The activity of sulfono-γ-AApeptide helical foldamers that mimic GLP-1 | Zendy

Peng Sang | Zendy; Zhihong Zhou | Zendy; Yan Shi | Zendy; Candy Lee | Zendy; Zaid Amso | Zendy; David Huang | Zendy; Timothy Odom | Zendy; Vân Nguyên-Trân | Zendy; Weijun Shen | Zendy; Jianfeng Cai | Zendy

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The activity of sulfono-γ-AApeptide helical foldamers that mimic GLP-1

Author(s) -

Peng Sang,

Zhihong Zhou,

Yan Shi,

Candy Lee,

Zaid Amso,

David Huang,

Timothy Odom,

Vân Nguyên-Trân,

Weijun Shen,

Jianfeng Cai

Publication year - 2020

Publication title -

science advances

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.928

H-Index - 146

ISSN - 2375-2548

DOI - 10.1126/sciadv.aaz4988

Subject(s) - helix (gastropod) , chemistry , amino acid , receptor , peptide , biological activity , biochemistry , biophysics , combinatorial chemistry , biology , ecology , snail , in vitro

Existing long α-helix mimicking necessitates the retention of most natural amino acid residues to maintain their biological activity. Here, we report the exploration of helical sulfono-γ-AApeptides with entire unnatural backbones for their ability to structurally and functionally mimic glucagon-like peptide 1 (GLP-1). Our findings suggest that efficient construction of novel GLP-1 receptor (GLP-1R) agonists could be achieved with nanomolar potencies. In addition, the resulting sulfono-γ-AApeptides were also proved to display remarkable stability against enzymatic degradation compared to GLP-1, augmenting their biological potential. This alternative strategy of α-helix mimicking, as a proof of concept, could provide a new paradigm to prepare GLP-1R agonists.

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