
Export Date: 6 March 2024
CODEN: OBCRA
Correspondence Address: Choi, S.H.; Department of Chemistry, , Seoul 120...</pre>
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Funding text: We are grateful to the Hungarian Research Foundation (OTKA NK81371 and PD103994) and TAMOP 4.2.2/B-10/1-2010-0012. I. M. M. acknowledges the award of a Janos Bolyai scholarship from the Hungarian Academy of Sciences.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" mtid="10022837"> <a href="/gui2/?type=authors&mode=browse&sel=10022837" target="_blank">Mandity, I M</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10055110"> <a href="/gui2/?type=authors&mode=browse&sel=10055110" target="_blank">Olasz, B</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10030147"> <a href="/gui2/?type=authors&mode=browse&sel=10030147" target="_blank">Otvos, S B</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="1381350"> <a href="/gui2/?type=authors&mode=browse&sel=1381350" target="_blank">Fulop, F ✉</a> </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;2730808" mtid="2730808" target="_blank">Continuous-Flow Solid-Phase Peptide Synthesis: A Revolutionary Reduction of the Amino Acid Excess</a></div> <div class="pub-info"> <span class="journal-title">CHEMSUSCHEM</span> <span class="journal-volume">7</span> : <span class="journal-issue">11</span> <span class="page"> pp. 3172-3176. , 5 p. </span> <span class="year">(2014)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_PAY" title=" Fizetős "> <a style="color:blue" title="10.1002/cssc.201402436" target="_blank" href="https://doi.org/10.1002/cssc.201402436"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000344538400024" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000344538400024"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84931378914" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84931378914"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="25196512" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=25196512&dopt=Abstract"> PubMed </a> </span> <span class="id identifier oa_RESTRICTED" title=" Korlátozott "> <a style="color:blue" title="4758" target="_blank" href="http://publicatio.bibl.u-szeged.hu/4758"> SZTE Publicatio </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:2730808 </span> <span class="status-holder"><span class="status-data status-VALIDATED"> Egyeztetett </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 50</span> | Független: 37 | Függő: 13 | Nem jelölt: 0 | WoS jelölt: 47 | Scopus jelölt: 48 | WoS/Scopus jelölt: 49 | DOI jelölt: 50 </div> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div class="autype autype0"> <span class="author-name" mtid="10022837"><a
href="/gui2/?type=authors&mode=browse&sel=10022837" target="_blank">Mandity I M
(<span class="authorship-author-name">Mándity István</span>
<span class="authorAux-mtmt"> Gyógyszerkémia, gyógyszerkutatás</span>)
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<span class="author-affil"><span title="Szegedi Tudományegyetem">SZTE</span>/<span title="Gyógyszerésztudományi Kar">GYTK</span>/Gyógyszerkémiai Intézet</span>
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<span class="author-name" mtid="10055110"><a
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<span class="authorAux-mtmt"> Elméleti Kémia</span>)
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<span class="author-name" mtid="10030147"><a
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<span class="author-affil"><span title="Szegedi Tudományegyetem">SZTE</span>/<span title="Gyógyszerésztudományi Kar">GYTK</span>/Gyógyszerkémiai Intézet</span>
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<span class="author-affil"><span title="Szegedi Tudományegyetem">SZTE</span>/<span title="MTA-SZTE Sztereokémiai Kutatócsoport">MTASZTESZK</span>/MTA-SZTE Sztereokémiai Kutatócsoport-GYTK; <span title="Szegedi Tudományegyetem">SZTE</span>/<span title="Gyógyszerésztudományi Kar">GYTK</span>/Gyógyszerkémiai Intézet</span>
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;2730808" target="_blank">Continuous-Flow Solid-Phase Peptide Synthesis: A Revolutionary Reduction of the Amino Acid Excess</a></div> <div> <span class="journal-title">CHEMSUSCHEM</span>
<span class="journal-issn">(<a target="_blank" href="https://portal.issn.org/resource/ISSN/1864-5631">1864-5631</a> <a target="_blank" href="https://portal.issn.org/resource/ISSN/1864-564X">1864-564X</a>)</span>:
<span class="journal-volume">7</span> <span class="journal-issue">11</span>
<span class="page">
pp 3172-3176
</span> <span class="year">(2014)</span>
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<span class="language" xmlns="http://www.w3.org/1999/html">Nyelv:
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PubMed
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<a style="color:blue" title="4758" target="_blank" href="http://publicatio.bibl.u-szeged.hu/4758">
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<div class="publication-citation" style="margin-left: 0.5cm;">
<span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 50</span>
| Független: 37
| Függő: 13
| Nem jelölt: 0
| WoS jelölt: 47
| Scopus jelölt: 48
| WoS/Scopus jelölt: 49
| DOI jelölt: 50
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<div class="publication-citation">
<a target="_blank" href="/api/publication?cond=citations.related;eq;2730808&sort=publishedYear,desc&sort=title">
Idézett közlemények száma: 14
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<div class="mtid"><span class="long-pub-mtid">Közlemény: 2730808</span>
| <span class="status-data status-VALIDATED"> Egyeztetett
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<span class="oldId">Régi azonosító: 2730808</span> |
Forrás Idéző
| <span class="type-subtype">Folyóiratcikk
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| <span class="pub-category">Tudományos</span>
| <span class="publication-sourceOfData">kézi felvitel</span>
