@article{MTMT:2764648,
	title = {Predicting Order and Disorder for β-Peptide Foldamers in Water},
	url = {https://m2.mtmt.hu/api/publication/2764648},
	author = {Németh, Lukács and Hegedüs, Zsófia and Martinek, Tamás},
	doi = {10.1021/ci5003476},
	journal-iso = {J CHEM INF MODEL},
	journal = {JOURNAL OF CHEMICAL INFORMATION AND MODELING},
	volume = {54},
	unique-id = {2764648},
	issn = {1549-9596},
	abstract = {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.},
	year = {2014},
	eissn = {1549-960X},
	pages = {2776-2783},
	orcid-numbers = {Hegedüs, Zsófia/0000-0002-5546-8167; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:2459240,
	title = {Foldameric α/β-Peptide Analogs of the β-Sheet-Forming Antiangiogenic Anginex: Structure and Bioactivity},
	url = {https://m2.mtmt.hu/api/publication/2459240},
	author = {Hegedüs, Zsófia and Wéber, Edit and Kriston-Pál, Éva and Makra, Ildikó and Czibula, Ágnes and Monostori, Éva and Martinek, Tamás},
	doi = {10.1021/ja408054f},
	journal-iso = {J AM CHEM SOC},
	journal = {JOURNAL OF THE AMERICAN CHEMICAL SOCIETY},
	volume = {135},
	unique-id = {2459240},
	issn = {0002-7863},
	abstract = {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.},
	year = {2013},
	eissn = {1520-5126},
	pages = {16578-16584},
	orcid-numbers = {Hegedüs, Zsófia/0000-0002-5546-8167; Wéber, Edit/0000-0002-5904-0619; Czibula, Ágnes/0000-0003-4461-2773; Monostori, Éva/0000-0002-7442-3562; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:1926671,
	title = {Unique α,β- and α,α,β,β-peptide foldamers based on cis-β-aminocyclopentanecarboxylic acid},
	url = {https://m2.mtmt.hu/api/publication/1926671},
	author = {Berlicki, Ł and Pilsl, L and Wéber, Edit and Mándity, István and Cabrele, C and Martinek, Tamás and Fülöp, Ferenc and Reiser, O},
	doi = {10.1002/anie.201107702},
	journal-iso = {ANGEW CHEM INT EDIT},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	volume = {51},
	unique-id = {1926671},
	issn = {1433-7851},
	abstract = {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.},
	keywords = {PEPTIDES; METHANOL; FOLDAMERS; amino acids; helical structures; aqueous media; Building blockes; High stability; cis-pentacine; β-amino acids},
	year = {2012},
	eissn = {1521-3773},
	pages = {2208-2212},
	orcid-numbers = {Wéber, Edit/0000-0002-5904-0619; Mándity, István/0000-0003-2865-6143; Martinek, Tamás/0000-0003-3168-8066; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1842289,
	title = {Self-association-driven transition of the β-peptidic H12 helix to the H18 helix},
	url = {https://m2.mtmt.hu/api/publication/1842289},
	author = {Szolnoki, Éva Tünde and Hetényi, Anasztázia and Martinek, Tamás and Szakonyi, Zsolt and Fülöp, Ferenc},
	doi = {10.1039/c1ob06627g},
	journal-iso = {ORG BIOMOL CHEM},
	journal = {ORGANIC & BIOMOLECULAR CHEMISTRY},
	volume = {10},
	unique-id = {1842289},
	issn = {1477-0520},
	abstract = {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.},
	keywords = {SECONDARY STRUCTURE; CIRCULAR-DICHROISM; SIDE-CHAINS; ACID OLIGOMERS; QUATERNARY STRUCTURE; ALPHA/BETA-PEPTIDES; STRUCTURAL-CHARACTERIZATION; AMPHIPATHIC PEPTIDES; MEMBRANE ENVIRONMENT; HETEROGENEOUS BACKBONES},
	year = {2012},
	eissn = {1477-0539},
	pages = {255-259},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Martinek, Tamás/0000-0003-3168-8066; Szakonyi, Zsolt/0000-0003-2432-8409; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1412123,
	title = {Building β-Peptide H10/12 Foldamer Helices with Six-Membered Cyclic Side-Chains: Fine-Tuning of Folding and Self-Assembly},
	url = {https://m2.mtmt.hu/api/publication/1412123},
	author = {Mándity, István and Fülöp, Lívia and Vass, Elemér and Tóth, Gábor and Martinek, Tamás and Fülöp, Ferenc},
	doi = {10.1021/ol102494m},
	journal-iso = {ORG LETT},
	journal = {ORGANIC LETTERS},
	volume = {12},
	unique-id = {1412123},
	issn = {1523-7060},
	abstract = {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.},
	keywords = {ASSOCIATION; FAMILY; DESIGN; SECONDARY STRUCTURE; NMR; OLIGOMERS; amino acids; CD; LYOTROPIC LIQUID-CRYSTALS},
	year = {2010},
	eissn = {1523-7052},
	pages = {5584-5587},
	orcid-numbers = {Mándity, István/0000-0003-2865-6143; Fülöp, Lívia/0000-0002-8010-0129; Vass, Elemér/0000-0001-8898-3846; Tóth, Gábor/0000-0002-3604-4385; Martinek, Tamás/0000-0003-3168-8066; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1504474,
