TY - JOUR AU - Park, H.S. AU - Lee, J.Y. AU - Kang, Y.K. TI - Exploring helix structures of γ-peptides based on 2-(aminomethyl)cyclopentanecarboxylic acid JF - BIOPOLYMERS J2 - BIOPOLYMERS PY - 2024 SN - 0006-3525 DO - 10.1002/bip.23575 UR - https://m2.mtmt.hu/api/publication/34757037 ID - 34757037 AB - Conformational search and density functional theory calculations were performed to explore the preferences of helical structures for chiro-specific oligo-γ-peptides of 2-(aminomethyl)cyclopentanecarboxylic acid (γAmc5) with a cyclopentyl constraint on the Cα–Cβ bond in solution. The dimer and tetramer of γAmc5 (1) with homochiral (1S, 2S) configurations exhibited a strong preference for the 9-membered helix foldamer in solution, except for the tetramer in water. However, the oligomers of γAmc5 (1) longer than tetramer preferentially adopted a right-handed (P)-2.614-helix (H1-14) as the peptide sequence becomes longer and as solvent polarity increases. The high stabilities for H1-14 foldamers of γAmc5 (1) in solution were ascribed to the favored solvation free energies. The calculated mean backbone torsion angles for H1-14 helix foldamers of γAmc5 (1) were similar to those calculated for oligomers of other γ-residues with cyclopentane or cyclohexane rings. However, the substitution of cyclopentane constraints on the Cα−Cβ bond of the γAmc5 (1) residue resulted in different conformational preferences and/or handedness of helix foldamers. In particular, the pyrrolidine-substituted analogs of the H1-14 foldamers of γAmc5 (1) with adjacent amine diads substituted at a proximal distance are expected to be potential catalysts for the crossed aldol condensation in nonpolar and polar solvents. © 2024 The Authors. Biopolymers published by Wiley Periodicals LLC. LA - English DB - MTMT ER - TY - JOUR AU - Sukumar, G. AU - Rahul, . AU - Nayani, K. AU - Mainkar, P.S. AU - Prashanth, J. AU - Sridhar, B. AU - Sarma, A.V.S. AU - Bharatam, J. AU - Chandrasekhar, S. TI - 6-Strand to Stable 10/12 Helix Conformational Switch by Incorporating Flexible β-hGly in the Homooligomers of Camphor Derived β-Amino Acid: NMR and X-Ray Crystallographic Evidence JF - ANGEWANDTE CHEMIE-INTERNATIONAL EDITION J2 - ANGEW CHEM INT EDIT PY - 2024 SN - 1433-7851 DO - 10.1002/anie.202403321 UR - https://m2.mtmt.hu/api/publication/34794036 ID - 34794036 AB - Rational design of unnatural amino acid building blocks capable of stabilizing predictable secondary structures similar to protein fragments is pivotal for foldamer chemistry/catalysis. Here, we introduce novel β-amino acid building blocks: [1S,2R,4R]exoCDA and [1S,2S,4R]endoCDA, derived from the abundantly available R(+)-camphor, which is traditionally known for its medicinal value. Further, we demonstrate that the homooligomers of exoCDA adopt 6-strand conformation, which switches to a robust 10/12-helix simply by inserting flexible β-hGly spacer at alternate positions (1 : 1 β-hGly/exoCDA heterooligomers), as evident by DFT-calculations, solution-state NMR spectroscopy and X-ray crystallography. To the best of our knowledge, this is the first example of crystalline-state structure of left-handed 10/12-mixed helix, that is free from the conventional approach of employing β-amino acids of either alternate chirality or alternate β2/β3 substitutions, to access the 10/12-helix. The results also show that the homooligomers of heterochiral exoCDA don′t adopt helical fold, instead exhibit banana-shaped strands, whereas the homodimers of the other diastereomer endoCDA, nucleate 8-membered turns. Furthermore, the homo-exoCDA and hetero-[β-hGly-exoCDA] oligomers are found to exhibit self-association properties with distinct morphological features. Overall, the results offer new possibilties of constructing discrete stable secondary and tertiary structures based on CDAs, which can accommodate flexible residues with desired side-chain substitutions. © 2024 Wiley-VCH GmbH. LA - English DB - MTMT ER - TY - JOUR AU - Chen, Yi-Kai AU - Simon, Isabella A. AU - Maslov, Ivan AU - Oyarce-Pino, Ivan E. AU - Kulkarni, Ketav AU - Hopper, Denham AU - Aguilar, Marie-Isabel AU - Vankadari, Naveen AU - Broughton, Brad R. S. AU - Del Borgo, Mark P. TI - A switch in N-terminal capping of β-peptides creates novel self-assembled nanoparticles JF - RSC ADVANCES J2 - RSC ADV VL - 13 PY - 2023 IS - 42 SP - 29401 EP - 29407 PG - 7 SN - 2046-2069 DO - 10.1039/d3ra04514e UR - https://m2.mtmt.hu/api/publication/34250241 ID - 34250241 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Reza, D. AU - Balo, R. AU - Otero, J.M. AU - Fletcher, A.M. AU - García-Fandino, R. AU - Sánchez-Pedregal, V.M. AU - Davies, S.G. AU - Estévez, R.J. AU - Estévez, J.C. TI - β-Peptides incorporating polyhydroxylated cyclohexane β-amino acid: synthesis and conformational study JF - ORGANIC & BIOMOLECULAR CHEMISTRY J2 - ORG BIOMOL CHEM VL - 21 PY - 2023 SP - 8535 EP - 8547 PG - 13 SN - 1477-0520 DO - 10.1039/d3ob00906h UR - https://m2.mtmt.hu/api/publication/34318027 ID - 34318027 AB - 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 LA - English DB - MTMT ER - TY - JOUR AU - Seo, Nuri AU - Son, Hoyang AU - Kim, Yonghan AU - Guzei, Ilia A. AU - Kang, Philjae AU - Choi, Soo Hyuk TI - Exploring a β-Amino Acid with a Seven-Membered Ring Constraint as a Foldamer Building Block for Nontraditional Helices JF - ORGANIC LETTERS J2 - ORG LETT VL - 25 PY - 2023 IS - 41 SP - 7497 EP - 7501 PG - 5 SN - 1523-7060 DO - 10.1021/acs.orglett.3c02746 UR - https://m2.mtmt.hu/api/publication/34233961 ID - 34233961 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Boruah, Alpana AU - Roy, Arup TI - Advances in hybrid peptide-based self-assembly systems and their applications JF - BIOMATERIALS SCIENCE J2 - BIOMATER SCI-UK VL - 10 PY - 2022 IS - 17 SP - 4694 EP - 4723 PG - 30 SN - 2047-4830 DO - 10.1039/d2bm00775d UR - https://m2.mtmt.hu/api/publication/33173758 ID - 33173758 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Choi, S. AU - Shim, J. AU - Kang, P. AU - Choi, S.H. TI - Effect of a: Cis -4-aminopiperidine-3-carboxylic acid (cis -APiC) residue on mixed-helical folding of unnatural peptides JF - ORGANIC & BIOMOLECULAR CHEMISTRY J2 - ORG BIOMOL CHEM VL - 20 PY - 2022 IS - 3 SP - 613 EP - 618 PG - 6 SN - 1477-0520 DO - 10.1039/d1ob02223g UR - https://m2.mtmt.hu/api/publication/32696667 ID - 32696667 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Choi, S. AU - Choi, S.H. TI - Synthesis and conformational analysis of an anti-β2,3-amino acid as a building block for unnatural peptide helices JF - BULLETIN OF THE KOREAN CHEMICAL SOCIETY J2 - B KOR CHEM SOC VL - 43 PY - 2022 IS - 2 SP - 241 EP - 245 PG - 5 SN - 0253-2964 DO - 10.1002/bkcs.12457 UR - https://m2.mtmt.hu/api/publication/32693883 ID - 32693883 AB - 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 LA - English DB - MTMT ER - TY - CHAP AU - Kato, T. ED - Makoto, Oba ED - Yosuke, Demizu TI - Foldamer T2 - Cell-Penetrating Peptides: Design, Development and Applications PB - Wiley-VCH Verlag CY - Weinheim SN - 9783527350117 PY - 2022 SP - 79 EP - 107 PG - 29 DO - 10.1002/9783527835997.ch7 UR - https://m2.mtmt.hu/api/publication/34127596 ID - 34127596 LA - English DB - MTMT ER - TY - JOUR AU - Shankar, Sudha AU - Jyothi, Deeti AU - Rahim, Junaid Ur AU - Pal, Purna Chandra AU - Singh, Umesh Prasad AU - Rai, Rajkishor TI - Conformation of Achiral alpha/beta Hybrid Peptides Containing Glycine and 1-Aminocyclohexaneacetic Acid JF - CHEMISTRYSELECT J2 - CHEMISTRYSELECT VL - 7 PY - 2022 IS - 10 PG - 6 SN - 2365-6549 DO - 10.1002/slct.202104453 UR - https://m2.mtmt.hu/api/publication/32955370 ID - 32955370 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Szefczyk, Monika TI - Peptide foldamer-based self-assembled nanostructures containing cyclic beta-amino acids JF - NANOSCALE J2 - NANOSCALE VL - 13 PY - 2021 IS - 26 SP - 11325 EP - 11333 PG - 9 SN - 2040-3364 DO - 10.1039/d1nr02220b UR - https://m2.mtmt.hu/api/publication/32234723 ID - 32234723 N1 - Cited By :10 Export Date: 5 April 2024 Correspondence Address: Szefczyk, M.; Department of Bioorganic Chemistry, Wybrzeże Wyspiańskiego 27, Poland; email: monika.szefczyk@pwr.edu.pl AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Aloisi, Adriano AU - Christensen, Niels Johan AU - Sørensen, Kasper K. AU - Guilbaud-Chéreau, Chloé AU - Jensen, Knud J. AU - Bianco, Alberto TI - Synthesis and Characterization of Adamantane-Containing Heteropeptides with a Chirality Switch JF - EUROPEAN JOURNAL OF ORGANIC CHEMISTRY J2 - EUR J ORG CHEM VL - 2020 PY - 2020 IS - 7 SP - 815 EP - 820 PG - 6 SN - 1434-193X DO - 10.1002/ejoc.201901666 UR - https://m2.mtmt.hu/api/publication/31385378 ID - 31385378 LA - English DB - MTMT ER - TY - JOUR AU - Blodgett, Karl N. AU - Jang, Geunhyuk AU - Kim, Sojung AU - Kim, Min Kyung AU - Choi, Soo Hyuk AU - Zwier, Timothy S. TI - Coexistence of Left- and Right-Handed 12/10-Mixed Helices in Cyclically Constrained beta-Peptides and Directed Formation of Single-Handed Helices upon Site-Specific Methylation JF - JOURNAL OF PHYSICAL CHEMISTRY A J2 - J PHYS CHEM A VL - 124 PY - 2020 IS - 28 SP - 5856 EP - 5870 PG - 15 SN - 1089-5639 DO - 10.1021/acs.jpca.0c03545 UR - https://m2.mtmt.hu/api/publication/31422389 ID - 31422389 AB - 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. LA - English DB - MTMT ER - TY - THES AU - Blodgett, Karl N. TI - Ultraviolet and Infrared Spectroscopy of Synthetic Peptides and Natural Products in the Gas Phase PY - 2020 SN - 9798379677206 UR - https://m2.mtmt.hu/api/publication/34839706 ID - 34839706 LA - English DB - MTMT ER - TY - JOUR AU - Misra, Rajkumar AU - George, Gijo AU - Reja, Rahi M. AU - Dey, Sanjit AU - Raghothama, Srinivasarao AU - Gopi, Hosahudya N. TI - Structural insight into hybrid peptide ε-helices JF - CHEMICAL COMMUNICATIONS J2 - CHEM COMMUN VL - 56 PY - 2020 IS - 14 SP - 2171 EP - 2173 PG - 3 SN - 1359-7345 DO - 10.1039/c9cc07413a UR - https://m2.mtmt.hu/api/publication/31385379 