@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}
}