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<div class="notDuplums"><a target="_blank" href="/api/publication/2730808/notduplums">3 Nem duplumnak jelölés</a>
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<div class="lastModified">Utolsó módosítás: 2024.02.27. 13:55 Pécsi Éva (MTMT Közp 3, admin)
</div>
<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Funding Agency and Grant Number: Hungarian Research FoundationOrszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [OTKA NK81371, PD103994]; TAMOP [4.2.2/B-10/1-2010-0012]; Hungarian Academy of SciencesHungarian Academy of Sciences
Funding text: We are grateful to the Hungarian Research Foundation (OTKA NK81371 and PD103994) and TAMOP 4.2.2/B-10/1-2010-0012. I. M. M. acknowledges the a...</pre>
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" mtid="10022837"> <a href="/gui2/?type=authors&mode=browse&sel=10022837" target="_blank">Mándity, IM</a> </span> <span class="author-type"> </span> ; <span class="author-name" > Monsignori, A </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10000567"> <a href="/gui2/?type=authors&mode=browse&sel=10000567" target="_blank">Fülöp, L</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10002835"> <a href="/gui2/?type=authors&mode=browse&sel=10002835" target="_blank">Forro, E</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="1381350"> <a href="/gui2/?type=authors&mode=browse&sel=1381350" target="_blank">Fülöp, F ✉</a> </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;2583563" mtid="2583563" target="_blank">Exploiting aromatic interactions for β-peptide foldamer helix stabilization: A significant design element</a></div> <div class="pub-info"> <span class="journal-title">CHEMISTRY-A EUROPEAN JOURNAL</span> <span class="journal-volume">20</span> : <span class="journal-issue">16</span> <span class="page"> pp. 4591-4597. , 7 p. </span> <span class="year">(2014)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_PAY" title=" Fizetős "> <a style="color:blue" title="10.1002/chem.201304448" target="_blank" href="https://doi.org/10.1002/chem.201304448"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000334080800013" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000334080800013"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84898846560" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84898846560"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="24664416" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=24664416&dopt=Abstract"> PubMed </a> </span> <span class="id identifier oa_RESTRICTED" title=" Korlátozott "> <a style="color:blue" title="4698" target="_blank" href="http://publicatio.bibl.u-szeged.hu/4698"> SZTE Publicatio </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="deleted-record">Zárolt</span> <span class="short-pub-mtid"> Közlemény:2583563 </span> <span class="status-holder"><span class="status-data status-VALIDATED"> Egyeztetett </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 28</span> | Független: 26 | Függő: 2 | Nem jelölt: 0 | WoS jelölt: 28 | Scopus jelölt: 28 | WoS/Scopus jelölt: 28 | DOI jelölt: 28 </div> </div> </div> </div><div class="JournalArticle Publication long-list"> <div class="authors"> <img title="Forrásközlemény" style="float: left" src="/frontend/resources/grid/publication-core-icon.png"> <img title="Idézőközlemény" style="float: left" src="/frontend/resources/grid/publication-citation-icon.png"> <div class="autype autype0"> <span class="author-name" mtid="10022837"><a href="/gui2/?type=authors&mode=browse&sel=10022837" target="_blank">Mándity IM (<span class="authorship-author-name">Mándity István</span> <span class="authorAux-mtmt"> Gyógyszerkémia, gyógyszerkutatás</span>) </a> </span> <span class="author-affil"><span title="Szegedi Tudományegyetem">SZTE</span>/<span title="Gyógyszerésztudományi Kar">GYTK</span>/Gyógyszerkémiai Intézet</span> ; 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Division of Organic Chemistry, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411 008, India
Central NMR Facility, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411 008, India
Centre for Material Characterizations, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411 008, India
Cited By :1
Export Date: 6 March 2024
CODEN: RSCAC
Correspondence Address: Sanjayan, G.J.; Division of Organic Chemistry, Dr. Homi Bhabha Road, Pune 411 008, India; email: gj.sanjayan@ncl.res.in
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Roy, A </span> <span class="author-type"> </span> ; <span class="author-name" > Kotmale, AS </span> <span class="author-type"> </span> ; <span class="author-name" > Gawade, RL </span> <span class="author-type"> </span> ; <span class="author-name" > Puranik, VG </span> <span class="author-type"> </span> ; <span class="author-name" > Rajamohanan, PR </span> <span class="author-type"> </span> ; <span class="author-name" > Sanjayan, GJ </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;23785370" mtid="23785370" target="_blank">Probing the folding induction ability of orthanilic acid in peptides: some observations</a></div> <div class="pub-info"> <span class="journal-title">RSC ADVANCES</span> <span class="journal-volume">4</span> : <span class="journal-issue">25</span> <span class="page"> pp. 13018-13025. , 8 p. </span> <span class="year">(2014)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1039/c3ra47039c" target="_blank" href="https://doi.org/10.1039/c3ra47039c"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000332485000048" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000332485000048"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84896755743" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84896755743"> Scopus </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:23785370 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;23785370" target="_blank">Probing the folding induction ability of orthanilic acid in peptides: some observations</a></div> <div> <span class="journal-title">RSC ADVANCES</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Division of Organic Chemistry, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411 008, India
