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Issue 86, 2013
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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

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Abstract

Interaction of the racemic helical homo-octapeptide made by the achiral Cα-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.

Graphical abstract: 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

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Article information


Submitted
23 Jun 2013
Accepted
02 Sep 2013
First published
02 Sep 2013

Chem. Commun., 2013,49, 10133-10135
Article type
Communication

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

F. Ceccacci, G. Mancini, P. Rossi, P. Scrimin, A. Sorrenti and P. Tecilla, Chem. Commun., 2013, 49, 10133
DOI: 10.1039/C3CC44713H

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