ID - 31385379 LA - English DB - MTMT ER - TY - JOUR AU - Nizami, Bilal AU - Bereczki-Szakál, Dorottya AU - Varró, Nikolett AU - El Battioui, Kamal AU - Udyavara Nagaraj, Vignesh AU - Szigyártó, Imola Csilla AU - Mándity, István AU - Beke-Somfai, Tamás TI - FoldamerDB: a database of peptidic foldamers JF - NUCLEIC ACIDS RESEARCH J2 - NUCLEIC ACIDS RES VL - 48 PY - 2020 IS - D1 SP - D1122 EP - D1128 SN - 0305-1048 DO - 10.1093/nar/gkz993 UR - https://m2.mtmt.hu/api/publication/30933404 ID - 30933404 N1 - 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-2.3.2-15-2016-00017b. Funding for open access charge: Momentum programme of the Hungarian Academy of Sciences [LP2016-2]. LA - English DB - MTMT ER - TY - JOUR AU - Rinaldi, Samuele TI - The Diverse World of Foldamers: Endless Possibilities of Self-Assembly JF - MOLECULES J2 - MOLECULES VL - 25 PY - 2020 IS - 14 PG - 67 SN - 1420-3049 DO - 10.3390/molecules25143276 UR - https://m2.mtmt.hu/api/publication/31417953 ID - 31417953 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Shankar, Sudha AU - Rahim, Junaid Ur AU - Rai, Rajkishor TI - Self-Assembly in Peptides Containing β-and γ-amino Acids JF - CURRENT PROTEIN AND PEPTIDE SCIENCE J2 - CURR PROTEIN PEPT SCI VL - 21 PY - 2020 IS - 6 SP - 584 EP - 597 PG - 14 SN - 1389-2037 DO - 10.2174/1389203721666200127112244 UR - https://m2.mtmt.hu/api/publication/31694069 ID - 31694069 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Bera, Santu AU - Gazit, Ehud TI - Self-assembly of Functional Nanostructures by Short Helical Peptide Building Block JF - PROTEIN AND PEPTIDE LETTERS J2 - PROTEIN PEPTIDE LETT VL - 26 PY - 2019 IS - 2 SP - 88 EP - 97 PG - 10 SN - 0929-8665 DO - 10.2174/0929866525666180917163142 UR - https://m2.mtmt.hu/api/publication/30956747 ID - 30956747 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Chan, Michael Ho-Yeung AU - Leung, Sammual Yu-Lut AU - Yam, Vivian Wing-Wah TI - Rational Design of Multi-Stimuli-Responsive Scaffolds: Synthesis of Luminescent Oligo(ethynylpyridine)-Containing Alkynylplatinum(II) Polypyridine Foldamers Stabilized by Pt···Pt Interactions JF - JOURNAL OF THE AMERICAN CHEMICAL SOCIETY J2 - J AM CHEM SOC VL - 141 PY - 2019 IS - 31 SP - 12312 EP - 12321 PG - 10 SN - 0002-7863 DO - 10.1021/jacs.9b04447 UR - https://m2.mtmt.hu/api/publication/30961080 ID - 30961080 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Nekkaa, Imane AU - Bogdán, Dóra AU - Gáti, Tamás AU - Béni, Szabolcs AU - Juhász, Tünde AU - Palkó, Márta AU - Paragi, Gábor AU - Tóth, Gábor AU - Fülöp, Ferenc AU - Mándity, István TI - Flow-chemistry enabled efficient synthesis of β-peptides: backbone topology vs. helix formation JF - CHEMICAL COMMUNICATIONS J2 - CHEM COMMUN VL - 55 PY - 2019 IS - 21 SP - 3061 EP - 3064 PG - 4 SN - 1359-7345 DO - 10.1039/c8cc10147g UR - https://m2.mtmt.hu/api/publication/30535263 ID - 30535263 N1 - 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 AB - Enantiodiscriminative helix formation was observed for beta-peptide H14 helices. This observation is caused by the synperiplanar orientation of H-O atoms which is more unfavorable than those for H-H interaction. The 1,2 H-O interaction leads to the destruction of the helical structure. The introduction of a double C-C bond in the backbone rules out helix formation. LA - English DB - MTMT ER - TY - JOUR AU - Veeresh, Kuruva AU - Gopi, Hosahudya N. TI - Design of Helical Peptide Foldamers through alpha,beta -> beta,gamma Double-Bond Migration JF - ORGANIC LETTERS J2 - ORG LETT VL - 21 PY - 2019 IS - 12 SP - 4500 EP - 4504 PG - 5 SN - 1523-7060 DO - 10.1021/acs.orglett.9b01365 UR - https://m2.mtmt.hu/api/publication/30961081 ID - 30961081 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Goldschmidt Gőz, Viktória AU - Pintér, István AU - Harmat, Veronika AU - Perczel, András TI - Approaches to Pyranuronic β-Sugar Amino Acid Building Blocks of Peptidosaccharide Foldamers JF - EUROPEAN JOURNAL OF ORGANIC CHEMISTRY J2 - EUR J ORG CHEM VL - 2018 PY - 2018 IS - 3 SP - 355 EP - 361 PG - 7 SN - 1434-193X DO - 10.1002/ejoc.201701612 UR - https://m2.mtmt.hu/api/publication/3332123 ID - 3332123 N1 - 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 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. AB - 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. LA - English DB - MTMT ER - TY - THES AU - Nekkaa, Imane TI - The Pharmaceutical Chemical Tendency Towards Continuous-Flow Processing: Novel Chemical Reactivities and Entities PY - 2018 SN - 9798381059410 UR - https://m2.mtmt.hu/api/publication/34839709 ID - 34839709 LA - English DB - MTMT ER - TY - THES AU - Olajos, Gábor TI - Beta-Amino Acid Substitutions in Beta-Sandwich Model Proteins PY - 2018 SN - 9798381064070 UR - https://m2.mtmt.hu/api/publication/34839710 ID - 34839710 LA - English DB - MTMT ER - TY - JOUR AU - Simon, Matthieu AU - Milbeo, Pierre AU - Liu, Hongtao AU - Andre, Christophe AU - Wenger, Emmanuel AU - Martinez, Jean