Site-selective photocatalytic functionalization of peptides and proteins at selenocysteine.

ABSTRACT: The importance of modified peptides and proteins for applications in drug discovery, and for illuminating biological processes at the molecular level, is fueling a demand for efficient methods that facilitate the precise modification of these biomolecules. Herein, we describe the development of a photocatalytic method for the rapid and efficient dimerization and site-specific functionalization of peptide and protein diselenides. This methodology, dubbed the photocatalytic diselenide contraction, involves irradiation at 450 nm in the presence of an iridium photocatalyst and a phosphine and results in rapid and clean conversion of diselenides to reductively stable selenoethers. A mechanism for this photocatalytic transformation is proposed, which is supported by photoluminescence spectroscop

SUBMITTER: Dowman LJ 

PROVIDER: S-EPMC9653470 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature