Issue 69, 2014

Stabilization of β-peptide helices by direct attachment of trifluoromethyl groups to peptide backbones

Abstract

The 14-helix structure of oligo-β-peptides was significantly stabilized by direct attachment of CF3 groups to their backbones. Our studies indicate that this stabilization originates from the CF3-promoted increase in the intramolecular hydrogen-bonding ability of their backbone amides, leading to a novel strategy to stabilize peptide folding.

Graphical abstract: Stabilization of β-peptide helices by direct attachment of trifluoromethyl groups to peptide backbones

Supplementary files

Article information

Article type
Communication
Submitted
22 Mar 2014
Accepted
30 Jun 2014
First published
08 Jul 2014

Chem. Commun., 2014,50, 9855-9858

Author version available

Stabilization of β-peptide helices by direct attachment of trifluoromethyl groups to peptide backbones

J. Cho, K. Sawaki, S. Hanashima, Y. Yamaguchi, M. Shiro, K. Saigo and Y. Ishida, Chem. Commun., 2014, 50, 9855 DOI: 10.1039/C4CC02136C

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