TY - JOUR AU - Ismail, Ruba AU - Sovány, Tamás AU - Gácsi, Attila AU - Ambrus, Rita AU - Katona, Gábor AU - Imre, Norbert AU - Pannonhalminé Csóka, Ildikó TI - Synthesis and Statistical Optimization of Poly (Lactic-Co-Glycolic Acid) Nanoparticles Encapsulating GLP1 Analog Designed for Oral Delivery JF - PHARMACEUTICAL RESEARCH J2 - PHAR RES VL - 36 PY - 2019 IS - 7 PG - 16 SN - 0724-8741 DO - 10.1007/s11095-019-2620-9 UR - https://m2.mtmt.hu/api/publication/30679490 ID - 30679490 N1 - University of Szeged, Faculty of Pharmacy, Institute of Pharmaceutical Technology and Regulatory Affairs, Eötvös u. 6, Szeged, H-6720, Hungary University of Szeged, Faculty of Pharmacy, Institute of Pharmaceutical Analysis, Somogyi u. 4, Szeged, H-6720, Hungary Export Date: 15 November 2019 CODEN: PHREE Correspondence Address: Csóka, I.; University of Szeged, Faculty of Pharmacy, Institute of Pharmaceutical Technology and Regulatory Affairs, Eötvös u. 6, Hungary; email: csoka@pharm.u-szeged.hu Chemicals/CAS: chlormethine, 51-75-2, 55-86-7, 82905-71-3; liraglutide, 204656-20-2; polyglactin, 26780-50-7, 34346-01-5; Drug Carriers; Emulsions; Hypoglycemic Agents; Liraglutide; Polylactic Acid-Polyglycolic Acid Copolymer Manufacturers: xi an health, China Funding details: EFOP-3.6.1-16-2016-00008 Funding text 1: This research was supported by the EU-funded Hungarian grant EFOP-3.6.1-16-2016-00008. University of Szeged, Faculty of Pharmacy, Institute of Pharmaceutical Technology and Regulatory Affairs, Eötvös u. 6, Szeged, H-6720, Hungary University of Szeged, Faculty of Pharmacy, Institute of Pharmaceutical Analysis, Somogyi u. 4, Szeged, H-6720, Hungary Cited By :1 Export Date: 22 November 2019 CODEN: PHREE Correspondence Address: Csóka, I.; University of Szeged, Faculty of Pharmacy, Institute of Pharmaceutical Technology and Regulatory Affairs, Eötvös u. 6, Hungary; email: csoka@pharm.u-szeged.hu Chemicals/CAS: chlormethine, 51-75-2, 55-86-7, 82905-71-3; liraglutide, 204656-20-2; polyglactin, 26780-50-7, 34346-01-5; Drug Carriers; Emulsions; Hypoglycemic Agents; Liraglutide; Polylactic Acid-Polyglycolic Acid Copolymer Manufacturers: xi an health, China Funding details: EFOP-3.6.1-16-2016-00008 Funding text 1: This research was supported by the EU-funded Hungarian grant EFOP-3.6.1-16-2016-00008. University of Szeged, Faculty of Pharmacy, Institute of Pharmaceutical Technology and Regulatory Affairs, Eötvös u. 6, Szeged, H-6720, Hungary University of Szeged, Faculty of Pharmacy, Institute of Pharmaceutical Analysis, Somogyi u. 4, Szeged, H-6720, Hungary Cited By :1 Export Date: 23 November 2019 CODEN: PHREE Correspondence Address: Csóka, I.; University of Szeged, Faculty of Pharmacy, Institute of Pharmaceutical Technology and Regulatory Affairs, Eötvös u. 6, Hungary; email: csoka@pharm.u-szeged.hu Chemicals/CAS: chlormethine, 51-75-2, 55-86-7, 82905-71-3; liraglutide, 204656-20-2; polyglactin, 26780-50-7, 34346-01-5; Drug Carriers; Emulsions; Hypoglycemic Agents; Liraglutide; Polylactic Acid-Polyglycolic Acid Copolymer Manufacturers: xi an health, China Funding details: EFOP-3.6.1-16-2016-00008 Funding text 1: This research was supported by the EU-funded Hungarian grant EFOP-3.6.1-16-2016-00008. 