Document Type
Article
Publication Date
2020
Digital Object Identifier (DOI)
https://doi.org/10.1126/sciadv.aaz4988
Abstract
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.
Rights Information
This work is licensed under a Creative Commons Attribution-Noncommercial 4.0 License
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Science Advances, v. 6, issue 20, art. eaaz4988
Scholar Commons Citation
Sang, Peng; Zhou, Zhihong; Shi, Yan; Lee, Candy; Amso, Zaid; Huang, David; Odom, Timothy; Nguyen-Tran, Vân T.B.; Shen, Weijun; and Cai, Jianfeng, "The Activity of Sulfono-γ-AApeptide Helical Foldamers that Mimic GLP-1" (2020). Chemistry Faculty Publications. 124.
https://digitalcommons.usf.edu/chm_facpub/124
