Published in
Royal Society of Chemistry, Chemical Communications, 86(49), p. 10133, 2013
DOI: 10.1039/c3cc44713h
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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
Journal article published in 2013 by
Francesca Ceccacci 
,
Giovanna Mancini,
Paola Rossi,
Paolo Scrimin,
Alessandro Sorrenti,
Paolo Tecilla
,
Giovanna Mancini,
Paola Rossi,
Paolo Scrimin,
Alessandro Sorrenti,
Paolo Tecilla
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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.