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.
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 / Francesca, Ceccacci; Giovanna, Mancini; Paola, Rossi; Paolo, Scrimin; Alessandro, Sorrenti; Tecilla, Paolo. - In: CHEMICAL COMMUNICATIONS. - ISSN 1359-7345. - STAMPA. - 49:(2013), pp. 10133-10135. [10.1039/c3cc44713h]
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
TECILLA, PAOLO
2013-01-01
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.Pubblicazioni consigliate
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