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Deracemization and the first CD spectrum of a 310-helical peptide made of achiral α-amino-isobutyric acid residues in a chiral membrane mimetic environment

By Francesca Ceccacci, Giovanna Mancini, Paola Rossi, Paolo Scrimin, Alessandro Sorrenti and Paolo Tecilla

Abstract

Interaction of the racemic helical homo-octapeptide made by the achiral Ca-methyl alanine (Aib) amino acid with a chiral enantiopure micellar aggregate made of N-dodecylproline led to the deracemization of the helical Aib sequence thus allowing us to obtain for the first time the CD signature in water of a 310 helix devoid of the contribution of any chiral amino acid

Topics: supramolecular chemistry, peptide conformation, chiral micellar aggregate
Year: 2013
DOI identifier: 10.1039/c3cc44713h
OAI identifier: oai:arts.units.it:11368/2713093
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