Issue 69, 2014
From the journal:

Chemical Communications

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

Joonil Cho,a   Kyohei Sawaki,b   Shinya Hanashima,c   Yoshiki Yamaguchi,c   Motoo Shiro,d   Kazuhiko Saigoe  and  Yasuhiro Ishida*a  

* Corresponding authors

a RIKEN Center for Emergent Matter Science, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan
E-mail: y-ishida@riken.jp

b Department of Chemistry and Biotechnology, School of Engineering, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-8656, Japan

c RIKEN Global Research Cluster, Structural Glycobiology Team, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan

d Rigaku Corporation, 3-9-12 Matsubara-cho, Akishima, Tokyo 196-8666, Japan

e School of Environmental Science and Engineering, Kochi University of Technology, Miyanokuchi, Tosayamada-cho, Kami, Kochi 782-8502, Japan

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

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Article information

DOI
https://doi.org/10.1039/C4CC02136C
Article type
Communication
Submitted
22 Mar 2014
Accepted
30 Jun 2014
First published
08 Jul 2014

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

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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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