Central NMR Facility, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411 008, India
Centre for Material Characterizations, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411 008, India
Ci...</pre>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Organic and Biomolecular Chemistry Division, CSIR - Indian Institute of Chemical Technology, Hyderabad 500007, India
Centre for NMR and SC, CSIR - Indian Institute of Chemical Technology, Hyderabad 500007, India
Institute of Biochemistry, Faculty of Biosciences, University of Leipzig, Brüderstrasse 34, 04103 Leipzig, Germany
...</pre>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Organic and Biomolecular Chemistry Division, CSIR-Indian Institute of Chemical Technology, Hyderabad, 500 007, India
Centre for NMR and Structural Chemistry, CSIR-Indian Institute of Chemical Technology, Hyderabad, 500 007, India
Cited By :4
Export Date: 6 March 2024
CODEN: CAAJB
...</pre>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :39
Export Date: 6 March 2024
CODEN: JACSA
Correspondence Address: Grinstaff, M.W.; Departments of Chemistry and Biomedical Engineering, Boston University, Boston, MA 02215, United States; email: mgrin@bu.edu</pre>
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Andre, Christophe </span> <span class="author-type"> </span> ; <span class="author-name" > Legrand, Baptiste </span> <span class="author-type"> </span> ; <span class="author-name" > Moulat, Laure </span> <span class="author-type"> </span> ; <span class="author-name" > Wenger, Emmanuel </span> <span class="author-type"> </span> ; <span class="author-name" > Didierjean, Claude </span> <span class="author-type"> </span> ; <span class="author-name" > Aubert, Emmanuel </span> <span class="author-type"> </span> ; <span class="author-name" > Averlant-Petit, Marie Christine </span> <span class="author-type"> </span> ; <span class="author-name" > Martinez, Jean </span> <span class="author-type"> </span> ; <span class="author-name" > Amblard, Muriel </span> <span class="author-type"> </span> ; <span class="author-name" > Calmes, Monique </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;24709148" mtid="24709148" target="_blank">Mixed Oligoureas Based on Constrained Bicyclic and Acyclic beta-Amino Acids Derivatives: On the Significance of the Subunit Configuration for Folding</a></div> <div class="pub-info"> <span class="journal-title">CHEMISTRY-A EUROPEAN JOURNAL</span> <span class="journal-volume">19</span> : <span class="journal-issue">50</span> <span class="page"> pp. 16963-16971. , 9 p. </span> <span class="year">(2013)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1002/chem.201302829" target="_blank" href="https://doi.org/10.1002/chem.201302829"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000327801800016" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000327801800016"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84889587181" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84889587181"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:black" title="24307359" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=24307359&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:24709148 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;24709148" target="_blank">Mixed Oligoureas Based on Constrained Bicyclic and Acyclic beta-Amino Acids Derivatives: On the Significance of the Subunit Configuration for Folding</a></div> <div> <span class="journal-title">CHEMISTRY-A EUROPEAN JOURNAL</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: IBMM, UMR 5247 CNRS, Universités Montpellier 1 et 2, 15 avenue Charles Flahault, 34093 Montpellier Cedex 5, France
CRM2, UMR 7063 CNRS, Université de Lorraine, Boulevard des Aiguilletes, 54506 Vandoeuvre-lès-Nancy Cedex, France
LCPM-UMR 7568 CNRS, Université de Lorraine, 1 rue Grandville, 54001 Nancy Cedex 1, France
Cited B...</pre>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Department of Chemistry, University of Wisconsin, Madison, WI 53706-1396, United States
Department of Chemistry, Yonsei University, Seoul 120-749, South Korea
Cited By :25
Export Date: 6 March 2024
CODEN: EJOCF
Correspondence Address: Gellman, S.H.; Department of Chemistry, , ...</pre>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Department of Chemistry, University of Wisconsin-Madison, Madison, WI 53706, United States
Department of Chemistry, Yale University, New Haven, CT 06511, United States
Cited By :24
Export Date: 6 March 2024
CODEN: JOCEA
Correspondence Address: Gellman, S.H.; Department of Chem...</pre>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :33
Export Date: 6 March 2024
CODEN: OBCRA
Correspondence Address: Gopi, H.N.; Department of Chemistry, Dr. Homi Bhabha Road, Pune-411 008, India; email: hn.gopi@iiserpune.ac.in</pre>
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Center for Materials Characterization, National Chemical Laboratory, Dr Homi Bhabha Road, Pune, 411 008, India
Cited By :21
Export Date: 6 March 2024
Correspondence Address: Sanjayan, G.J.; Division of Organic Chemistry, Dr Homi Bhabha Road, Pune, 411 008, India; email: gj.sanjayan@ncl.res.in
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Division of Organic Chemistry, National Chemical Laboratory, Dr Homi Bhabha Road, Pune, 411 008, India
Central NMR Facility, National Chemical Laboratory, Dr Homi Bhabha Road, Pune, 411 008, India
Center for Materials Characterization, National Chemical Laboratory, Dr Homi Bhabha Road, Pune, 411 008, India
Cited By :21 ...</pre>
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<div class="lastModified">Utolsó módosítás: 2024.02.27. 15:02 Pécsi Éva (MTMT Közp 3, admin)
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Export Date: 6 March 2024
Correspondence Address: Kimura, S.; Department of Material Chemistry, Japan</pre>