	title = {VCD studies on cyclic peptides assembled from L-alpha-amino acids and a trans-2-aminocyclopentane- or trans-2-aminocyclohexane carboxylic acid},
	url = {https://m2.mtmt.hu/api/publication/1504474},
	author = {Vass, Elemér and Strijowski, U and Wollschlager, K and Mándity, István and Szilvágyi, Gábor and Jewginski, M and Gaus, K and Royo, S and Majer, Zsuzsanna (Deckerné) and Sewald, N and Hollósi, Miklós},
	doi = {10.1002/psc.1272},
	journal-iso = {J PEPT SCI},
	journal = {JOURNAL OF PEPTIDE SCIENCE},
	volume = {16},
	unique-id = {1504474},
	issn = {1075-2617},
	year = {2010},
	eissn = {1099-1387},
	pages = {613-620},
	orcid-numbers = {Vass, Elemér/0000-0001-8898-3846; Mándity, István/0000-0003-2865-6143}
}

@article{MTMT:1232853,
	title = {Design of Peptidic Foldamer Helices: A Stereochemical Patterning Approach},
	url = {https://m2.mtmt.hu/api/publication/1232853},
	author = {Mándity, István and Wéber, Edit and Martinek, Tamás and Olajos, Gábor and Tóth, Gábor and Vass, Elemér and Fülöp, Ferenc},
	doi = {10.1002/anie.200805095},
	journal-iso = {ANGEW CHEM INT EDIT},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	volume = {48},
	unique-id = {1232853},
	issn = {1433-7851},
	keywords = {SEQUENCES; SECONDARY STRUCTURE; CONFORMATIONS; DE-NOVO DESIGN; PROTEINOGENIC SIDE-CHAINS; FOLDAMERS; OLIGOMERS; amino acids; NMR spectroscopy; ALPHA/BETA-PEPTIDES; helical structures; BETA-AMINO-ACID; BETA(3)-PEPTIDES},
	year = {2009},
	eissn = {1521-3773},
	pages = {2171-2175},
	orcid-numbers = {Mándity, István/0000-0003-2865-6143; Wéber, Edit/0000-0002-5904-0619; Martinek, Tamás/0000-0003-3168-8066; Olajos, Gábor/0000-0002-2479-4891; Tóth, Gábor/0000-0002-3604-4385; Vass, Elemér/0000-0001-8898-3846; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1155852,
	title = {Regio- and stereoselective synthesis of constrained enantiomeric beta-amino acid derivatives},
	url = {https://m2.mtmt.hu/api/publication/1155852},
	author = {Szakonyi, Zsolt and Martinek, Tamás and Sillanpaa, R and Fülöp, Ferenc},
	doi = {10.1016/j.tetasy.2008.09.026},
	journal-iso = {TETRAHEDRON ASYMMETR},
	journal = {TETRAHEDRON-ASYMMETRY},
	volume = {19},
	unique-id = {1155852},
	issn = {0957-4166},
	abstract = {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.},
	keywords = {CHLOROSULFONYL ISOCYANATE; SECONDARY STRUCTURE; DIETHYLZINC; CHEMISTRY; ALDEHYDES; PEPTIDES; ALCOHOLS; TRANSFORMATIONS; CONFIGURATION; REDUCTION},
	year = {2008},
	eissn = {1362-511X},
	pages = {2296-2303},
	orcid-numbers = {Szakonyi, Zsolt/0000-0003-2432-8409; Martinek, Tamás/0000-0003-3168-8066; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1012935,
	title = {Secondary structure dependent self-assembly of beta-peptides into nanosized fibrils and membranes},
	url = {https://m2.mtmt.hu/api/publication/1012935},
	author = {Martinek, Tamás and Hetényi, Anasztázia and Fülöp, Lívia and Mándity, István and Tóth, Gábor and Dékány, Imre and Fülöp, Ferenc},
	doi = {10.1002/anie.200504158},
	journal-iso = {ANGEW CHEM INT EDIT},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	volume = {45},
	unique-id = {1012935},
	issn = {1433-7851},
	keywords = {ASSOCIATION; BETA-PEPTIDES; NANOFIBERS; ACID OLIGOMERS; PROTEINOGENIC SIDE-CHAINS; FOLDAMERS; nanomaterials; TERTIARY STRUCTURE; peptide mimetics},
	year = {2006},
	eissn = {1521-3773},
	pages = {2396-2400},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066; Hetényi, Anasztázia/0000-0001-8080-6992; Fülöp, Lívia/0000-0002-8010-0129; Mándity, István/0000-0003-2865-6143; Tóth, Gábor/0000-0002-3604-4385; Dékány, Imre/0000-0001-5472-5355; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:2750,
	title = {ANALYSIS OF THE CIRCULAR-DICHROISM SPECTRUM OF PROTEINS USING THE CONVEX CONSTRAINT ALGORITHM - A PRACTICAL GUIDE},
	url = {https://m2.mtmt.hu/api/publication/2750},
	author = {Perczel, András and Park, K and Fasman, GD},
	doi = {10.1016/0003-2697(92)90046-A},
	journal-iso = {ANAL BIOCHEM},
	journal = {ANALYTICAL BIOCHEMISTRY},
	volume = {203},
	unique-id = {2750},
	issn = {0003-2697},
	year = {1992},
	eissn = {1096-0309},
	pages = {83-93},
	orcid-numbers = {Perczel, András/0000-0003-1252-6416}
}