RESUMO
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.
Assuntos
5-Hidroxitriptofano/química , Compostos de Anilina/química , Proteínas de Fluorescência Verde/química , 5-Hidroxitriptofano/genética , Escherichia coli/genética , Proteínas de Fluorescência Verde/genética , Oxirredução , Engenharia de Proteínas/métodosRESUMO
The synthesis of small molecule based 1,3,5-trisubstituted benzenes for photo-mediated capture of human carbonic anhydrase II with visualisation by fluorescence is described.