Environmental Effects Determine the Structure of Potential β-Amino Acid Based Foldamers

Autor:	Miriam Royo, Jesús Jiménez-Barbero, Víctor M. Sánchez-Pedregal, Rosalino Balo, Juan C. Estévez, Ana Ardá, Fredy Sussman, M. Carmen Villaverde, Ramón J. Estévez, Ana Gimeno
Rok vydání:	2018
Předmět:	chemistry.chemical_classification 010405 organic chemistry Chemistry Stereochemistry Amino Acids Basic Organic Chemistry General Chemistry Nuclear magnetic resonance spectroscopy 010402 general chemistry 01 natural sciences Micelle Catalysis 0104 chemical sciences Amino acid Molecular dynamics Solvents Cycloleucine Peptides
Zdroj:	Chemistry - A European Journal. 24:10625-10629
ISSN:	0947-6539
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::051e357d6f44b1b60cf4a264bf2efa82 https://doi.org/10.1002/chem.201801953 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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