Premium
An Oxidative Bioconjugation Strategy Targeted to a Genetically Encoded 5‐Hydroxytryptophan
Author(s) -
Sarathi Addy Partha,
Italia James S.,
Chatterjee Abhishek
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800111
Subject(s) - bioconjugation , chemistry , residue (chemistry) , biochemistry , recombinant dna , escherichia coli , oxidative phosphorylation , amino acid , combinatorial chemistry , gene
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.