TY - JOUR AU - Nekkaa, Imane AU - Palkó, Márta AU - Mándity, István AU - Fülöp, Ferenc TI - Continuous-flow retro-Diels-Alder reaction: an efficient method for the preparation of pyrimidinone derivatives JF - BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY J2 - BEILSTEIN J ORG CHEM VL - 14 PY - 2018 SP - 318 EP - 324 PG - 7 SN - 1860-5397 DO - 10.3762/bjoc.14.20 UR - https://m2.mtmt.hu/api/publication/3374074 ID - 3374074 N1 - Funding Agency and Grant Number: Hungarian Research Foundation (OTKA) [K 115731]; [GINOP-2.3.2-15-2016-00014] 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 project is acknowledged. AB - The syntheses of various pyrimidinones as potentially bioactive products by means of the highly controlled continuous-flow retro-Diels-Alder reaction of condensed pyrimidinone derivatives are presented. Noteworthy, the use of this approach allowed us to rapidly screen a selection of conditions and quickly confirm the viability of preparing the desired pyrimidinones in short reaction times. Yields typically higher than those published earlier using conventional batch or microwave processes were achieved. LA - English DB - MTMT ER - TY - JOUR AU - Nekkaa, Imane AU - Palkó, Márta AU - Mándity, István AU - Miklós, Ferenc AU - Fülöp, Ferenc TI - Continuous-Flow retro-Diels–Alder Reaction: A Process Window for Designing Heterocyclic Scaffolds JF - EUROPEAN JOURNAL OF ORGANIC CHEMISTRY J2 - EUR J ORG CHEM VL - 2018 PY - 2018 IS - 32 SP - 4456 EP - 4464 PG - 9 SN - 1434-193X DO - 10.1002/ejoc.201800682 UR - https://m2.mtmt.hu/api/publication/27671648 ID - 27671648 N1 - Funding Agency and Grant Number: Hungarian Research Foundation (OTKA) [K 115731]; [GINOP-2.3.2-15-2016-00014] Funding text: We are grateful to the Hungarian Research Foundation (OTKA No. K 115731). The financial support from the GINOP-2.3.2-15-2016-00014 project is acknowledged. Institute of Pharmaceutical Chemistry, University of Szeged, Eötvös u. 6, Szeged, 6720, Hungary Institute of Organic Chemistry, Semmelweis University, Hogyes Endre u. 7, Budapest, 1092, Hungary MTA TTK Lendület Artificial Transporter Research Group, Institute of Materials and Environmental Chemistry, Hungarian Academy of Sciences, Magyar Tudosok krt. 2, Budapest, 1117, Hungary MTA-SZTE Stereochemistry Research Group, Hungarian Academy of Sciences, Eötvös u. 6, Szeged, 6720, Hungary Cited By :4 Export Date: 25 July 2020 CODEN: EJOCF Correspondence Address: Fülöp, F.; Institute of Pharmaceutical Chemistry, University of Szeged, Eötvös u. 6, Hungary; email: fulop@pharm.u-szeged.hu LA - English DB - MTMT ER - TY - JOUR AU - Bartus, Éva AU - Hegedüs, Zsófia AU - Wéber, Edit AU - Csipak, Brigitta AU - Szakonyi, Gerda AU - Martinek, Tamás TI - De Novo Modular Development of a Foldameric Protein-Protein Interaction Inhibitor for Separate Hot Spots: A Dynamic Covalent Assembly Approach JF - CHEMISTRYOPEN J2 - CHEMISTRYOPEN VL - 6 PY - 2017 IS - 2 SP - 236 EP - 241 PG - 6 SN - 2191-1363 DO - 10.1002/open.201700012 UR - https://m2.mtmt.hu/api/publication/3213189 ID - 3213189 LA - English DB - MTMT ER - TY - JOUR AU - Mándity, István AU - Ötvös, Sándor Balázs AU - Szőllősi, György AU - Fülöp, Ferenc TI - Harnessing the Versatility of Continuous-Flow Processes: Selective and Efficient Reactions JF - CHEMICAL RECORD J2 - CHEM REC VL - 16 PY - 2016 IS - 3 SP - 1018 EP - 1033 PG - 16 SN - 1527-8999 DO - 10.1002/tcr.201500286 UR - https://m2.mtmt.hu/api/publication/3048904 ID - 3048904 N1 - Funding Agency and Grant Number: Hungarian Research Foundation (OTKA)Orszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [K 115731, K 109278]; Janos Bolyai scholarshipHungarian Academy of Sciences; Hungarian Academy of SciencesHungarian Academy of Sciences Funding text: We are grateful to the Hungarian