An Oxidative Bioconjugation Strategy Targeted to a Genetically Encoded 5-Hydroxytryptophan.

ABSTRACT: Approaches that enable the chemoselective, covalent modification of proteins in a site-specific manner have emerged as a powerful technology for a wide range of applications. The electron-rich unnatural amino acid 5-hydroxytryptophan was recently genetically encoded in both Escherichia coli and eukaryotes, thereby allowing its site-specific incorporation into virtually any recombinant protein. Herein, we report the chemoselective conjugation of various aromatic amines to full-length proteins under mild, oxidative conditions that target this site-specifically incorporated 5-hydroxytryptophan residue.

SUBMITTER: Sarathi Addy P 

PROVIDER: S-EPMC6392015 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature