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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

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

Sarathi Addy Partha P   Italia James S JS   Chatterjee Abhishek A  

Chembiochem : a European journal of chemical biology 20180601 13


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 und  ...[more]

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