@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:1012938,
	title = {Application of alicyclic beta-amino acids in peptide chemistry},
	url = {https://m2.mtmt.hu/api/publication/1012938},
	author = {Fülöp, Ferenc and Martinek, Tamás and Tóth, Gábor},
	doi = {10.1039/B501173F},
	journal-iso = {CHEM SOC REV},
	journal = {CHEMICAL SOCIETY REVIEWS},
	volume = {35},
	unique-id = {1012938},
	issn = {0306-0012},
	abstract = {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.},
	keywords = {DERIVATIVES; TRANSFORMATION; STEREOSELECTIVE-SYNTHESIS; HELIX; OLIGOMERS; DESIGN PRINCIPLES; TRANS-2-AMINOCYCLOPENTANECARBOXYLIC ACID; SELF-ASSOCIATION; DESYMMETRIZATION},
	year = {2006},
	eissn = {1460-4744},
	pages = {323-334},
	orcid-numbers = {Fülöp, Ferenc/0000-0003-1066-5287; Martinek, Tamás/0000-0003-3168-8066; Tóth, Gábor/0000-0002-3604-4385}
}

@article{MTMT:1013825,
	title = {cis-2-aminocyclopentanecarboxylic acid oligomers adopt a sheetlike structure: Switch from helix to nonpolar strand},
	url = {https://m2.mtmt.hu/api/publication/1013825},
	author = {Martinek, Tamás and Tóth, Gábor and Vass, Elemér and Hollósi, Miklós and Fülöp, Ferenc},
	doi = {10.1002/1521-3773(20020517)41:10<1718::AID-ANIE1718>3.0.CO;2-2},
	journal-iso = {ANGEW CHEM INT EDIT},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	volume = {41},
	unique-id = {1013825},
	issn = {1433-7851},
	keywords = {SECONDARY STRUCTURE; SIDE-CHAINS; SPECTROSCOPY; BETA-PEPTIDES; FOLDAMERS; CHIRALITY; amino acids; conformation analysis; NMR spectroscopy; TURNS},
	year = {2002},
	eissn = {1521-3773},
	pages = {1718-1721},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066; Tóth, Gábor/0000-0002-3604-4385; Vass, Elemér/0000-0001-8898-3846; Fülöp, Ferenc/0000-0003-1066-5287}
}