AU - Amblard, Muriel AU - Aubert, Emmanuel AU - Legrand, Baptiste AU - Calmes, Monique TI - 12/10-Helix in Mixed beta-Peptides Alternating Bicyclic and Acyclic beta-Amino Acids: Probing the Relationship between Bicyclic Side Chain and Helix Stability JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 24 PY - 2018 IS - 70 SP - 18795 EP - 18800 PG - 6 SN - 0947-6539 DO - 10.1002/chem.201804404 UR - https://m2.mtmt.hu/api/publication/30378683 ID - 30378683 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Sussman, Fredy AU - Sanchez-Pedregal, Victor M. AU - Estevez, Juan C. AU - Balo, Rosalino AU - Jimenez-Barbero, Jesus AU - Arda, Ana AU - Gimeno, Ana AU - Royo, Miriam AU - Carmen Villaverde, M. AU - Estevez, Ramon J. TI - Environmental Effects Determine the Structure of Potential beta-Amino Acid Based Foldamers JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 24 PY - 2018 IS - 42 SP - 10625 EP - 10629 PG - 5 SN - 0947-6539 DO - 10.1002/chem.201801953 UR - https://m2.mtmt.hu/api/publication/30378685 ID - 30378685 AB - This work shows that hybrid peptides formed by alternating trans-2-aminocyclopentanecarboxylic acid (trans-ACPC) and trans-2-aminocyclohexanecarboxylic acid (trans-ACHC) do not fold in the solvents typically used in the study of their homo-oligomers. Only when the peptides are assayed in SDS micelles are the predicted helical structures obtained. This indicates that the environment could play an equally important role (as the backbone stereochemistry) in determining their fold, possibly by providing a sequestered environment. LA - English DB - MTMT ER - TY - JOUR AU - Chan, Michael Ho-Yeung AU - Ng, Maggie AU - Leung, Sammual Yu-Lut AU - Lam, Wai Han AU - Yam, Vivian Wing-Wah TI - Synthesis of Luminescent Platinum(II) 2,6-Bis-(N-dodecylbenzimidazol-2 '-yl)pyridine Foldamers and Their Supramolecular Assembly and Metallogel Formation JF - JOURNAL OF THE AMERICAN CHEMICAL SOCIETY J2 - J AM CHEM SOC VL - 139 PY - 2017 IS - 25 SP - 8639 EP - 8645 PG - 7 SN - 0002-7863 DO - 10.1021/jacs.7b03635 UR - https://m2.mtmt.hu/api/publication/26744684 ID - 26744684 LA - English DB - MTMT ER - TY - JOUR AU - Del Borgo, Mark P AU - Kulkarni, Ketav AU - Aguilar, Marie-Isabel TI - Unique Functional Materials Derived from beta-Amino Acid Oligomers JF - AUSTRALIAN JOURNAL OF CHEMISTRY J2 - AUST J CHEM VL - 70 PY - 2017 IS - 2 SP - 126 EP - 129 PG - 4 SN - 0004-9425 DO - 10.1071/CH16511 UR - https://m2.mtmt.hu/api/publication/26581834 ID - 26581834 LA - English DB - MTMT ER - TY - JOUR AU - Misra, Rajkumar AU - Raja, K Muruga Poopathi AU - Hofmann, Hans-Joerg AU - Gopi, Hosahudya N TI - Modulating the Structural Properties of alpha,gamma-Hybrid Peptides by alpha-Amino Acid Residues: Uniform 12-Helix Versus "Mixed" 12/10-Helix JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 23 PY - 2017 IS - 65 SP - 16644 EP - 16652 PG - 9 SN - 0947-6539 DO - 10.1002/chem.201703871 UR - https://m2.mtmt.hu/api/publication/27100837 ID - 27100837 LA - English DB - MTMT ER - TY - JOUR AU - Thodupunuri, Prashanth AU - Katukuri, Sirisha AU - Ramakrishna, Kallaganti V S AU - Sharma, Gangavaram V M AU - Kunwar, Ajit C AU - Sarma, Akella V S AU - Hofmann, Hans-Joerg TI - Solvent-Directed Switch of a Left-Handed 10/12-Helix into a Right-Handed 12/10-Helix in Mixed β-Peptides JF - JOURNAL OF ORGANIC CHEMISTRY J2 - J ORG CHEM VL - 82 PY - 2017 IS - 4 SP - 2018 EP - 2031 PG - 14 SN - 0022-3263 DO - 10.1021/acs.joc.6b02856 UR - https://m2.mtmt.hu/api/publication/26581886 ID - 26581886 LA - English DB - MTMT ER - TY - THES AU - Walters, Christopher R. TI - Improving the Usage of Unnatural Amino Acids in Proteins: Thioamides and Other Biophysical Probes PY - 2017 SN - 978-0-355-61827-3 UR - https://m2.mtmt.hu/api/publication/34839711 ID - 34839711 LA - English DB - MTMT ER - TY - JOUR AU - Chin, SL AU - Lu, Q AU - Dane, EL AU - Dominguez, L AU - McKnight, CJ AU - Straub, JE AU - Grinstaff, MW TI - Combined Molecular Dynamics Simulations and Experimental Studies of the Structure and Dynamics of Poly-Amido-Saccharides JF - JOURNAL OF THE AMERICAN CHEMICAL SOCIETY J2 - J AM CHEM SOC VL - 138 PY - 2016 IS - 20 SP - 6532 EP - 6540 PG - 9 SN - 0002-7863 DO - 10.1021/jacs.6b01837 UR - https://m2.mtmt.hu/api/publication/25948521 ID - 25948521 LA - English DB - MTMT ER - TY - JOUR AU - Demizu, Yosuke AU - Okitsu, Koyo AU - Yamashita, Hiroko AU - Doi, Mitsunobu AU - Misawa, Takashi AU - Oba, Makoto AU - Tanaka, Masakazu AU - Kurihara, Masaaki TI - alpha-Helical Structures of Oligopeptides with an Alternating L-Leu-Aib Segment JF - EUROPEAN JOURNAL OF ORGANIC CHEMISTRY J2 - EUR J ORG CHEM VL - 2016 PY - 2016 IS - 16 SP - 2815 EP - 2820 PG - 6 SN - 1434-193X DO - 10.1002/ejoc.201600327 UR - https://m2.mtmt.hu/api/publication/26035014 ID - 26035014 LA - English DB - MTMT ER - TY - JOUR AU - Francesca, Clerici AU - Emanuela, Erba AU - Maria, Luisa Gelmi AU - Sara, Pellegrino TI - Non-standard amino acids and peptides: From