A genetically encoded alkyne directs palladium-mediated protein labeling on live mammalian cell surface.
ACS Chem Biol
; 10(2): 379-84, 2015 Feb 20.
Article
em En
| MEDLINE
| ID: mdl-25347611
ABSTRACT
The merging of site-specific incorporation of small bioorthogonal functional groups into proteins via amber codon suppression with bioorthogonal chemistry has created exciting opportunities to extend the power of organic reactions to living systems. Here we show that a new alkyne amino acid can be site-selectively incorporated into mammalian proteins via a known orthogonal pyrrolysyl-tRNA synthetase/tRNACUA pair and directs an unprecedented, palladium-mediated cross-coupling reaction-driven protein labeling on live mammalian cell surface. A comparison study with the alkyne-encoded proteins in vitro indicated that this terminal alkyne is better suited for the palladium-mediated cross-coupling reaction than the copper-catalyzed click chemistry.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Paládio
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Revista:
ACS Chem Biol
Ano de publicação:
2015
Tipo de documento:
Article
País de afiliação:
Estados Unidos