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Conformations of peptides containing a chiral cyclic α, α-disubstituted α-amino acid within the sequence of Aib residues

✍ Scribed by Yosuke Demizu; Masakazu Tanaka; Mitsunobu Doi; Masaaki Kurihara; Haruhiro Okuda; Hiroshi Suemune

Publisher
John Wiley and Sons
Year
2010
Tongue
English
Weight
231 KB
Volume
16
Category
Article
ISSN
1075-2617

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✦ Synopsis

Abstract

A single chiral cyclic α,α‐disubstituted amino acid, (3__S__,4__S__)‐1‐amino‐(3,4‐dimethoxy)cyclopentanecarboxylic acid [(S,S)‐Ac~5~c^dOM^], was placed at the N‐terminal or C‐terminal positions of achiral α‐aminoisobutyric acid (Aib) peptide segments. The IR and ^1^H NMR spectra indicated that the dominant conformations of two peptides Cbz‐[(S,S)‐Ac~5~c^dOM^]‐(Aib)~4~‐OEt (1) and Cbz‐(Aib)~4~‐[(S,S)‐Ac~5~c^dOM^]‐OMe (2) in solution were helical structures. X‐ray crystallographic analysis of 1 and 2 revealed that a left‐handed (M) 3~10~‐helical structure was present in 1 and that a right‐handed (P) 3~10~‐helical structure was present in 2 in their crystalline states. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.

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