1. Genetic incorporation of a 2-naphthol group into proteins for site-specific azo coupling.
- Author
-
Chen S and Tsao ML
- Subjects
- Amino Acyl-tRNA Synthetases genetics, Amino Acyl-tRNA Synthetases metabolism, Directed Molecular Evolution methods, Escherichia coli chemistry, Escherichia coli metabolism, Escherichia coli Proteins chemistry, Escherichia coli Proteins metabolism, Methanococcus enzymology, Methanococcus genetics, Models, Molecular, Naphthols chemistry, Protein Engineering methods, Tyrosine metabolism, Escherichia coli genetics, Escherichia coli Proteins genetics, Naphthols metabolism, Tyrosine analogs & derivatives, Tyrosine genetics
- Abstract
The 2-naphthol analogue of tyrosine, 2-amino-3-(6-hydroxy-2-naphthyl)propanoic acid (NpOH), has been genetically introduced into proteins in Escherichia coli . This is achieved through the directed evolution of orthogonal aminoacyl-tRNA synthetase/tRNA pairs that selectively charge the target amino acid in response to the amber stop codon, UAG. Moreover, chemoselective azo coupling reactions have been revealed between the 2-naphthol group and diazotized aniline derivatives that are substituted with an electron donating moiety. The coupling reactions required a very mild condition (pH 7) with great reaction rate (less than 2 h at 0 °C), high efficiency, and excellent selectivity.
- Published
- 2013
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