期刊
ACS CHEMICAL BIOLOGY
卷 10, 期 2, 页码 379-384出版社
AMER CHEMICAL SOC
DOI: 10.1021/cb500649q
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资金
- National Institutes of Health [GM 085092]
- National Science Foundation [CHE-1305826]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1305826] Funding Source: National Science Foundation
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/tRNA(CUA) 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.
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