Deracemization and the first CD spectrum of a 3(10)-helical peptide made of achiral α-amino-isobutyric acid residues in a chiral membrane mimetic environment.
Interaction of the racemic helical homo-octapeptide made by the achiral C(α)-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.
CNR, Istituto di Metodologie Chimiche, c/o University of Rome "Sapienza", Department of Chemistry, p.le A. Moro 5, I-00165 Roma, Italy. giovanna.mancini@uniroma1.it.
Francesca
F
Ceccacci
Giovanna
G
Mancini
Paola
P
Rossi
Paolo
P
Scrimin
Alessandro
A
Sorrenti
Paolo
P
Tecilla
D000409:Alanine / Q000737:chemistry*; D000621:Aminoisobutyric Acids / Q000737:chemistry*; D032701:Biomimetics; D002942:Circular Dichroism; D008566:Membranes / Q000737:chemistry*; D000432:Methanol / Q000737:chemistry*; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry*; D013237:Stereoisomerism
D000621:Aminoisobutyric Acids; D010455:Peptides; C100049:2-aminoisobutyric acid; D000409:Alanine; D000432:Methanol