Interaction of the racemic helical homo-octapeptide made by the achiral Ca-methyl alanine (Aib) amino acid with a chiral enantiopure micellar aggregatemade 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.

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

F Ceccacci;G Mancini;
2013

Abstract

Interaction of the racemic helical homo-octapeptide made by the achiral Ca-methyl alanine (Aib) amino acid with a chiral enantiopure micellar aggregatemade 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.
2013
Istituto per i Sistemi Biologici - ISB (ex IMC)
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/253910
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