self-assembly to nanomaterials JF - TETRAHEDRON LETTERS J2 - TETRAHEDRON LETT VL - 57 PY - 2016 IS - 50 SP - 5540 EP - 5550 PG - 11 SN - 0040-4039 DO - 10.1016/j.tetlet.2016.11.022 UR - https://m2.mtmt.hu/api/publication/26287147 ID - 26287147 LA - English DB - MTMT ER - TY - JOUR AU - Gopalakrishnan, Ranganath AU - Frolov, Andrey I AU - Knerr, Laurent AU - Drury, William J III AU - Valeur, Eric TI - Therapeutic Potential of Foldamers: From Chemical Biology Tools To Drug Candidates? JF - JOURNAL OF MEDICINAL CHEMISTRY J2 - J MED CHEM VL - 59 PY - 2016 IS - 21 SP - 9599 EP - 9621 PG - 23 SN - 0022-2623 DO - 10.1021/acs.jmedchem.6b00376 UR - https://m2.mtmt.hu/api/publication/26393033 ID - 26393033 LA - English DB - MTMT ER - TY - JOUR AU - Sharma, GVM AU - Ravindranath, H AU - Bhaskar, A AU - Sirisha, K AU - Ramakrishna, KVS AU - Sarma, AVS TI - Design and Synthesis of Diastereomeric (3)-Peptides from (R,R)/(S,S)-APyC and (R)/(S)-(3)-Caa: Determination of Enantiomeric Handedness JF - EUROPEAN JOURNAL OF ORGANIC CHEMISTRY J2 - EUR J ORG CHEM VL - 2016 PY - 2016 IS - 1 SP - 168 EP - 175 PG - 8 SN - 1434-193X DO - 10.1002/ejoc.201501053 UR - https://m2.mtmt.hu/api/publication/25404532 ID - 25404532 LA - English DB - MTMT ER - TY - JOUR AU - Shin, Seonho AU - Lee, Mihye AU - Guzei, Ilia A AU - Kang, Young Kee AU - Choi, Soo Hyuk TI - 12/10-Helical beta-Peptide with Dynamic Folding Propensity: Coexistence of Right- and Left-Handed Helices in an Enantiomeric Foldamer JF - JOURNAL OF THE AMERICAN CHEMICAL SOCIETY J2 - J AM CHEM SOC VL - 138 PY - 2016 IS - 40 SP - 13390 EP - 13395 PG - 6 SN - 0002-7863 DO - 10.1021/jacs.6b08235 UR - https://m2.mtmt.hu/api/publication/26226966 ID - 26226966 LA - English DB - MTMT ER - TY - JOUR AU - Gopalan, Romila D AU - Del Borgo, Mark P AU - Mechler, Adam I AU - Perlmutter, Patrick AU - Aguilar, Marie-Isabel TI - Geometrically Precise Building Blocks: the Self-Assembly of beta-Peptides JF - CHEMISTRY & BIOLOGY J2 - CHEM BIOL VL - 22 PY - 2015 IS - 11 SP - 1417 EP - 1423 PG - 7 SN - 1074-5521 DO - 10.1016/j.chembiol.2015.10.005 UR - https://m2.mtmt.hu/api/publication/25371239 ID - 25371239 LA - English DB - MTMT ER - TY - JOUR AU - Kann, N AU - Johansson, JR AU - Beke-Somfai, Tamás TI - Conformational properties of 1,4- and 1,5-substituted 1,2,3-triazole amino acids-building units for peptidic foldamers JF - ORGANIC & BIOMOLECULAR CHEMISTRY J2 - ORG BIOMOL CHEM VL - 13 PY - 2015 IS - 9 SP - 2776 EP - 2785 PG - 10 SN - 1477-0520 DO - 10.1039/c4ob02359e UR - https://m2.mtmt.hu/api/publication/3016896 ID - 3016896 N1 - Cited By :19 Export Date: 17 April 2024 CODEN: OBCRA Correspondence Address: Kann, N.; Department of Chemical and Biological Engineering, Sweden AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Kwon, Sunmi AU - Kang, Philjae AU - Choi, Moon-Gun AU - Choi, Soo Hyuk TI - cis-2-Aminocyclohex-4-enecarboxylic acid as a new building block of helical foldamers JF - NEW JOURNAL OF CHEMISTRY J2 - NEW J CHEM VL - 39 PY - 2015 IS - 5 SP - 3221 EP - 3224 PG - 4 SN - 1144-0546 DO - 10.1039/c4nj02056a UR - https://m2.mtmt.hu/api/publication/24792442 ID - 24792442 LA - English DB - MTMT ER - TY - JOUR AU - Mándity, István AU - Fülöp, Ferenc TI - An overview of peptide and peptoid foldamers in medicinal chemistry JF - EXPERT OPINION ON DRUG DISCOVERY J2 - EXPERT OPIN DRUG DIS VL - 10 PY - 2015 IS - 11 SP - 1163 EP - 1177 PG - 15 SN - 1746-0441 DO - 10.1517/17460441.2015.1076790 UR - https://m2.mtmt.hu/api/publication/2993085 ID - 2993085 LA - English DB - MTMT ER - TY - JOUR AU - Olajos, Gábor AU - Hetényi, Anasztázia AU - Wéber, Edit AU - Németh, Lukács AU - Szakonyi, Zsolt AU - Fülöp, Ferenc AU - Martinek, Tamás TI - Induced Folding of Protein-Sized Foldameric β-Sandwich Models with Core β-Amino Acid Residues JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 21 PY - 2015 IS - 16 SP - 6173 EP - 6180 PG - 8 SN - 0947-6539 DO - 10.1002/chem.201405581 UR - https://m2.mtmt.hu/api/publication/2868602 ID - 2868602 N1 - 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). CAplus AN 2015:484036; MEDLINE PMID: 25677195 (Journal; Article; Research Support, Non-U.S. Gov't); AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Sarkar, R AU - Debnath, M AU - Maji, K AU - Haldar, D TI - Solvent assisted structural diversity: Supramolecular sheet and double helix of a short aromatic γ-peptide JF - RSC ADVANCES J2 - RSC ADV VL - 5 PY - 2015 IS - 93 SP - 76257 EP - 76262 PG - 6 SN - 2046-2069 DO - 10.1039/c5ra12831e UR - https://m2.mtmt.hu/api/publication/25137453 ID - 25137453 LA - English DB - MTMT ER - TY - JOUR AU - Giuliano, MW AU - Maynard, SJ AU - Almeida, AM AU - Guo, L AU - Guzei, IA AU - Spencer, LC AU - Gellman, SH TI - A γ-Amino Acid That Favors 12/10-Helical Secondary Structure in α/γ-Peptides JF - JOURNAL OF THE AMERICAN CHEMICAL SOCIETY J2 - J AM CHEM SOC VL - 136 PY - 2014 IS - 42 SP - 15046 EP - 15053 PG - 8 SN - 0002-7863 DO - 10.1021/ja5076585 UR - https://m2.mtmt.hu/api/publication/24327528 ID - 24327528 LA - English DB - MTMT ER - TY - JOUR AU - Jadhav, Sandip V AU - Misra, Rajkumar AU - Gopi, Hosahudya N TI - Foldamers to Nanotubes: Influence of Amino Acid Side Chains in the Hierarchical Assembly of alpha,gamma(4)-Hybrid Peptide Helices JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 20 PY - 2014 IS - 50 SP - 16523 EP - 16528 PG - 6 SN - 0947-6539 DO - 10.1002/chem.201404961 UR - https://m2.mtmt.hu/api/publication/24777367 ID - 24777367 LA - English DB - MTMT ER - TY - JOUR AU - Johansson, JR AU - Hermansson, E AU - Nordén, B AU - Kann, N AU - Beke-Somfai, Tamás TI - δ-Peptides from RuAAC-derived 1,5-disubstituted triazole units JF - EUROPEAN JOURNAL OF ORGANIC CHEMISTRY J2 - EUR J ORG CHEM VL - 2014 PY - 2014 IS - 13 SP - 2703 EP - 2713 PG - 11 SN - 1434-193X DO - 10.1002/ejoc.201400018 UR - https://m2.mtmt.hu/api/publication/3016900 ID - 3016900 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Lee, W AU - Kwon, S AU - Kang, P AU - Guzei, IA AU - Choi, SH TI - Helical folding of alpha/beta-peptides containing beta-amino acids with an eight-membered ring constraint JF - ORGANIC & BIOMOLECULAR CHEMISTRY J2 - ORG BIOMOL CHEM VL - 12 PY - 2014 IS - 17 SP - 2641 EP - 2644 PG - 4 SN - 1477-0520 DO - 10.1039/c4ob00266k UR - https://m2.mtmt.hu/api/publication/24539870 ID - 24539870 LA - English DB - MTMT ER - TY - JOUR AU - Mándity, István AU - Olasz, Balázs AU - Ötvös, Sándor Balázs AU - Fülöp, Ferenc TI - Continuous-Flow Solid-Phase Peptide Synthesis: A Revolutionary Reduction of the Amino Acid Excess JF - CHEMSUSCHEM J2 - CHEMSUSCHEM VL - 7 PY - 2014 IS - 11 SP - 3172 EP - 3176 PG - 5 SN - 1864-5631 DO - 10.1002/cssc.201402436 UR - https://m2.mtmt.hu/api/publication/2730808 ID - 2730808 N1 - 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 award of a Janos Bolyai scholarship from the Hungarian Academy of Sciences. ISSN:1864-5631 LA - English DB - MTMT ER - TY - JOUR AU - Mándity, István AU - Monsignori, A AU - Fülöp, Lívia AU - Forró, Enikő AU - Fülöp, Ferenc TI - Exploiting aromatic interactions for β-peptide foldamer helix stabilization: A significant design element JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 20 PY - 2014 IS - 16 SP - 4591 EP - 4597 PG - 7 SN - 0947-6539 DO - 10.1002/chem.201304448 UR - https://m2.mtmt.hu/api/publication/2583563 ID - 2583563 LA - English DB - MTMT ER - TY - JOUR AU - Roy, A AU - Kotmale, AS AU - Gawade, RL AU - Puranik, VG AU - Rajamohanan, PR AU - Sanjayan, GJ TI - Probing the folding induction ability of orthanilic acid in peptides: some observations JF - RSC ADVANCES J2 - RSC ADV VL - 4 PY - 2014 IS - 25 SP - 13018 EP - 13025 PG - 8 SN - 2046-2069 DO - 10.1039/c3ra47039c UR - https://m2.mtmt.hu/api/publication/23785370 ID - 23785370 LA - English DB - MTMT ER - TY - THES AU - Sarah, Elizabeth Stidham TI - Synthesis and characterization of carboxylate-containing polymers for biomedical applications PY - 2014 UR - https://m2.mtmt.hu/api/publication/26287263 ID - 26287263 LA - English DB - MTMT ER - TY - JOUR AU - Sharma, Gangavaram V M AU - Ravindranath, Hajari AU - Bhaskar, Akkala AU - Jeelani, Basha Shaik AU - Gurava, Reddy Potti Reddy Gari AU - Sirisha, Katukuri AU - Sarma, Akella V S AU - Hofmann, Hans-Joerg TI - Design and study of peptides containing 1:1 left- and right-handed helical patterns from aminopyrancarboxylic acids. JF - EUROPEAN JOURNAL OF ORGANIC CHEMISTRY J2 - EUR J ORG CHEM VL - 2014 PY - 2014 IS - 20 SP - 4295 EP - 4308 PG - 14 SN - 1434-193X DO - 10.1002/ejoc.201402123 UR - https://m2.mtmt.hu/api/publication/24222995 ID - 24222995 LA - English DB - MTMT ER - TY - JOUR AU - Sharma, GVM AU - Yadav, TA AU - Marumudi, K AU - Thodupunuri, P AU - Reddy, PP AU - Kunwar, AC TI - Three-Residue Turn in β-Peptides Nucleated by a 12/10 Helix JF - CHEMISTRY-AN ASIAN JOURNAL J2 - CHEM-ASIAN J VL - 9 PY - 2014 IS - 11 SP - 3153 EP - 3162 PG - 10 SN - 1861-4728 DO - 10.1002/asia.201402465 UR - https://m2.mtmt.hu/api/publication/24327538 ID - 24327538 LA - English DB - MTMT ER - TY - JOUR AU - Stidham, SE AU - Chin, SL AU - Dane, EL AU - Grinstaff, MW TI - Carboxylated Glucuronic Poly-amido-saccharides as Protein Stabilizing Agents JF - JOURNAL OF THE AMERICAN CHEMICAL SOCIETY J2 - J AM CHEM SOC VL - 136 PY - 2014 IS - 27 SP - 9544 EP - 9547 PG - 4 SN - 0002-7863 DO - 10.1021/ja5036804 UR - https://m2.mtmt.hu/api/publication/24137307 ID - 24137307 LA - English DB - MTMT ER - TY - JOUR AU - Andre, Christophe AU - Legrand, Baptiste AU - Moulat, Laure AU - Wenger, Emmanuel AU - Didierjean, Claude AU - Aubert, Emmanuel AU - Averlant-Petit, Marie Christine AU - Martinez, Jean AU - Amblard, Muriel AU - Calmes, Monique TI - Mixed Oligoureas Based on Constrained Bicyclic and Acyclic beta-Amino Acids Derivatives: On the Significance of the Subunit Configuration for Folding JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 19 PY - 2013 IS - 50 SP - 16963 EP - 16971 PG - 9 SN - 0947-6539 DO - 10.1002/chem.201302829 UR - https://m2.mtmt.hu/api/publication/24709148 ID - 24709148 LA - English DB - MTMT ER - TY - JOUR AU - Choi, SH AU - Ivancic, M AU - Guzei, IA AU - Gellman, SH TI - Structural Characterization of Peptide Oligomers Containing (1R,2S)-2-Aminocyclohexanecarboxylic Acid (cis-ACHC) JF - EUROPEAN JOURNAL OF ORGANIC CHEMISTRY J2 - EUR J ORG CHEM VL - 2013 PY - 2013 IS - 17 SP - 3464 EP - 3469 PG - 6 SN - 1434-193X DO - 10.1002/ejoc.201300118 UR - https://m2.mtmt.hu/api/publication/23202867 ID - 23202867 LA - English DB - MTMT ER - TY - JOUR AU - Giuliano, MW AU - Maynard, SJ AU - Almeida, AM AU - Reidenbach, AG AU - Guo, L AU - Ulrich, EC AU - Guzei, IA AU - Gellman, SH TI - Evaluation of a Cyclopentane-Based gamma-Amino Acid for the Ability to Promote alpha/gamma-Peptide Secondary Structure JF - JOURNAL OF ORGANIC CHEMISTRY J2 - J ORG CHEM VL - 78 PY - 2013 IS - 24 SP - 12351 EP - 12361 PG - 11 SN - 0022-3263 DO - 10.1021/jo401501g UR - https://m2.mtmt.hu/api/publication/23616893 ID - 23616893 LA - English DB - MTMT ER - TY - JOUR AU - Jadhav, SV AU - Bandyopadhyay, A AU - Gopi, HN TI - Protein secondary structure mimetics: crystal conformations of alpha/gamma(4)-hybrid peptide 12-helices with proteinogenic side chains and their analogy with alpha- and beta-peptide helices JF - ORGANIC & BIOMOLECULAR CHEMISTRY J2 - ORG BIOMOL CHEM VL - 11 PY - 2013 IS - 3 SP - 509 EP - 514 PG - 6 SN - 1477-0520 DO - 10.1039/c2ob26805a UR - https://m2.mtmt.hu/api/publication/23041670 ID - 23041670 LA - English DB - MTMT ER - TY - THES AU - JOHAN, R JOHANSSON TI - Synthesis of Nitrogen Heterocycles and Ruthenium Complexes PB - Chalmers Tekniska Hogskola (Sweden) PY - 2013 SP - 85 UR - https://m2.mtmt.hu/api/publication/24556726 ID - 24556726 LA - English DB - MTMT ER - TY - JOUR AU - Kale, SS AU - Priya, G AU - Kotmale, AS AU - Gawade, RL AU - Puranik, VG AU - Rajamohanan, PR AU - Sanjayan, GJ TI - Orthanilic acid-promoted reverse turn formation in peptides JF - CHEMICAL COMMUNICATIONS J2 - CHEM COMMUN VL - 49 PY - 2013 IS - 22 SP - 2222 EP - 2224 PG - 3 SN - 1359-7345 DO - 10.1039/c3cc40522b UR - https://m2.mtmt.hu/api/publication/23051561 ID - 23051561 LA - English DB - MTMT ER - TY - CHAP AU - Kimura, Shunsaku AU - Ueda, Motoki ED - Aleman, C ED - Bianco, A ED - Venanzi, M TI - Molecular architecture with peptide assembling for nanomaterials. T2 - Peptide Materials: From Nanostuctures to Applications PB - John Wiley & Sons CY - Chichester SN - 9781118592410 PB - John Wiley & Sons PY - 2013 SP - 149 EP - 170 PG - 22 DO - 10.1002/9781118592403.ch5 UR - https://m2.mtmt.hu/api/publication/26796642 ID - 26796642 LA - English DB - MTMT ER - TY - JOUR AU - Lee, Mihye AU - Shim, Jihyun AU - Kang, Philjae AU - Guzei, Ilia A AU - Choi, Soo Hyuk TI - Structural Characterization of α/β-Peptides having Alternating Residues: X-ray Structures of the 11/9-Helix from Crystals of Racemic Mixtures JF - ANGEWANDTE CHEMIE-INTERNATIONAL EDITION J2 - ANGEW CHEM INT EDIT VL - 52 PY - 2013 IS - 48 SP - 12564 EP - 12567 PG - 4 SN - 1433-7851 DO - 10.1002/anie.201306404 UR - https://m2.mtmt.hu/api/publication/24877170 ID - 24877170 LA - English DB - MTMT ER - TY - THES AU - Martinek, Tamás TI - Peptid foldamerek: szerkezet és alkalmazás PB - Szegedi Tudományegyetem (SZTE) PY - 2013 UR - https://m2.mtmt.hu/api/publication/26287265 ID - 26287265 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Molski, MA AU - Goodman, JL AU - Chou, FC AU - Baker, D AU - Das, R AU - Schepartz, A TI - Remodeling a beta-peptide bundle JF - CHEMICAL SCIENCE J2 - CHEM SCI VL - 4 PY - 2013 IS - 1 SP - 319 EP - 324 PG - 6 SN - 2041-6520 DO - 10.1039/c2sc21117c UR - https://m2.mtmt.hu/api/publication/22813656 ID - 22813656 LA - English DB - MTMT ER - TY - JOUR AU - Berlicki, Ł AU - Pilsl, L AU - Wéber, Edit AU - Mándity, István AU - Cabrele, C AU - Martinek, Tamás AU - Fülöp, Ferenc AU - Reiser, O TI - Unique α,β- and α,α,β,β-peptide foldamers based on cis-β-aminocyclopentanecarboxylic acid JF - ANGEWANDTE CHEMIE-INTERNATIONAL EDITION J2 - ANGEW CHEM INT EDIT VL - 51 PY - 2012 IS - 9 SP - 2208 EP - 2212 PG - 5 SN - 1433-7851 DO - 10.1002/anie.201107702 UR - https://m2.mtmt.hu/api/publication/1926671 ID - 1926671 N1 - 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 University Bochum, 44801 Bochum, Germany Paris Lodron University Salzburg, Department of Molecular Biology, Billrothstrasse 11, 5020 Salzburg, Austria Cited By :69 Export Date: 1 October 2021 CODEN: ACIEF Correspondence Address: Martinek, T.A.; Institute of Pharmaceutical Chemistry, , 6720 Szeged, Hungary; email: martinek@pharm.u-szeged.hu Chemicals/CAS: cycloleucine, 52-52-8; Cycloleucine, 52-52-8; Peptides AB - Waterproof: cis-β-Aminocylopentanecarboxylic acid is a highly suitable building block for the synthesis of α,β- and α,α,β, β-peptides that have unique helical structures with high stability in methanol and aqueous media. