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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… Click to show full 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.
Journal Title: ChemBioChem
Year Published: 2018
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