TY - JOUR AU - Németh, Lukács AU - Hegedüs, Zsófia AU - Martinek, Tamás TI - Predicting Order and Disorder for β-Peptide Foldamers in Water JF - JOURNAL OF CHEMICAL INFORMATION AND MODELING J2 - J CHEM INF MODEL VL - 54 PY - 2014 IS - 10 SP - 2776 EP - 2783 PG - 8 SN - 1549-9596 DO - 10.1021/ci5003476 UR - https://m2.mtmt.hu/api/publication/2764648 ID - 2764648 AB - Following a quantitative validation approach, we tested the AMBER ff03 and GAFF force fields with the TIP3P explicit water model in molecular dynamic simulations of beta-peptide foldamers. The test sequences were selected to represent a wide range of folding behavior in water: compact helix, strand mimetic geometry, and the state of disorder. The combination AMBER ff03-TIP3P successfully predicted the experimentally observed conformational properties and reproduced the NOE distances and backbone (3)J coupling data at a good level. GAFF was unable to produce folded structures correctly due to its biased torsion potentials. We can recommend AMBER ff03-TIP3P for simulations involving beta-peptide sequences in aqueous media including ordered and disordered structures. LA - English DB - MTMT ER - TY - JOUR AU - Hegedüs, Zsófia AU - Wéber, Edit AU - Kriston-Pál, Éva AU - Makra, Ildikó AU - Czibula, Ágnes AU - Monostori, Éva AU - Martinek, Tamás TI - Foldameric α/β-Peptide Analogs of the β-Sheet-Forming Antiangiogenic Anginex: Structure and Bioactivity JF - JOURNAL OF THE AMERICAN CHEMICAL SOCIETY J2 - J AM CHEM SOC VL - 135 PY - 2013 IS - 44 SP - 16578 EP - 16584 PG - 7 SN - 0002-7863 DO - 10.1021/ja408054f UR - https://m2.mtmt.hu/api/publication/2459240 ID - 2459240 AB - The principles of beta-sheet folding and design for alpha-peptidic sequences are well established, while those for sheet mimetics containing homologated amino acid building blocks are still under investigation. To reveal the structure-function relations of beta-amino-acid-containing foldamers, we followed a top-down approach to study a series of alpha/beta-peptidic analogs of anginex, a beta-sheet-forming antiangiogenic peptide. Eight anginex analogs were developed by systematic alpha --> beta(3) substitutions and analyzed by using NMR and CD spectroscopy. The foldamers retained the beta-sheet tendency, though with a decreased folding propensity. beta-Sheet formation could be induced by a micellar environment, similarly to that of the parent peptide. The destructuring effect was higher when the alpha --> beta(3) exchange was located in the beta-sheet core. Analysis of the beta-sheet stability versus substitution pattern and the local conformational bias of the bulky beta(3)V and beta(3)I residues revealed that a mismatch between the H-bonding preferences of the alpha- and beta-residues played a minor role in the structure-breaking effect. Temperature-dependent CD and NMR measurements showed that the hydrophobic stabilization was scaled-down for the alpha/beta-peptides. Analysis of the biological activity of the foldamer peptides showed that four anginex derivatives dose-dependently inhibited the proliferation of a mouse endothelial cell line. The alpha --> beta(3) substitution strategy applied in this work can be a useful approach to the construction of bioactive beta-sheet mimetics with a reduced aggregation tendency and improved pharmacokinetic properties. 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 - 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 - 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 - Vass, Elemér AU - Strijowski, U AU - Wollschlager, K AU - Mándity, István AU - Szilvágyi, Gábor AU - Jewginski, M AU - Gaus, K AU - Royo, S AU - Majer, Zsuzsanna (Deckerné) AU - Sewald, N AU - Hollósi, Miklós TI - VCD studies on cyclic peptides assembled from L-alpha-amino acids and a trans-2-aminocyclopentane- or trans-2-aminocyclohexane carboxylic acid JF - JOURNAL OF PEPTIDE SCIENCE J2 - J PEPT SCI VL - 16 PY - 2010 IS - 11 SP - 613 EP - 620 PG - 8 SN - 1075-2617 DO - 10.1002/psc.1272 UR - https://m2.mtmt.hu/api/publication/1504474 ID - 1504474 N1 - Megjegyzés-22208883 DI: 10.1002/psc.1272 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 - Szakonyi, Zsolt AU - Martinek, Tamás AU - Sillanpaa, R AU - Fülöp, Ferenc TI - Regio- and stereoselective synthesis of constrained enantiomeric beta-amino acid derivatives JF - TETRAHEDRON-ASYMMETRY J2 - TETRAHEDRON ASYMMETR VL - 19 PY - 2008 IS - 19 SP - 2296 EP - 2303 PG - 8 SN - 0957-4166 DO - 10.1016/j.tetasy.2008.09.026 UR - https://m2.mtmt.hu/api/publication/1155852 ID - 1155852 AB - Chlorosulfonyl isocyanate addition to (-)- and (+)-apopinene furnished monoterpene-fused beta-lactams in highly regio- and stereospecific reactions. beta-Lactams 5 and 13 exhibited reactivities similar to those of the cycloalkane-fused analogs and were easily converted to the p-amino acid and its protected derivatives. The base-catalyzed isomerization of the cis-amino ester afforded the corresponding trans-amino acid enantiomers in excellent yields. The complete isomerization is explained by the stability difference, which was estimated by ab initio calculations between the cis- and trans-diastereomers. (C) 2008 Elsevier Ltd. All rights reserved. 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 - Perczel, András AU - Park, K AU - Fasman, GD TI - ANALYSIS OF THE CIRCULAR-DICHROISM SPECTRUM OF PROTEINS USING THE CONVEX CONSTRAINT ALGORITHM - A PRACTICAL GUIDE JF - ANALYTICAL BIOCHEMISTRY J2 - ANAL BIOCHEM VL - 203 PY - 1992 SP - 83 EP - 93 PG - 11 SN - 0003-2697 DO - 10.1016/0003-2697(92)90046-A UR - https://m2.mtmt.hu/api/publication/2750 ID - 2750 N1 - Cited By :421 Export Date: 30 June 2023 CODEN: ANBCA Correspondence Address: Fasman, G.D.; Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254, United States LA - English DB - MTMT ER -