Issue 14, 2012

Constrained α/γ-peptides: a new stable extended structure in solution without any hydrogen bond and characterized by a four-fold symmetry

Abstract

Small α/γ-peptides alternating α-aminoisobutyric acid and cyclic γ-amino acid residues are described. NMR studies together with restrained simulated annealing revealed that an extended backbone conformation largely dominates in solution for as short as 4-residues long oligomers. This new fold type is devoid of any hydrogen bond and characterized by a four-fold symmetry.

Graphical abstract: Constrained α/γ-peptides: a new stable extended structure in solution without any hydrogen bond and characterized by a four-fold symmetry

Supplementary files

Article information

Article type
Communication
Submitted
04 Nov 2011
Accepted
12 Dec 2011
First published
11 Jan 2012

Chem. Commun., 2012,48, 1982-1984

Constrained α/γ-peptides: a new stable extended structure in solution without any hydrogen bond and characterized by a four-fold symmetry

F. Bouillère, D. Feytens, D. Gori, R. Guillot, C. Kouklovsky, E. Miclet and V. Alezra, Chem. Commun., 2012, 48, 1982 DOI: 10.1039/C2CC16852A

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