| Literature DB >> 29809294 |
Fredy Sussman1, Víctor M Sánchez-Pedregal1, Juan C Estévez1, Rosalino Balo1, Jesús Jiménez-Barbero2,3,4, Ana Ardá2, Ana Gimeno2, Miriam Royo5,6, M Carmen Villaverde1, Ramón J Estévez1.
Abstract
This work shows that hybrid peptides formed by alternating trans-2-aminocyclopentanecarboxylic acid (trans-ACPC) and trans-2-aminocyclohexanecarboxylic acid (trans-ACHC) do not fold in the solvents typically used in the study of their homo-oligomers. Only when the peptides are assayed in SDS micelles are the predicted helical structures obtained. This indicates that the environment could play an equally important role (as the backbone stereochemistry) in determining their fold, possibly by providing a sequestered environment.Entities:
Keywords: NMR spectroscopy; environmental effects; foldamers; micelles; molecular dynamics
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Year: 2018 PMID: 29809294 DOI: 10.1002/chem.201801953
Source DB: PubMed Journal: Chemistry ISSN: 0947-6539 Impact factor: 5.236