title: 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.
authors.affiliation: Univ Paris-Sud, Laboratoire de Chimie des Procédés et Substances Naturelles, ICMMO, UMR 8182, CNRS, Bât 410, Orsay, F-91405, France.
authors.forename: Francelin
authors.initials: F
authors.lastname: Bouillère
authors.forename: Debby
authors.initials: D
authors.lastname: Feytens
authors.forename: Didier
authors.initials: D
authors.lastname: Gori
authors.forename: Régis
authors.initials: R
authors.lastname: Guillot
authors.forename: Cyrille
authors.initials: C
authors.lastname: Kouklovsky
authors.forename: Emeric
authors.initials: E
authors.lastname: Miclet
authors.forename: Valérie
authors.initials: V
authors.lastname: Alezra
mesh_terms: D006860:Hydrogen Bonding; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D012996:Solutions / Q000737:chemistry
chemical_list: D010455:Peptides; D012996:Solutions