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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.

SUBMITTER: Cheung CHP

PROVIDER: S-EPMC8153220 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature

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Construction of diverse peptide structural architectures <i>via</i> chemoselective peptide ligation.

Cheung Carina Hey Pui CHP Xu Jianchao J Lee Chi Lung CL Zhang Yanfeng Y Wei Ruohan R Bierer Donald D Huang Xuhui X Li Xuechen X

Chemical science 20210413 20

Herein, we report the development of a facile synthetic strategy for constructing diverse peptide structural architectures <i>via</i> 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 pep ...[more]

PMID: 34123337

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