@article{MTMT:30535263,
	title = {Flow-chemistry enabled efficient synthesis of β-peptides: backbone topology vs. helix formation},
	url = {https://m2.mtmt.hu/api/publication/30535263},
	author = {Nekkaa, Imane and Bogdán, Dóra and Gáti, Tamás and Béni, Szabolcs and Juhász, Tünde and Palkó, Márta and Paragi, Gábor and Tóth, Gábor and Fülöp, Ferenc and Mándity, István},
	doi = {10.1039/c8cc10147g},
	journal-iso = {CHEM COMMUN},
	journal = {CHEMICAL COMMUNICATIONS},
	volume = {55},
	unique-id = {30535263},
	issn = {1359-7345},
	abstract = {Enantiodiscriminative helix formation was observed for beta-peptide H14 helices. This observation is caused by the synperiplanar orientation of H-O atoms which is more unfavorable than those for H-H interaction. The 1,2 H-O interaction leads to the destruction of the helical structure. The introduction of a double C-C bond in the backbone rules out helix formation.},
	keywords = {SELECTIVITY; DESIGN; SECONDARY STRUCTURE; STABILITY; OLIGOMERS; AMINO-ACID; FOLDAMER HELICES},
	year = {2019},
	eissn = {1364-548X},
	pages = {3061-3064},
	orcid-numbers = {Bogdán, Dóra/0000-0003-4455-8914; Béni, Szabolcs/0000-0001-7056-6825; Palkó, Márta/0000-0002-8265-7377; Paragi, Gábor/0000-0001-5408-1748; Tóth, Gábor/0000-0002-3604-4385; Fülöp, Ferenc/0000-0003-1066-5287; Mándity, István/0000-0003-2865-6143}
}