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<div class="lastModified">Utolsó módosítás: 2024.02.27. 15:19 Pécsi Éva (MTMT Közp 3, admin)
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Department of Chemistry, Yonsei University, Seoul, 120-749, South Korea
Department of Chemistry, University of Wisconsin, Madison, 53706, United States
Cited By :38
Export Date: 6 March 2024
CODEN: ACIEF
Correspondence Address: Choi, S.H.; Department of Chemistry, , Seoul, 120...</pre>
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Department of Chemistry, Yale University, New Haven, CT 06511, United States
Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142, United States
Department of Biochemistry, Stanford University, Stanford, CA 94305, United States
Department of Biochemistry, University of Washington, Seattle, WA 98195, United States
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Department of Chemistry, Yale University, New Haven, CT 06511, United States
Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142, United States
Department of Biochemistry, Stanford University, Stanford, CA 94305, United States
Department of Biochemistry, University of Washington, Seattle,...</pre>
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Institute of Pharmaceutical Chemistry, University of Szeged, 6720 Szeged, Hungary
Faculty of Chemistry and Biochemistry, Ruhr University Bochum, 44801 Bochum, Germany
Paris Lodron University Salzburg, Department of Molecular Biology, Billrothstrasse 11, 5020 Salzburg, Austria
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Export Date: 1 October 2021
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Berlicki, Ł </span> <span class="author-type"> </span> ; <span class="author-name" > Pilsl, L </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10027663"> <a href="/gui2/?type=authors&mode=browse&sel=10027663" target="_blank">Wéber, E</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10022837"> <a href="/gui2/?type=authors&mode=browse&sel=10022837" target="_blank">Mándity, I M</a> </span> <span class="author-type"> </span> ; <span class="author-name" > Cabrele, C </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10001168"> <a href="/gui2/?type=authors&mode=browse&sel=10001168" target="_blank">Martinek, T A</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="1381350"> <a href="/gui2/?type=authors&mode=browse&sel=1381350" target="_blank">Fülöp, F</a> </span> <span class="author-type"> </span> ; <span class="author-name" > Reiser, O ✉ </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;1926671" mtid="1926671" target="_blank">Unique α,β- and α,α,β,β-peptide foldamers based on cis-β-aminocyclopentanecarboxylic acid</a></div> <div class="pub-info"> <span class="journal-title">ANGEWANDTE CHEMIE-INTERNATIONAL EDITION</span> <span class="journal-volume">51</span> : <span class="journal-issue">9</span> <span class="page"> pp. 2208-2212. , 5 p. </span> <span class="year">(2012)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_PAY" title=" Fizetős "> <a style="color:blue" title="10.1002/anie.201107702" target="_blank" href="https://doi.org/10.1002/anie.201107702"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000300691900039" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000300691900039"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84857609735" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84857609735"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="22282376" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=22282376&dopt=Abstract"> PubMed </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="http://onlinelibrary.wiley.com/doi/10.1002/anie.201107702/pdf" target="_blank" href="http://onlinelibrary.wiley.com/doi/10.1002/anie.201107702/pdf"> Egyéb URL </a> </span> <span class="id identifier oa_CLOSED" title=" Zárt "> <a style="color:blue" title="10388" target="_blank" href="http://publicatio.bibl.u-szeged.hu/10388"> SZTE Publicatio </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:1926671 </span> <span class="status-holder"><span class="status-data status-VALIDATED"> Egyeztetett </span></span> <span class="pub-core">Forrás Idéző Duplum </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 83</span> | Független: 51 | Függő: 32 | Nem jelölt: 0 | WoS jelölt: 78 | Scopus jelölt: 76 | WoS/Scopus jelölt: 81 | DOI jelölt: 78 </div> </div> </div> </div><div class="JournalArticle Publication long-list">
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;
<span class="author-name" >Pilsl L
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;
<span class="author-name" mtid="10027663"><a
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<span class="author-affil"><span title="Szegedi Tudományegyetem">SZTE</span>/<span title="Gyógyszerésztudományi Kar">GYTK</span>/<span title="Gyógyszerkémiai Intézet">GYKI</span>/MTA-SZTE Lendület Peptidfoldamer Kutatócsoport</span>
;
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;
<span class="author-name" >Reiser O ✉
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;1926671" target="_blank">Unique α,β- and α,α,β,β-peptide foldamers based on cis-β-aminocyclopentanecarboxylic acid</a></div> <div> <span class="journal-title">ANGEWANDTE CHEMIE-INTERNATIONAL EDITION</span>
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<div class="duplumMark">Duplumjelölés:
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(Lövei Anett (ELTE TTK 5-ös admin))
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<div class="lastModified">Utolsó módosítás: 2022.07.17. 01:55 Áts József (admin)
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Universität Regensburg, Institut für Organische Chemie, Universitätsstrasse 31, 93053 Regensburg, Germany
Department of Bioorganic Chemistry, Wrocław University of Technology, 50-370 Wrocław, Poland
Institute of Pharmaceutical Chemistry, University of Szeged, 6720 Szeged, Hungary
Faculty of Chemistry and Biochemistry, Ruhr ...</pre>
