Modular synthesis of clickable peptides via late-stage maleimidation on C(7)-H tryptophan.

ABSTRACT: Cyclic peptides have attracted tremendous attention in the pharmaceutical industry owing to their excellent cell penetrability, stability, thermostability, and drug-like properties. However, the currently available facile methodologies for creating such peptides are rather limited. Herein, we report an efficient and direct peptide cyclization via rhodium(III)-catalyzed C(7)-H maleimidation. Notably, this catalytical system has excellent regioselectivity and high tolerance of functional groups which enable late-stage cyclization of peptides. This architecture of cyclic peptides exhibits higher bioactivity than its parent linear peptides. Moreover, the Trp-substituted maleimide displays excellent reactivity toward Michael addition, indicating its potential as a click functional group for app

SUBMITTER: Wang P 

PROVIDER: S-EPMC10322970 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature