13-Helix folding of a β/γ-peptide manifold designed from a "minimal-constraint" blueprint. Issue 50 (27th May 2016)

• Record Type: Journal Article
• Authors: Grison, Claire M.; Robin, Sylvie; Aitken, David J.
• Is Part Of: Chemical communications. Volume 52:Issue 50(2016)
• Page Start: 7802
• Page End: 7805
• Publication Date: 2016-05-27
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c6cc02142e
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : A bottom-up design rationale was used to select an alternating β/γ-peptide motif which folds into a well-defined 13-helix in solution. 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.