Research Foundation (OTKA Nos. K 115731 and K 109278). S.B.O. acknowledges the award of a Janos Bolyai scholarship and a postdoctoral fellowship (Postdoctoral Research Program) from the Hungarian Academy of Sciences. ISSN:1527-8999 LA - English DB - MTMT ER - TY - JOUR AU - Mándity, István AU - Ötvös, Sándor Balázs AU - Fülöp, Ferenc TI - Strategic application of residence-time control in continuous-flow reactors JF - CHEMISTRYOPEN J2 - CHEMISTRYOPEN VL - 4 PY - 2015 IS - 3 SP - 212 EP - 223 PG - 12 SN - 2191-1363 DO - 10.1002/open.201500018 UR - https://m2.mtmt.hu/api/publication/2860289 ID - 2860289 N1 - Institute of Pharmaceutical Chemistry, University of Szeged, Eötvös u. 6, Szeged, H-6720, Hungary MTA-SZTE Stereochemistry Research Group, Hungarian Academy of Sciences, Eötvös u. 6, Szeged, H-6720, Hungary Cited By :55 Export Date: 21 February 2022 CODEN: CHOPC Correspondence Address: Fülöp, F.; Institute of Pharmaceutical Chemistry, Eötvös u. 6, Hungary 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 - Ötvös, László AU - Wade, JD TI - Current challenges in peptide-based drug discovery. JF - FRONTIERS IN CHEMISTRY J2 - FRONT CHEM VL - 2 PY - 2014 PG - 4 SN - 2296-2646 DO - 10.3389/fchem.2014.00062 UR - https://m2.mtmt.hu/api/publication/3010570 ID - 3010570 N1 - Összes idézések száma a WoS-ban: 0 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 - 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 - Mándity, István AU - Fülöp, Lívia AU - Vass, Elemér AU - Tóth, Gábor AU - Martinek, Tamás AU - Fülöp, Ferenc TI - Building β-Peptide H10/12 Foldamer Helices with Six-Membered Cyclic Side-Chains: Fine-Tuning of Folding and Self-Assembly JF - ORGANIC LETTERS J2 - ORG LETT VL - 12 PY - 2010 IS - 23 SP - 5584 EP - 5587 PG - 4 SN - 1523-7060 DO - 10.1021/ol102494m UR - https://m2.mtmt.hu/api/publication/1412123 ID - 1412123 AB - The ability of the beta-peptidic H10/12 helix to tolerate side-chains containing six-membered alicyclic rings was studied. cis-2-Aminocyclohex-3-ene carboxylic acid (cis-ACHEC) res dues afforded H10/12 helix formation with alternating backbone configuration. Conformational polymorphism was observed for the alternating cis-ACHC hexamer, where chemical exchange takes place between the major left-handed H10/12 helix and a minor folded conformation. The hydrophobically driven self-assembly was achieved for the cis-ACHC-containing helix which was observed as vesicles similar to 100 nm in diameter. LA - English DB - MTMT ER - TY - JOUR AU - Mándity, István AU - Wéber, Edit AU - Martinek, Tamás AU - Olajos, Gábor AU - Tóth, Gábor AU - Vass, Elemér AU - Fülöp, Ferenc TI - Design of Peptidic Foldamer Helices: A Stereochemical Patterning Approach JF - ANGEWANDTE CHEMIE-INTERNATIONAL EDITION J2 - ANGEW CHEM INT EDIT VL - 48 PY - 2009 IS - 12 SP - 2171 EP - 2175 PG - 5 SN - 1433-7851 DO - 10.1002/anie.200805095 UR - https://m2.mtmt.hu/api/publication/1232853 ID - 1232853 N1 - Institutes of Pharmaceutical Chemistry and Medical Chemistry, Universitiy of Szeged, Etvs u. 6, 6720 Szeged, Hungary Department of Organic Chemistry, Etvs Loránd University, Pázmány P. s. 1A, 1117 Budapest, Hungary Cited By :101 Export Date: 5 April 2024 CODEN: ACIEA Correspondence Address: Mándity, I. M.; Institutes of Pharmaceutical Chemistry and Medical Chemistry, Etvs u. 6, 6720 Szeged, Hungary LA - English DB - MTMT ER - TY - JOUR AU - Fülöp, Ferenc AU - Martinek, Tamás AU - Tóth, Gábor TI - Application of alicyclic beta-amino acids in peptide chemistry JF - CHEMICAL SOCIETY REVIEWS J2 - CHEM SOC REV VL - 35 PY - 2006 IS - 4 SP - 323 EP - 334 PG - 12 SN - 0306-0012 DO - 10.1039/B501173F UR - https://m2.mtmt.hu/api/publication/1012938 ID - 1012938 N1 - Megjegyzés-21956224 Z9: 133 WC: Chemistry, Multidisciplinary Megjegyzés-21957808 