title: 13-Helix folding of a β/γ-peptide manifold designed from a "minimal-constraint" blueprint.
abstract: A bottom-up design rationale was adopted to devise β/γ-peptide foldamer manifolds which would adopt preferred 13-helix conformations, relying on minimal steric imposition brought by the constituent amino acid residues. In this way, a well-defined 13-helix conformer was revealed for short oligomers of trans-2-aminocyclobutanecarboxylic acid and γ(4)-amino acids in alternation, which gave good topological superposition upon an α-helix motif.
authors.affiliation: CP3A Organic Synthesis Group, ICMMO, UMR 8182, CNRS, Université Paris-Sud, Université Paris-Saclay, 15 Rue Georges Clemenceau, 91405 Orsay cedex, France. david.aitken@u-psud.fr.
authors.forename: Claire M
authors.initials: CM
authors.lastname: Grison
authors.affiliation: CP3A Organic Synthesis Group, ICMMO, UMR 8182, CNRS, Université Paris-Sud, Université Paris-Saclay, 15 Rue Georges Clemenceau, 91405 Orsay cedex, France. david.aitken@u-psud.fr and Université Paris Descartes, UFR Sciences Pharmaceutiques et Biologiques, 4 Avenue de l'Observatoire, 75270 Paris cedex 06, France.
authors.forename: Sylvie
authors.initials: S
authors.lastname: Robin
authors.affiliation: CP3A Organic Synthesis Group, ICMMO, UMR 8182, CNRS, Université Paris-Sud, Université Paris-Saclay, 15 Rue Georges Clemenceau, 91405 Orsay cedex, France. david.aitken@u-psud.fr.
authors.forename: David J
authors.initials: DJ
authors.lastname: Aitken