Issue 90, 2015

The discovery of 9/8-ribbons, β/γ-peptides with curved shapes governed by a combined configuration-conformation code

Abstract

The de novo design of a β/γ-peptidic foldamer motif has led to the discovery of an unprecedented 9/8-ribbon featuring an uninterrupted alternating C9/C8 hydrogen-bonding network. The ribbons adopt partially curved topologies determined synchronistically by the β-residue configuration and the γ-residue conformation sets.

Graphical abstract: The discovery of 9/8-ribbons, β/γ-peptides with curved shapes governed by a combined configuration-conformation code

  • This article is part of the themed collection: Foldamers

Supplementary files

Article information

Article type
Communication
Submitted
10 ذو القعدة 1436
Accepted
02 ذو الحجة 1436
First published
02 ذو الحجة 1436
This article is Open Access
Creative Commons BY-NC license

Chem. Commun., 2015,51, 16233-16236

Author version available

The discovery of 9/8-ribbons, β/γ-peptides with curved shapes governed by a combined configuration-conformation code

C. M. Grison, S. Robin and D. J. Aitken, Chem. Commun., 2015, 51, 16233 DOI: 10.1039/C5CC07136D

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