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 - Mihalik, Balázs AU - Pálvölgyi, Adrienn AU - Bogár, Ferenc AU - Megyeri, Katalin AU - Ling, István AU - Barkóczy, József AU - Bartha, Ferenc AU - Martinek, Tamás AU - Gacsályi, István AU - Antoni, Ferenc András TI - Loop-F of the alpha-subunit determines the pharmacologic profile of novel competitive inhibitors of GABA(A) receptors JF - EUROPEAN JOURNAL OF PHARMACOLOGY J2 - EUR J PHARMACOL VL - 798 PY - 2017 SP - 129 EP - 136 PG - 8 SN - 0014-2999 DO - 10.1016/j.ejphar.2017.01.033 UR - https://m2.mtmt.hu/api/publication/3193426 ID - 3193426 N1 - Funding Agency and Grant Number: Lendulet (Momentum) program of the Hungarian Academy of Sciences\n Funding text: With the exception of FBc, FBd and TM all authors were employees of Egis Pharmaceuticals PLC, Budapest, Hungary. The work of TM is supported by the Lendulet (Momentum) program of the Hungarian Academy of Sciences. We thank Dr. Patricia Machado (Les Laboratoires Servier, Suresnes, France) for helpful comments on the manuscript.\n Division of Preclinical Research, Egis Pharmaceuticals PLC, Hungary Chemical Research Division, Egis Pharmaceuticals PLC, Budapest, Hungary MTA-SZTE Supramolecular and Nanostructured Materials Research Group of HAS, University of Szeged, Hungary Department of Medical Chemistry, University of Szeged, Hungary Institute of Pharmaceutical Analysis, SZTE-MTA Lendület Foldamer Research Group, University of Szeged, Szeged, Hungary Cited By :5 Export Date: 22 May 2020 CODEN: EJPHA Correspondence Address: Antoni, F.A.Hungary; email: franzantoni@gmail.com Chemicals/CAS: bicuculline, 485-49-4; etomidate, 15301-65-2, 33125-97-2, 51919-80-3; 4 aminobutyric acid, 28805-76-7, 56-12-2; Benzodiazepines; GABA-A Receptor Antagonists; gamma-Aminobutyric Acid; Oxazoles; Protein Subunits; Receptors, GABA-A Division of Preclinical Research, Egis Pharmaceuticals PLC, Hungary Chemical Research Division, Egis Pharmaceuticals PLC, Budapest, Hungary MTA-SZTE Supramolecular and Nanostructured Materials Research Group of HAS, University of Szeged, Hungary Department of Medical Chemistry, University of Szeged, Hungary Institute of Pharmaceutical Analysis, SZTE-MTA Lendület Foldamer Research Group, University of Szeged, Szeged, Hungary Cited By :5 Export Date: 1 January 2021 CODEN: EJPHA Correspondence Address: Antoni, F.A.Hungary; email: franzantoni@gmail.com Chemicals/CAS: bicuculline, 485-49-4; etomidate, 15301-65-2, 33125-97-2, 51919-80-3; 4 aminobutyric acid, 28805-76-7, 56-12-2; Benzodiazepines; GABA-A Receptor Antagonists; gamma-Aminobutyric Acid; Oxazoles; Protein Subunits; Receptors, GABA-A Division of Preclinical Research, Egis Pharmaceuticals PLC, Hungary Chemical Research Division, Egis Pharmaceuticals PLC, Budapest, Hungary MTA-SZTE Supramolecular and Nanostructured Materials Research Group of HAS, University of Szeged, Hungary Department of Medical Chemistry, University of Szeged, Hungary Institute of Pharmaceutical Analysis, SZTE-MTA Lendület Foldamer Research Group, University of Szeged, Szeged, Hungary Cited By :5 Export Date: 31 May 2021 CODEN: EJPHA Correspondence Address: Antoni, F.A.Hungary; email: franzantoni@gmail.com Chemicals/CAS: bicuculline, 485-49-4; etomidate, 15301-65-2, 33125-97-2, 51919-80-3; 4 aminobutyric acid, 28805-76-7, 56-12-2; Benzodiazepines; GABA-A Receptor Antagonists; gamma-Aminobutyric Acid; Oxazoles; Protein Subunits; Receptors, GABA-A LA - English DB - MTMT ER - TY - JOUR AU - Hetényi, Anasztázia AU - Hegedüs, Zsófia AU - Fajka-Boja, Roberta AU - Monostori, Éva AU - E Kövér, Katalin AU - Martinek, Tamás TI - Target-specific NMR detection of protein–ligand interactions with antibody-relayed 15N-group selective STD JF - JOURNAL OF BIOMOLECULAR NMR J2 - J BIOMOL NMR VL - 66 PY - 2016 IS - 4 SP - 227 EP - 232 PG - 6 SN - 0925-2738 DO - 10.1007/s10858-016-0076-3 UR - https://m2.mtmt.hu/api/publication/3148106 ID - 3148106 N1 - Funding Agency and Grant Number: Hungarian