Issue 50, 2016

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 γ4-amino acids in alternation, which gave good topological superposition upon an α-helix motif.

Graphical abstract: 13-Helix folding of a β/γ-peptide manifold designed from a “minimal-constraint” blueprint

  • This article is part of the themed collection: Foldamers

Supplementary files

Article information

Article type
Communication
Submitted
10 Marts 2016
Accepted
09 Maijs 2016
First published
12 Maijs 2016
This article is Open Access
Creative Commons BY license

Chem. Commun., 2016,52, 7802-7805

13-Helix folding of a β/γ-peptide manifold designed from a “minimal-constraint” blueprint

C. M. Grison, S. Robin and D. J. Aitken, Chem. Commun., 2016, 52, 7802 DOI: 10.1039/C6CC02142E

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements