Issue 20, 2021

Construction of diverse peptide structural architectures via chemoselective peptide ligation

Abstract

Herein, we report the development of a facile synthetic strategy for constructing diverse peptide structural architectures via chemoselective peptide ligation. The key advancement involved is to utilize the benzofuran moiety as the peptide salicylaldehyde ester surrogate, and Dap–Ser/Lys–Ser dipeptide as the hydroxyl amino functionality, which could be successfully introduced at the side chain of peptides enabling peptide ligation. With this method, the side chain-to-side chain cyclic peptide, branched/bridged peptides, tailed cyclic peptides and multi-cyclic peptides have been designed and successfully synthesized with native peptidic linkages at the ligation sites. This strategy has provided an alternative strategic opportunity for synthetic peptide development. It also serves as an inspiration for the structural design of PPI inhibitors with new modalities.

Graphical abstract: Construction of diverse peptide structural architectures via chemoselective peptide ligation

Supplementary files

Article information

Article type
Edge Article
Submitted
01 Mar 2021
Accepted
13 Apr 2021
First published
13 Apr 2021
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2021,12, 7091-7097

Construction of diverse peptide structural architectures via chemoselective peptide ligation

C. H. P. Cheung, J. Xu, C. L. Lee, Y. Zhang, R. Wei, D. Bierer, X. Huang and X. Li, Chem. Sci., 2021, 12, 7091 DOI: 10.1039/D1SC01174J

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