Research Foundation OTKA [PD83600, K105459]; Hungarian Academy of Sciences, Lendulet program [LP-2011-009]; European Union; State of Hungary; European Social Fund [TAMOP-4.2.4.A/2-11/1-2012-0001]; EU; European Regional Development Fund [GINOP-2.3.3-15-2016-00004, GINOP-2.3.3-15-2016-00010]\n Funding text: This work was supported by the Hungarian Research Foundation OTKA projects PD83600 and K105459 and the Hungarian Academy of Sciences, Lendulet program (LP-2011-009). This research was supported by the European Union and the State of Hungary, co-financed by the European Social Fund in the framework of TAMOP-4.2.4.A/2-11/1-2012-0001 'National Excellence Program'. The research was supported by the EU and co-financed by the European Regional Development Fund under the projects GINOP-2.3.3-15-2016-00004 and GINOP-2.3.3-15-2016-00010.\n Funding Agency and Grant Number: Hungarian Research Foundation OTKA [PD83600, K105459]; Hungarian Academy of Sciences, Lendulet program [LP-2011-009]; European Union; State of Hungary; European Social Fund [TAMOP-4.2.4.A/2-11/1-2012-0001]; EU; European Regional Development Fund [GINOP-2.3.3-15-2016-00004, GINOP-2.3.3-15-2016-00010] Funding text: This work was supported by the Hungarian Research Foundation OTKA projects PD83600 and K105459 and the Hungarian Academy of Sciences, Lendulet program (LP-2011-009). This research was supported by the European Union and the State of Hungary, co-financed by the European Social Fund in the framework of TAMOP-4.2.4.A/2-11/1-2012-0001 'National Excellence Program'. The research was supported by the EU and co-financed by the European Regional Development Fund under the projects GINOP-2.3.3-15-2016-00004 and GINOP-2.3.3-15-2016-00010. AB - Fragment-based drug design has been successfully applied to challenging targets where the detection of the weak protein-ligand interactions is a key element. H-1 saturation transfer difference (STD) NMR spectroscopy is a powerful technique for this work but it requires pure homogeneous proteins as targets. Monoclonal antibody (mAb)-relayed N-15-GS STD spectroscopy has been developed to resolve the problem of protein mixtures and impure proteins. A N-15-labelled target-specific mAb is selectively irradiated and the saturation is relayed through the target to the ligand. Tests on the anti-Gal-1 mAb/Gal-1/lactose system showed that the approach is experimentally feasible in a reasonable time frame. This method allows detection and identification of binding molecules directly from a protein mixture in a multicomponent system. LA - English DB - MTMT ER - TY - JOUR AU - Hetényi, Anasztázia AU - Németh, Lukács AU - Wéber, Edit AU - Szakonyi, Gerda AU - Winter, Zoltán AU - Jósvay, Katalin AU - Bartus, Éva AU - Oláh, Zoltán AU - Martinek, Tamás TI - Competitive inhibition of TRPV1 – calmodulin interaction by vanilloids JF - FEBS LETTERS J2 - FEBS LETT VL - 590 PY - 2016 IS - 16 SP - 2768 EP - 2775 PG - 8 SN - 0014-5793 DO - 10.1002/1873-3468.12267 UR - https://m2.mtmt.hu/api/publication/3087152 ID - 3087152 N1 - Funding Agency and Grant Number: Hungarian Academy of Sciences; Lendulet Program [LP-2011-009]; MTA Postdoctoral Fellowship E.W., Gedeon Richter Plc. [TP7-017]; Hungarian Research Foundation [OTKA K112442]; Richter Gedeon Talentum Alapitvany; European Union; State of Hungary; European Social Fund [TAMOP-4.2.4.A/ 2-11/1-2012-0001]\n Funding text: This work was supported by the Hungarian Academy of Sciences, Lendulet Program (LP-2011-009), MTA Postdoctoral Fellowship E.W., Gedeon Richter Plc. (TP7-017), the Hungarian Research Foundation (OTKA K112442) and Financial support from Richter Gedeon Talentum Alapitvany (Ph.D. Scholarship to E.B.). This research was supported by the European Union and the State of Hungary, cofinanced by the European Social Fund in the framework of TAMOP-4.2.4.A/ 2-11/1-2012-0001 'National Excellence Program'.