Late-Stage Aromatic C-H Bond Functionalization for Cysteine/Selenocysteine Bioconjugation.

ABSTRACT: Bioconjugation of peptides and proteins has become an indispensable tool in fundamental biological research and drug development. Herein, we report a copper-mediated efficient cysteine/selenocysteine-specific bioconjugation through direct C-H functionalization of electron-rich arenes under biocompatible reaction conditions. In this method, a series of commercial electron-rich arenes, including natural products and drug molecules, are conjugated to cysteine/selenocysteine-containing peptides and proteins. Furthermore, we show that this new bioconjugation method allows the efficient stapling of peptides, as well as the cross-linking of different peptides to a single arene, all in high yields. The tunable electron density of small molecules enables the selective modification of selenocysteine

SUBMITTER: Zhao Z 

PROVIDER: S-EPMC12412152 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature