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Updated: May 25, 2026

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
Published on: September 28, 2022
Constrained α/γ-peptides: a new stable extended structure in solution without any hydrogen bond and characterized by
Francelin Bouillère1, Debby Feytens, Didier Gori
1Univ Paris-Sud, Laboratoire de Chimie des Procédés et Substances Naturelles, ICMMO, UMR 8182, CNRS, Bât 410, Orsay, F-91405, France.
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.
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