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Dane, EL </span> <span class="author-type"> </span> ; <span class="author-name" > Grinstaff, MW </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;24248717" mtid="24248717" target="_blank">Poly-amido-saccharides: Synthesis via Anionic Polymerization of a beta-Lactam Sugar Monomer</a></div> <div class="pub-info"> <span class="journal-title">JOURNAL OF THE AMERICAN CHEMICAL SOCIETY</span> <span class="journal-volume">134</span> : <span class="journal-issue">39</span> <span class="page"> pp. 16255-16264. , 10 p. </span> <span class="year">(2012)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1021/ja305900r" target="_blank" href="https://doi.org/10.1021/ja305900r"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000309335000030" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000309335000030"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84867068839" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84867068839"> Scopus </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:24248717 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :75
Export Date: 6 March 2024
CODEN: JACSA
Correspondence Address: Grinstaff, M.W.; Department of Chemistry and Biomedical Engineering, , Boston, MA 02215, United States; email: mgrin@bu.edu</pre>
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Chirality of the monomeric residues controls and determines the prevalent folding of small oligopeptides (from di- to tetramers) composed of 2-aminocyclobutane-1-carboxylic acid (ACBA) derivatives with the same or different absolute and relative configuration. The cis-form of the monomeric ACBA gives rise to two conformers, namely, Z6 and Z8, while the trans-form manifests uniquely as an H8 structure. By combining these subunits in oligo- and polypeptides, their local structural preference remains, thus allowing the rational design of new short foldamers. A lego-type molecular architecture evolves; the overall look depends only on the conformational properties of the structural building units. A versatile and efficient method to predict the backbone folds of designed cyclobutane β-peptides is based on QM calculations. Predictions are corroborated by high-resolution NMR studies on selected stereoisomers, most of them being new foldamers that have been synthesized and characterized for the first time. Thus, the chiral expression of monomeric building units results in the defined secondary structures of small oligomers. As a result of this study, a new set of chirality controlled foldamers is provided to probe as biocompatible biopolymers. © 2012 American Chemical Society.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Gorrea, E </span> <span class="author-type"> </span> ; <span class="author-name" > Pohl, G </span> <span class="author-type"> </span> ; <span class="author-name" > Nolis, P </span> <span class="author-type"> </span> ; <span class="author-name" > Celis, S </span> <span class="author-type"> </span> ; <span class="author-name" > Burusco, KK </span> <span class="author-type"> </span> ; <span class="author-name" > Branchadell, V </span> <span class="author-type"> </span> ; <span class="author-name" mtid="1062306"> <a href="/gui2/?type=authors&mode=browse&sel=1062306" target="_blank">Perczel, A</a> </span> <span class="author-type"> </span> ; <span class="author-name" > Ortuño, RM </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;2129197" mtid="2129197" target="_blank">Secondary structure of short β-peptides as the chiral expression of monomeric building units: A rational and predictive model</a></div> <div class="pub-info"> <span class="journal-title">JOURNAL OF ORGANIC CHEMISTRY</span> <span class="journal-volume">77</span> : <span class="journal-issue">21</span> <span class="page"> pp. 9795-9806. , 12 p. </span> <span class="year">(2012)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1021/jo302034b" target="_blank" href="https://doi.org/10.1021/jo302034b"> DOI </a> </span> <span class="id identifier oa_NONE" title=" Nincs "> <span class="isbnOrIssn"> ISSN: </span> <a style="color:blue" title="0022-3263" target="_blank" href="https://portal.issn.org/resource/ISSN/0022-3263"> 0022-3263 </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000311190200039" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000311190200039"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84868383829" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84868383829"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="23030251" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=23030251&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:2129197 </span> <span class="status-holder"><span class="status-data status-CHECKED"> Hitelesített </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 27</span> | Független: 13 | Függő: 14 | Nem jelölt: 0 | WoS jelölt: 27 | Scopus jelölt: 21 | WoS/Scopus jelölt: 27 | DOI jelölt: 27 </div> </div> </div> </div><div class="JournalArticle Publication long-list"> <div class="authors"> <img title="Forrásközlemény" style="float: left" src="/frontend/resources/grid/publication-core-icon.png"> <img title="Idézőközlemény" style="float: left" src="/frontend/resources/grid/publication-citation-icon.png"> <div class="autype autype0"> <span class="author-name" >Gorrea E </span> ; 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Funding Agency and Grant Number: Hungarian Research FoundationOrszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [NK81371, K83882, TAMOP-4.2.1/B-09/1/KONV-2010-0005]; COSTEuropean Cooperation in Science and Technology (COST) [CM0803]; Janos Bolyai FellowshipHungarian Academy of Sciences; HAS [LP2011-009/2011]
Funding text: We thank the Hungarian Research Foundation (NK81371 and K83882), TAMOP-4.2.1/B-09/1/KONV-2010-0005 and COST (CM0803) for financial support. T.A.M. acknowledges the Janos Bolyai Fellowship and the "Lendulet'' programme (LP2011-009/2011) from the HAS.
