@article{MTMT:2993079, title = {Foldameric probes for membrane interactions by induced β-sheet folding}, url = {https://m2.mtmt.hu/api/publication/2993079}, author = {Hegedüs, Zsófia and Makra, Ildikó and Imre, Norbert and Hetényi, Anasztázia and Mándity, István and Monostori, Éva and Martinek, Tamás}, doi = {10.1039/C5CC09257D}, journal-iso = {CHEM COMMUN}, journal = {CHEMICAL COMMUNICATIONS}, volume = {52}, unique-id = {2993079}, issn = {1359-7345}, abstract = {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.}, keywords = {PROTEIN; ACID; DESIGN; SECONDARY STRUCTURE; ANGIOGENESIS; CIRCULAR-DICHROISM; Practical guide; HAIRPIN; PEPTIDE ANGINEX}, year = {2016}, eissn = {1364-548X}, pages = {1891-1894}, orcid-numbers = {Hegedüs, Zsófia/0000-0002-5546-8167; Hetényi, Anasztázia/0000-0001-8080-6992; Mándity, István/0000-0003-2865-6143; Monostori, Éva/0000-0002-7442-3562; Martinek, Tamás/0000-0003-3168-8066} } @article{MTMT:2817673, title = {Peptides containing β-amino acid patterns: Challenges and successes in medicinal chemistry}, url = {https://m2.mtmt.hu/api/publication/2817673}, author = {Cabrele, C and Martinek, Tamás and Reiser, O and Berlicki, Ł}, doi = {10.1021/jm5010896}, journal-iso = {J MED CHEM}, journal = {JOURNAL OF MEDICINAL CHEMISTRY}, volume = {57}, unique-id = {2817673}, issn = {0022-2623}, abstract = {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.}, year = {2014}, eissn = {1520-4804}, pages = {9718-9739}, orcid-numbers = {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} }