@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}
}