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Non-natural folded polymers (foldamers) display considerable versatility, and the design of such molecules is of great current interest. In this respect, peptidic foldamers are perhaps the best-characterized systems, as they populate a number of residue-controlled secondary structures, which have found various biological applications and have also led to the creation of nanostructured materials. This critical review covers recent developments related to diverse building blocks and modern foldamer design principles, such as the stereochemical patterning methods. The recent achievements concerning tertiary/quaternary structures and the self-assembling foldameric nanostructures are also addressed (176 references).
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" mtid="10001168"> <a href="/gui2/?type=authors&mode=browse&sel=10001168" target="_blank">Martinek, TA</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="1381350"> <a href="/gui2/?type=authors&mode=browse&sel=1381350" target="_blank">Fulop, F ✉</a> </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;1842290" mtid="1842290" target="_blank">Peptidic foldamers: ramping up diversity</a></div> <div class="pub-info"> <span class="journal-title">CHEMICAL SOCIETY REVIEWS</span> <span class="journal-volume">41</span> : <span class="journal-issue">2</span> <span class="page"> pp. 687-702. , 16 p. </span> <span class="year">(2012)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1039/c1cs15097a" target="_blank" href="https://doi.org/10.1039/c1cs15097a"> DOI </a> </span> <span class="id identifier oa_CLOSED" title=" Zárt "> <a style="color:black" title="60951" target="_blank" href="http://real.mtak.hu/60951"> REAL </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000298854900012" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000298854900012"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="83455254495" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-83455254495"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="21769415" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=21769415&dopt=Abstract"> PubMed </a> </span> <span class="id identifier oa_RESTRICTED" title=" Korlátozott "> <a style="color:blue" title="10397" target="_blank" href="http://publicatio.bibl.u-szeged.hu/10397"> SZTE Publicatio </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:1842290 </span> <span class="status-holder"><span class="status-data status-VALIDATED"> Egyeztetett </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Összefoglaló cikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 445</span> | Független: 390 | Függő: 55 | Nem jelölt: 0 | WoS jelölt: 409 | Scopus jelölt: 418 | WoS/Scopus jelölt: 420 | DOI jelölt: 421 </div> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;1842290" target="_blank">Peptidic foldamers: ramping up diversity</a></div> <div> <span class="journal-title">CHEMICAL SOCIETY REVIEWS</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Funding Agency and Grant Number: Hungarian Research FoundationOrszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [NK81371, K83882, TAMOP-4.2.1/B-09/1/KONV-2010-0005]; COSTEuropean Cooperation in Science and Technology (COST) [CM0803]; Janos Bolyai FellowshipHungarian Academy of Sciences; HAS [LP2011-009/2011]
Funding text: We thank the Hungarian Research Foundation (NK81371 and K8388...</pre>
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Cooperative interaction between multiple chiral centers dictates the absolute handedness of structural folding. We have designed and prepared a series of chiral C 3-symmetric tris(N-salicylidenamine) derivatives that adopt three-blade propeller-like conformations. Synthetic access to an expanded family of such constructs was aided by enzymatic resolution and C-C cross-coupling reactions of aryl-substituted chiral propargylic alcohol derivatives. These key structural components were integrated into molecular propellers of predetermined helical screw sense. Through comparative studies on a homologous set of molecules, we found that installation of phenylene-ethynylene-derived π-conjugation profoundly affected the stabilities of the helically folded structures, as evidenced by UV/Vis and circular dichroism (CD) studies. Increasing the number of hydrogen bonds through additional substitution also enhanced the populations of the folded conformations in solution. In addition to introducing steric bias to control structural folding, linearly π-conjugated groups function as spatially well-defined chromophores that give rise to characteristic exciton-coupled circular dichroism. Absolute configurations of chiral centers could thus be further confirmed by comparing the torsional relationships between pairs of chromophores on adjacent subunits, which are fully consistent with the computationally predicted structural models. Twist to fold: Chiral alcohol groups effectively direct the absolute helicities of three-bladed propeller-shaped C 3-symmetric molecules through tight O-H⋯O-H contacts. The stabilities of the conformations of these systems depend upon the numbers of hydrogen bonds and the steric bulk of the π-conjugated substituents on thestereogenic centers. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :6
Export Date: 6 March 2024
CODEN: EJOCF
Correspondence Address: Lee, D.; Department of Chemistry, 800 East Kirkwood Avenue, Bloomington, IN 47405, United States; email: dongwhan@indiana.edu</pre>
