Issue 14, 2012
From the journal:

Chemical Communications

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

Francelin Bouillère,a   Debby Feytens,b   Didier Gori,a   Régis Guillot,a   Cyrille Kouklovsky,a   Emeric Miclet*b  and  Valérie Alezra*a  

* Corresponding authors

a Univ Paris-Sud, Laboratoire de Chimie des Procédés et Substances Naturelles, ICMMO, UMR 8182, CNRS, Bât 410, Orsay, France
E-mail: valerie.alezra@u-psud.fr
Fax: +33 1 69 15 46 79
Tel: +33 1 69 15 76 50

b Univ Paris 06, Laboratoire des BioMolécules, UMR 7203 CNRS-UPMC-ENS, 4 Place Jussieu, France
E-mail: emeric.miclet@upmc.fr
Fax: +33 1 44 27 71 50
Tel: +33 1 44 27 31 15

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

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Article information

DOI
https://doi.org/10.1039/C2CC16852A
Article type
Communication
Submitted
04 Nov 2011
Accepted
12 Dec 2011
First published
11 Jan 2012

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

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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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