\n Funding Agency and Grant Number: Hungarian Academy of Sciences; Lendulet Program [LP-2011-009]; MTA Postdoctoral Fellowship E.W., Gedeon Richter Plc. [TP7-017]; Hungarian Research Foundation [OTKA K112442]; Richter Gedeon Talentum Alapitvany; European Union; State of Hungary; European Social Fund [TAMOP-4.2.4.A/ 2-11/1-2012-0001] Funding text: This work was supported by the Hungarian Academy of Sciences, Lendulet Program (LP-2011-009), MTA Postdoctoral Fellowship E.W., Gedeon Richter Plc. (TP7-017), the Hungarian Research Foundation (OTKA K112442) and Financial support from Richter Gedeon Talentum Alapitvany (Ph.D. Scholarship to E.B.). This research was supported by the European Union and the State of Hungary, cofinanced by the European Social Fund in the framework of TAMOP-4.2.4.A/ 2-11/1-2012-0001 'National Excellence Program'. AB - There is enormous interest toward vanilloid agonists of the pain receptor TRPV1 in analgesic therapy, but the mechanisms of their sensory neuron-blocking effects at high or repeated doses are still a matter of debate. Our results have demonstrated that capsaicin and resiniferatoxin form nanomolar complexes with calmodulin, and competitively inhibit TRPV1-calmodulin interaction. These interactions involve the protein recognition interface of calmodulin, which is responsible for all of the cell-regulatory calmodulin-protein interactions. These results draw attention to a previously unknown vanilloid target, which may contribute to the explanation of the paradoxical pain-modulating behavior of these important pharmacons. LA - English DB - MTMT ER - TY - JOUR AU - Fajka-Boja, Roberta AU - Suhajdáné Urbán, Veronika AU - Szebeni, Gábor AU - Czibula, Ágnes AU - Blaskó, Andrea AU - Kriston-Pál, Éva AU - Makra, Ildikó AU - Hornung, Ákos AU - Szabó, Enikő AU - Uher, Ferenc AU - Than, Nándor Gábor AU - Monostori, Éva TI - Galectin-1 is a local but not systemic immunomodulatory factor in mesenchymal stromal cells JF - CYTOTHERAPY J2 - CYTOTHERAPY VL - 18 PY - 2016 IS - 3 SP - 360 EP - 370 PG - 11 SN - 1465-3249 DO - 10.1016/j.jcyt.2015.12.004 UR - https://m2.mtmt.hu/api/publication/3024122 ID - 3024122 AB - BACKGROUND AIMS: Mesenchymal stromal cells (MSCs) have powerful immunosuppressive activity. This function of MSCs is attributed to plethora of the expressed immunosuppressive factors, such as galectin-1 (Gal-1), a pleiotropic lectin with robust anti-inflammatory effect. Nevertheless, whether Gal-1 renders or contributes to the immunosuppressive effect of MSCs has not been clearly established. Therefore, this question was the focus of a complex study. METHODS: MSCs were isolated from bone marrows of wild-type and Gal-1 knockout mice and their in vitro anti-proliferative and apoptosis-inducing effects on activated T cells were examined. The in vivo immunosuppressive activity was tested in murine models of type I diabetes and delayed-type hypersensitivity. RESULTS: Both Gal-1-expressing and -deficient MSCs inhibited T-cell proliferation. Inhibition of T-cell proliferation by MSCs was mediated by nitric oxide but not PD-L1 or Gal-1. In contrast, MSC-derived Gal-1 triggered apoptosis in activated T cells that were directly coupled to MSCs, representing a low proportion of the T-cell population. Furthermore, absence of Gal-1 in MSCs did not