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Prabhakaran, P </span> <span class="author-type"> </span> ; <span class="author-name" > Azzarito, V </span> <span class="author-type"> </span> ; <span class="author-name" > Jacobs, T </span> <span class="author-type"> </span> ; <span class="author-name" > Hardie, MJ </span> <span class="author-type"> </span> ; <span class="author-name" > Kilner, CA </span> <span class="author-type"> </span> ; <span class="author-name" > Edwards, TA </span> <span class="author-type"> </span> ; <span class="author-name" > Warriner, SL </span> <span class="author-type"> </span> ; <span class="author-name" > Wilson, AJ </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;22405393" mtid="22405393" target="_blank">Conformational properties of O-alkylated benzamides</a></div> <div class="pub-info"> <span class="journal-title">TETRAHEDRON</span> <span class="journal-volume">68</span> : <span class="journal-issue">23</span> <span class="page"> pp. 4485-4491. , 7 p. </span> <span class="year">(2012)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1016/j.tet.2011.11.078" target="_blank" href="https://doi.org/10.1016/j.tet.2011.11.078"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000304570000022" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000304570000022"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="84860656436" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-84860656436"> Scopus </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:22405393 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;22405393" target="_blank">Conformational properties of O-alkylated benzamides</a></div> <div> <span class="journal-title">TETRAHEDRON</span>
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<div class="lastModified">Utolsó módosítás: 2024.02.27. 15:18 Pécsi Éva (MTMT Közp 3, admin)
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: School of Chemistry, University of Leeds, Woodhouse Lane, Leeds LS2 9JT, United Kingdom
Astbury Centre for Structural Molecular Biology, University of Leeds, Woodhouse Lane, Leeds LS2 9JT, United Kingdom
Institute of Structural and Molecular Biology, University of Leeds, Woodhouse Lane, Leeds LS2 9JT, United Kingdom
Cited B...</pre>
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<div class="Thesis Publication short-list"> <div class="authors"> <span class="author-name" mtid="10027663"> <a href="/gui2/?type=authors&mode=browse&sel=10027663" target="_blank">Wéber, Edit</a> </span> <span class="author-type"> </span> </div > <div class="title"><a href="/gui2/?mode=browse¶ms=publication;2786402" mtid="2786402" target="_blank">Investigation of protein–ligand interactions of targets with solvent-exposed binding sites</a> 56 p.</div> <div class="pub-info"> <span class="publisher">Szegedi Tudományegyetem (SZTE)</span>, <span class="school">Gyógyszertudományok Doktori Iskola,</span> <span class="consultantAuthor">Martinek Tamás </span> <span class="applicationYear">Disszertáció benyújtásának éve: 2012,</span> <span class="acceptanceYear">Védés éve: 2012</span> <span class="publishedYear">Megjelenés/Fokozatszerzés éve: 2012</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:blue" title="10.14232/phd.1475" target="_blank" href="https://doi.org/10.14232/phd.1475"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:black" title="9382" target="_blank" href="http://www.doktori.hu/index.php?menuid=193&vid=9382"> ODT védés </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="http://doktori.bibl.u-szeged.hu/1475/1/dissz_weber_cont.pdf" target="_blank" href="http://doktori.bibl.u-szeged.hu/1475/1/dissz_weber_cont.pdf"> Teljes dokumentum </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:black" title="12652377319443495543" target="_blank" href="http://scholar.Google.com/scholar?hl=en&lr=&cluster=12652377319443495543"> Google scholar </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:2786402 </span> <span class="status-holder"><span class="status-data status-VALIDATED"> Egyeztetett </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Disszertáció (PhD ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="Thesis Publication long-list"> <div class="authors"> <img title="Forrásközlemény" style="float: left" src="/frontend/resources/grid/publication-core-icon.png"> <img title="Idézőközlemény" style="float: left" src="/frontend/resources/grid/publication-citation-icon.png"> <div class="autype autype0"> <span class="author-name" mtid="10027663"><a href="/gui2/?type=authors&mode=browse&sel=10027663" target="_blank">Wéber Edit (<span class="authorship-author-name">Wéber Edit</span> <span class="authorAux-mtmt"> gyógyszerkémia</span>) </a> </span> <span class="author-affil"><span title="Szegedi Tudományegyetem">SZTE</span>/<span title="Gyógyszerésztudományi Kar">GYTK</span>/Gyógyszerkémiai Intézet; <span title="Szegedi Tudományegyetem">SZTE</span>/<span title="Doktori Iskolák">DI</span>/Gyógyszertudományok Doktori Iskola</span> </div> </div> <div class="title"><a href="/gui2/?mode=browse¶ms=publication;2786402" target="_blank">Investigation of protein–ligand interactions of targets with solvent-exposed binding sites</a></div> <div> <span class="publisher">Szegedi Tudományegyetem (SZTE),</span> <span class="school">Gyógyszertudományok Doktori Iskola,</span> <span class="mabDiscipline">természettudományok / kémiai tudományok.</span> <span class="pageLength">56 p.