title: A genetically encoded alkyne directs palladium-mediated protein labeling on live mammalian cell surface.
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.
authors.affiliation: Department of Chemistry, State University of New York at Buffalo , Buffalo, New York 14260, United States.
authors.forename: Nan
authors.initials: N
authors.lastname: Li
authors.forename: Carlo P
authors.initials: CP
authors.lastname: Ramil
authors.forename: Reyna K V
authors.initials: RK
authors.lastname: Lim
authors.forename: Qing
authors.initials: Q
authors.lastname: Lin
mesh_terms: D066246:ErbB Receptors / Q000235:genetics / Q000378:metabolism; D005786:Gene Expression Regulation; D049452:Green Fluorescent Proteins / Q000235:genetics / Q000378:metabolism; D057809:HEK293 Cells; D006801:Humans; D018613:Microscopy, Confocal; D008958:Models, Molecular; D010165:Palladium / Q000737:chemistry*; D011487:Protein Conformation; D013194:Staining and Labeling
chemical_list: C485184:enhanced green fluorescent protein; D049452:Green Fluorescent Proteins; D010165:Palladium; C512478:EGFR protein, human; D066246:ErbB Receptors