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Issue 50, 2017
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A precisely positioned chiral center in an i, i + 7 tether modulates the helicity of the backbone peptide

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Abstract

In some cases, helical peptides stabilized by an i, i + 7 tether exhibit better target binding and cellular functions compared to their i, i + 4 analogues. Herein, we carried out a systematic study of the effects of an in-tether chiral center on the i, i + 7 system. We screened the optimal cross linking mode, tether length, in-tether chiral center positions, and absolute configurations. From these studies, we determined that a chiral center of R absolute configuration at the γ-position to the C-terminal of a 10-membered tether could function to efficiently induce helicity of the backbone peptides. This is an important addition to the current i, i + 4 in-tether chiral center induced helicity strategy (CIH strategy), and could have broad biological applications.

Graphical abstract: A precisely positioned chiral center in an i, i + 7 tether modulates the helicity of the backbone peptide

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Publication details

The article was received on 16 May 2017, accepted on 29 May 2017 and first published on 31 May 2017


Article type: Communication
DOI: 10.1039/C7CC03799F
Citation: Chem. Commun., 2017,53, 6728-6731
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    A precisely positioned chiral center in an i, i + 7 tether modulates the helicity of the backbone peptide

    K. Hu, C. Sun, D. Yang, Y. Wu, C. Shi, L. Chen, T. Liao, J. Guo, Y. Liu and Z. Li, Chem. Commun., 2017, 53, 6728
    DOI: 10.1039/C7CC03799F

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