Z9: 133 WC: Chemistry, Multidisciplinary CAplus AN 2006:279672; MEDLINE PMID: 16565749 (Journal; General Review; Article; Research Support, Non-U.S. Gov't; Review); AB - The self-organizing beta-peptides have attracted considerable interest in the fields of foldamer chemistry and biochemistry. These compounds exhibit various stable secondary structure motifs that can be exploited to construct biologically active substances and nanostructured tertiary structures. The secondary structures can be controlled via the beta-amino acid sequence, and cyclic beta-amino acid residues play a crucial role in the design. The most important procedures for the preparation of cyclic beta-amino acid monomers and peptides are discussed in this tutorial review. Besides the secondary structure design principles, the methods of folded structure detection are surveyed. LA - English DB - MTMT ER - TY - JOUR AU - Martinek, Tamás AU - Mándity, István AU - Fülöp, Lívia AU - Tóth, Gábor AU - Vass, Elemér AU - Hollósi, Miklós AU - Forró, Enikő AU - Fülöp, Ferenc TI - Effects of the alternating backbone configuration on the secondary structure and self-assembly of beta-peptides JF - JOURNAL OF THE AMERICAN CHEMICAL SOCIETY J2 - J AM CHEM SOC VL - 128 PY - 2006 IS - 41 SP - 13539 EP - 13544 PG - 6 SN - 0002-7863 DO - 10.1021/ja063890c UR - https://m2.mtmt.hu/api/publication/1078988 ID - 1078988 AB - Heterochiral homo-oligomers with alternating backbone configurations were constructed by using the different enantiomers of the cis- and trans-2-aminocyclopentanecarboxylic acid (ACPC) monomers. Molecular modeling and the spectroscopic techniques (NMR, ECD, and VCD) unequivocally proved that the alternating heterochiral cis-ACPC sequences form an H10/12 helix, where extra stabilization can be achieved via the cyclic side chains. The ECD and TEM measurements, together with molecular modeling, revealed that the alternating heterochiral trans-ACPC oligomers tend to attain a polar-strand secondary structure in solution, which can self-assemble into nanostructured fibrils. The observations indicate that coverage of all the possible secondary structures (various helix types and strand-mimicking conformations) can be attained with the help of cyclic beta-amino acid diastereomers. A relationship has been established between the backbone chirality pattern and the prevailing secondary structure, which underlines the role of stereochemical control in the beta-peptide secondary structure design and may contribute to future biological applications. LA - English DB - MTMT ER - TY - JOUR AU - Hetényi, Anasztázia AU - Mándity, István AU - Martinek, Tamás AU - Tóth, Gábor AU - Fülöp, Ferenc TI - Chain-length-dependent helical motifs and self-association of beta-peptides with constrained side chains JF - JOURNAL OF THE AMERICAN CHEMICAL SOCIETY J2 - J AM CHEM SOC VL - 127 PY - 2005 IS - 2 SP - 547 EP - 553 PG - 7 SN - 0002-7863 DO - 10.1021/ja0475095 UR - https://m2.mtmt.hu/api/publication/1012850 ID - 1012850 N1 - Megjegyzés-21956229 Z9: 53 WC: Chemistry, Multidisciplinary AB - Homo-oligomers constructed by using trans-2-aminocyclohexanecarboxylic acid monomers without protecting groups were studied. Both ab initio theory and NMR measurements showed that the tetramer tends to adopt a 10-helix motif, while the pentamer and hexamer form the known 14-helix. It was concluded that the conformationally constrained backbone is flexible enough to afford both 10-helical and 14-helical motifs, this observation in turn providing evidence of the true folding process. Self-association or the helical units was also detected, and the results of variable-temperature diffusion NMR measurements strongly suggested the presence of helical bundles in methanol solution. LA - English DB - MTMT ER -