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 - Forró, Enikő AU - Fülöp, Ferenc TI - The First Direct Enzymatic Hydrolysis of Alicyclic Beta-amino Esters: A Route to Enantiopure Cis And Trans Beta-amino Acids JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 13 PY - 2007 IS - 22 SP - 6397 EP - 6401 PG - 5 SN - 0947-6539 DO - 10.1002/chem.200700257 UR - https://m2.mtmt.hu/api/publication/1085087 ID - 1085087 AB - The first direct enzymatic method is reported for the synthesis of cis and trans P-amino acid enantiomers through the lipase-catalyzed enantioselective hydrolysis of alicyclic beta-amino esters in organic media. High enantioselectivities (E usually > 100) were observed when the Candida antarctica lipase B catalyzed reactions were performed with H2O (0.5 equivalents) in iPr(2)O at 65 degrees C. The resolved products, obtained in good yields (>= 42%), could be easily separated. 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 - Jones, Richard AU - Godorhazy, L AU - Varga, N AU - Szalay, D AU - Urge, L AU - Darvas, Ferenc TI - Continuous-flow high pressure hydrogenation reactor for optimization and high-throughput synthesis JF - JOURNAL OF COMBINATORIAL CHEMISTRY J2 - J COMB CHEM VL - 8 PY - 2006 IS - 1 SP - 110 EP - 116 PG - 7 SN - 1520-4766 DO - 10.1021/cc050107o UR - https://m2.mtmt.hu/api/publication/3038970 ID - 3038970 AB - This paper reports on a novel continuous-flow hydrogenation reactor and its integration with a liquid handler to generate a fully automated high-throughput hydrogenation system for library synthesis. The reactor, named the H-Cube, combines endogenous hydrogen generation from the electrolysis of water with a continuous flow-through system. The system makes significant advances over current batch hydrogenation reactors in terms of safety, reaction validation efficiency, and rates of reaction. The hydrogenation process is described along with a detailed description of the device's main parts. The reduction of a series of functional groups, varying in difficulty up to 70 °C and 70 bar are also described. The paper concludes with the integration of the device into an automated liquid handler followed by the reduction of a nitro compound in a high throughput manner. The system is fully automated and can conduct 5 reactions in the time it takes to perform and workup one reaction manually on a standard batch reactor. © 2006 American Chemical Society. LA - English DB - MTMT ER - TY - JOUR AU - Martinek, Tamás AU - Hetényi, Anasztázia AU - Fülöp, Lívia AU - Mándity, István AU - Tóth, Gábor AU - Dékány, Imre AU - Fülöp, Ferenc TI - Secondary structure dependent self-assembly of beta-peptides into nanosized fibrils and membranes JF - ANGEWANDTE CHEMIE-INTERNATIONAL EDITION J2 - ANGEW CHEM INT EDIT VL - 45 PY - 2006 IS - 15 SP - 2396 EP - 2400 PG - 5 SN - 1433-7851 DO - 10.1002/anie.200504158 UR - https://m2.mtmt.hu/api/publication/1012935 ID - 1012935 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 - TY - JOUR AU - Martinek, Tamás AU - Fülöp, Ferenc TI - Side-chain control of beta-peptide secondary structures - Design principles JF - EUROPEAN JOURNAL OF BIOCHEMISTRY J2 - EUR J BIOCHEM VL - 270 PY - 2003 IS - 18 SP - 3657 EP - 3666 PG - 10 SN - 0014-2956 DO - 10.1046/j.1432-1033.2003.03756.x UR - https://m2.mtmt.hu/api/publication/1013519 ID - 1013519 N1 - Cited By :147 Export Date: 27 September 2021 CODEN: EJBCA Correspondence Address: Fülöp, F.; Inst. of Pharmaceutical Chemistry, Eotvos u. 6, Szeged, Hungary; email: fulop@pharma.szote.u-szeged.hu Chemicals/CAS: Amino Acids; Peptides; Solvents AB - As one of the most important families of non-natural polymers with the propensity to form well-defined secondary structures, the beta-peptides are attracting increasing attention. The compounds incorporating beta-amino acid residues have found various applications in medicinal chemistry and biochemistry. The conformational pool of beta-peptides comprises several periodic folded conformations, which can be classified as helices, and nonpolar and polar strands. The latter two are prone to form pleated sheets. The numerous studies that have been performed on the side-chain dependence of the stability of the folded structures allow certain conclusions concerning the principles of design of the beta-peptide foldamers. The folding propensity is influenced by local torsional, side-chain to backbone and long-range side-chain interactions. Although beta-peptide foldamers are sensitive to solvent, the systematic choice of the side-chain pattern and spatiality allows the design of the desired specific secondary structure. The application of beta-peptide foldamers may open up new directions in the synthesis of highly organized artificial tertiary structures with biochemical functions. LA - English DB - MTMT ER - TY - JOUR AU - Martinek, Tamás AU - Tóth, Gábor AU - Vass, Elemér AU - Hollósi, Miklós AU - Fülöp, Ferenc TI - cis-2-aminocyclopentanecarboxylic acid oligomers adopt a sheetlike structure: Switch from helix to nonpolar strand JF - ANGEWANDTE CHEMIE-INTERNATIONAL EDITION J2 - ANGEW CHEM INT EDIT VL - 41 PY - 2002 IS - 10 SP - 1718 EP - 1721 PG - 4 SN - 1433-7851 DO - 10.1002/1521-3773(20020517)41:10<1718::AID-ANIE1718>3.0.CO;2-2 UR - https://m2.mtmt.hu/api/publication/1013825 ID - 1013825 LA - English DB - MTMT ER -