</span> </div> <div class="thesis-cons"> Témavezető(k): <span class="consultantAuthor"><b>Martinek Tamás</b> <span class="authorAux-mtmt">Gyógyszerkémia</span> </span> </div> <div class="applicationYear"> <span class="applicationYear">Disszertáció benyújtásának éve: 2012</span> , <span class="acceptanceYear">Védés éve: 2012 </span> </div> <div class="publishedYear">Megjelenés/Fokozatszerzés éve: 2012 </div> <div class="pub-footer"> <span class="language" xmlns="http://www.w3.org/1999/html">Nyelv: Angol | </span> <span class="identifiers"> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:blue" title="10.14232/phd.1475" target="_blank" href="https://doi.org/10.14232/phd.1475"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:black" title="9382" target="_blank" href="http://www.doktori.hu/index.php?menuid=193&vid=9382"> ODT védés </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="http://doktori.bibl.u-szeged.hu/1475/1/dissz_weber_cont.pdf" target="_blank" href="http://doktori.bibl.u-szeged.hu/1475/1/dissz_weber_cont.pdf"> Teljes dokumentum </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:black" title="12652377319443495543" target="_blank" href="http://scholar.Google.com/scholar?hl=en&lr=&cluster=12652377319443495543"> Google scholar </a> </span> </span> <div class="publication-citation"> <a target="_blank" href="/api/publication?cond=citations.related;eq;2786402&sort=publishedYear,desc&sort=title"> Idézett közlemények száma: 4 </a> </div> <div class="mtid"><span class="long-pub-mtid">Közlemény: 2786402</span> | <span class="status-data status-VALIDATED"> Egyeztetett </span> <span class="oldId">Régi azonosító: 2786402</span> | Forrás Idéző | <span class="type-subtype">Disszertáció ( PhD ) </span> | <span class="pub-category">Tudományos</span> | <span class="publication-sourceOfData">kézi felvitel</span> </div> <div class="lastModified">Utolsó módosítás: 2019.11.18. 13:36 Márton Réka (SZTE admin5-INAKTÍV) </div> </div></div>
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Declerck, V </span> <span class="author-type"> </span> ; <span class="author-name" > Aitken, DJ </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;21529827" mtid="21529827" target="_blank">A refined synthesis of enantiomerically pure 2-aminocyclobutanecarboxylic acids</a></div> <div class="pub-info"> <span class="journal-title">AMINO ACIDS</span> <span class="journal-volume">41</span> : <span class="journal-issue">3</span> <span class="page"> pp. 587-595. , 9 p. </span> <span class="year">(2011)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1007/s00726-011-0918-y" target="_blank" href="https://doi.org/10.1007/s00726-011-0918-y"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000292741700005" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000292741700005"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="80052318244" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-80052318244"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="21541680" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=21541680&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:21529827 </span> <span class="status-holder"><span class="status-data status-ADMIN_APPROVED"> Admin láttamozott </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;21529827" target="_blank">A refined synthesis of enantiomerically pure 2-aminocyclobutanecarboxylic acids</a></div> <div> <span class="journal-title">AMINO ACIDS</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :32
Export Date: 6 March 2024
CODEN: AACIE
Correspondence Address: Aitken, D.J.; Laboratoire de Synthèse Organique et Méthodologie, 15 rue Georges Clemenceau, Orsay Cedex 91405, France; email: david.aitken@u-psud.fr</pre>
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" > Kodama, K </span> <span class="author-type"> </span> ; <span class="author-name" > Sugawara, K </span> <span class="author-type"> </span> ; <span class="author-name" > Hirose, T </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;23594320" mtid="23594320" target="_blank">Synthesis of Chiral 1,3-Diamines Derived from cis-2-Benzamidocyclohexanecarboxylic Acid and Their Application in the Cu-Catalyzed Enantioselective Henry Reaction</a></div> <div class="pub-info"> <span class="journal-title">CHEMISTRY-A EUROPEAN JOURNAL</span> <span class="journal-volume">17</span> : <span class="journal-issue">48</span> <span class="page"> pp. 13584-13592. , 9 p. </span> <span class="year">(2011)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1002/chem.201102136" target="_blank" href="https://doi.org/10.1002/chem.201102136"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000298059600027" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000298059600027"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="81755163894" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-81755163894"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:black" title="22025350" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=22025350&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:23594320 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core"> Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> </div> </div> </div><div class="JournalArticle Publication long-list">
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<span class="author-name" >Sugawara K
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;23594320" target="_blank">Synthesis of Chiral 1,3-Diamines Derived from cis-2-Benzamidocyclohexanecarboxylic Acid and Their Application in the Cu-Catalyzed Enantioselective Henry Reaction</a></div> <div> <span class="journal-title">CHEMISTRY-A EUROPEAN JOURNAL</span>
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<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Cited By :57
Export Date: 6 March 2024
CODEN: CEUJE
Correspondence Address: Kodama, K.; Department of Applied Chemistry, 255 Shimo-Okubo, Sakura-ku, Saitama 338-8570, Japan; email: kodama@mail.saitama-u.ac.jp</pre>
</div></div>