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. LA - English DB - MTMT ER - TY - JOUR AU - Dane, EL AU - Grinstaff, MW TI - Poly-amido-saccharides: Synthesis via Anionic Polymerization of a beta-Lactam Sugar Monomer JF - JOURNAL OF THE AMERICAN CHEMICAL SOCIETY J2 - J AM CHEM SOC VL - 134 PY - 2012 IS - 39 SP - 16255 EP - 16264 PG - 10 SN - 0002-7863 DO - 10.1021/ja305900r UR - https://m2.mtmt.hu/api/publication/24248717 ID - 24248717 LA - English DB - MTMT ER - TY - JOUR AU - Gorrea, E AU - Pohl, G AU - Nolis, P AU - Celis, S AU - Burusco, KK AU - Branchadell, V AU - Perczel, András AU - Ortuño, RM TI - Secondary structure of short β-peptides as the chiral expression of monomeric building units: A rational and predictive model JF - JOURNAL OF ORGANIC CHEMISTRY J2 - J ORG CHEM VL - 77 PY - 2012 IS - 21 SP - 9795 EP - 9806 PG - 12 SN - 0022-3263 DO - 10.1021/jo302034b UR - https://m2.mtmt.hu/api/publication/2129197 ID - 2129197 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Martinek, Tamás AU - Fülöp, Ferenc TI - Peptidic foldamers: ramping up diversity JF - CHEMICAL SOCIETY REVIEWS J2 - CHEM SOC REV VL - 41 PY - 2012 IS - 2 SP - 687 EP - 702 PG - 16 SN - 0306-0012 DO - 10.1039/c1cs15097a UR - https://m2.mtmt.hu/api/publication/1842290 ID - 1842290 N1 - 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. CAplus AN 2012:19612; MEDLINE PMID: 21769415 (Journal; General Review; Article; Research Support, Non-U.S. Gov't; Review); AB - 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). LA - English DB - MTMT ER - TY - JOUR AU - Opsitnick, E.A. AU - Jiang, X. AU - Hollenbeck, A.N. AU - Lee, D. TI - Hydrogen-bond-assisted helical folding of propeller-shaped molecules: Effects of extended π-conjugation on chiral selection, conformational stability, and exciton coupling JF - EUROPEAN JOURNAL OF ORGANIC CHEMISTRY J2 - EUR J ORG CHEM VL - 2012 PY - 2012 IS - 4 SP - 708 EP - 720 PG - 13 SN - 1434-193X DO - 10.1002/ejoc.201101351 UR - https://m2.mtmt.hu/api/publication/32696670 ID - 32696670 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Pihlaja, Kalevi AU - Kleinpeter, H C Erich TI - Professor Ferenc Fulop - a tribute. JF - ARKIVOC J2 - ARKIVOC VL - 2012 PY - 2012 IS - 5 SP - 1 EP - 5 PG - 5 SN - 1551-7012 DO - 10.3998/ark.5550190.0013.501 UR - https://m2.mtmt.hu/api/publication/24452654 ID - 24452654 LA - English DB - MTMT ER - TY - JOUR AU - Prabhakaran, P AU - Azzarito, V AU - Jacobs, T AU - Hardie, MJ AU - Kilner, CA AU - Edwards, TA AU - Warriner, SL AU - Wilson, AJ TI - Conformational properties of O-alkylated benzamides JF - TETRAHEDRON J2 - TETRAHEDRON VL - 68 PY - 2012 IS - 23 SP - 4485 EP - 4491 PG - 7 SN - 0040-4020 DO - 10.1016/j.tet.2011.11.078 UR - https://m2.mtmt.hu/api/publication/22405393 ID - 22405393 LA - English DB - MTMT ER - TY - JOUR AU - Szolnoki, Éva Tünde AU - Hetényi, Anasztázia AU - Martinek, Tamás AU - Szakonyi, Zsolt AU - Fülöp, Ferenc TI - Self-association-driven transition of the β-peptidic H12 helix to the H18 helix JF - ORGANIC & BIOMOLECULAR CHEMISTRY J2 - ORG BIOMOL CHEM VL - 10 PY - 2012 IS - 2 SP - 255 EP - 259 PG - 5 SN - 1477-0520 DO - 10.1039/c1ob06627g UR - https://m2.mtmt.hu/api/publication/1842289 ID - 1842289 AB - Various patterns of foldameric oligomers formed by trans-ABHC ((1S,2S,3S, 5S)-2-amino-6,6-dimethylbicyclo-[3.3.1]heptane-3-carboxylic acid) and beta(3)-hSer residues were studied. NMR, ECD and molecular modelling demonstrated that octameric and nonameric sequences with multiple i-i+3 ABHC pair repulsions attain the beta-H18 helix in CD3OH. As a close relative of the alpha-helix, this helix type is stabilized by i-i+4 backbone H-bond interactions. The formation of the beta-H18 helix was found to be solvent-and concentration-dependent. Upon dilution, the beta-H18 -> beta-H12 helix transition was revealed by concentration-dependent ECD, DOSY-NMR and TEM measurements. LA - English DB - MTMT ER - TY - THES AU - Wéber, Edit TI - Investigation of protein–ligand interactions of targets with solvent-exposed binding sites PB - Szegedi Tudományegyetem (SZTE) PY - 2012 SP - 56 DO - 10.14232/phd.1475 UR - https://m2.mtmt.hu/api/publication/2786402 ID - 2786402 LA - English DB - MTMT ER - TY - JOUR AU - Declerck, V AU - Aitken, DJ TI - A refined synthesis of enantiomerically pure 2-aminocyclobutanecarboxylic acids JF - AMINO ACIDS J2 - AMINO ACIDS VL - 41 PY - 2011 IS - 3 SP - 587 EP - 595 PG - 9 SN - 0939-4451 DO - 10.1007/s00726-011-0918-y UR - https://m2.mtmt.hu/api/publication/21529827 ID - 21529827 LA - English DB - MTMT ER - TY - JOUR AU - Kodama, K AU - Sugawara, K AU - Hirose, T TI - Synthesis of Chiral 1,3-Diamines Derived from cis-2-Benzamidocyclohexanecarboxylic Acid and Their Application in the Cu-Catalyzed Enantioselective Henry Reaction JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 17 PY - 2011 IS - 48 SP - 13584 EP - 13592 PG - 9 SN - 0947-6539 DO - 10.1002/chem.201102136 UR - https://m2.mtmt.hu/api/publication/23594320 ID - 23594320 LA - English DB - MTMT ER -