affect their in vivo immunosuppressive effect. CONCLUSIONS: These results serve as evidence that Gal-1 does not play a role in the systemic immunosuppressive effect of MSCs. However, a local contribution of Gal-1 to modulation of T-cell response by direct cell-to-cell interaction cannot be excluded. Notably, this study serves a good model to understand how the specificity of a pleiotropic protein depends on the type and localization of the producing effector cell and its target. LA - English DB - MTMT ER - TY - JOUR AU - Hegedüs, Zsófia AU - Makra, Ildikó AU - Imre, Norbert AU - Hetényi, Anasztázia AU - Mándity, István AU - Monostori, Éva AU - Martinek, Tamás TI - Foldameric probes for membrane interactions by induced β-sheet folding JF - CHEMICAL COMMUNICATIONS J2 - CHEM COMMUN VL - 52 PY - 2016 IS - 9 SP - 1891 EP - 1894 PG - 4 SN - 1359-7345 DO - 10.1039/C5CC09257D UR - https://m2.mtmt.hu/api/publication/2993079 ID - 2993079 N1 - Funding Agency and Grant Number: Hungarian Academy of Sciences; Lendulet program [LP-2011-009]; [TAMOP-4.2.6-14/1]\n Funding text: This work was supported by the Hungarian Academy of Sciences, Lendulet program (LP-2011-009) and TAMOP-4.2.6-14/1. Csaba Vizler is gratefully acknowledged for providing the bEND.3 cell line.\n Funding Agency and Grant Number: Hungarian Academy of Sciences; Lendulet program [LP-2011-009]; [TAMOP-4.2.6-14/1] Funding text: This work was supported by the Hungarian Academy of Sciences, Lendulet program (LP-2011-009) and TAMOP-4.2.6-14/1. Csaba Vizler is gratefully acknowledged for providing the bEND.3 cell line. Funding Agency and Grant Number: Hungarian Academy of SciencesHungarian Academy of Sciences; Lendulet program [LP-2011-009]; [TAMOP-4.2.6-14/1] Funding text: This work was supported by the Hungarian Academy of Sciences, Lendulet program (LP-2011-009) and TAMOP-4.2.6-14/1. Csaba Vizler is gratefully acknowledged for providing the bEND.3 cell line. AB - Design strategies were devised for alpha/beta-peptide foldameric analogues of the antiangiogenic anginex with the goal of mimicking the diverse structural features from the unordered conformation to a folded beta-sheet in response to membrane interactions. Structure-activity relationships were investigated in the light of different beta-sheet folding levels. 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 - Cabrele, C AU - Martinek, Tamás AU - Reiser, O AU - Berlicki, Ł TI - Peptides containing β-amino acid patterns: Challenges and successes in medicinal chemistry JF - JOURNAL OF MEDICINAL CHEMISTRY J2 - J MED CHEM VL - 57 PY - 2014 IS - 23 SP - 9718 EP - 9739 PG - 22 SN - 0022-2623 DO - 10.1021/jm5010896 UR - https://m2.mtmt.hu/api/publication/2817673 ID - 2817673 AB - The construction of bioactive peptides using β-amino acid-containing sequence patterns is a very promising strategy to obtain analogues that exhibit properties of high interest for medicinal chemistry applications. β-Amino acids have been shown to modulate the conformation, dynamics, and proteolytic susceptibility of native peptides. They can be either combined with α-amino acids by following specific patterns, which results in backbone architectures with well-defined orientations of the side chain functional groups, or assembled in de novo-designed bioactive β- or α,β-peptidic sequences. Such peptides display various biological functions, including antimicrobial activity, inhibition of protein-protein interactions, agonism/antagonism of GPCR ligands, and anti-angiogenic activity. LA - English DB - MTMT ER - 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 -