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Genetic incorporation of a 2-naphthol group into proteins for site-specific azo coupling.
- Source :
-
Bioconjugate chemistry [Bioconjug Chem] 2013 Oct 16; Vol. 24 (10), pp. 1645-9. Date of Electronic Publication: 2013 Oct 02. - Publication Year :
- 2013
-
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.
- 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
Subjects
Details
- Language :
- English
- ISSN :
- 1520-4812
- Volume :
- 24
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- Bioconjugate chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 24073629
- Full Text :
- https://doi.org/10.1021/bc400168u