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Issue 69, 2014
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Stabilization of β-peptide helices by direct attachment of trifluoromethyl groups to peptide backbones

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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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Publication details

The article was received on 22 Mar 2014, accepted on 30 Jun 2014 and first published on 08 Jul 2014


Article type: Communication
DOI: 10.1039/C4CC02136C
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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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