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Fluorogenic protein labeling using a genetically encoded unstrained alkene
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DOI：10.1039/c6sc03635j.png)
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摘要
En 中文
We developed a new fluorogenic bioorthogonal reaction that is based on the inverse electron-demand Diels-Alder reaction between styrene (an unstrained alkene) and a simple tetrazine. The reaction forms a new fluorophore with no literature precedent. We have identified an aminoacyl-tRNA synthetase/tRNA pair for the efficient and site-specific incorporation of a styrene-containing amino acid into proteins in response to amber nonsense codon. Fluorogenic labeling of purified proteins and intact proteins in live cells were demonstrated. The fluorogenicity of the styrene-tetrazine reaction can be potentially applied to the study of protein folding and function under physiological conditions with low background fluorescence interference.
Keyword:
DIELS-ALDER REACTIONS
1,3-DIPOLAR CYCLOADDITION REACTION
UNNATURAL AMINO-ACIDS
MAMMALIAN-CELLS
TRANS-CYCLOOCTENES
CLICK CHEMISTRY
LIVING CELLS
TETRAZINE CYCLOADDITIONS
LIGATION
PROBES
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期刊
IF:
7.4
论文数:
1.7W
被引数:
9.3W
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引用论文
Genetically encoded norbornene directs site-specific cellular protein labelling via a rapid bioorthogonal reaction.png)
NATURE CHEMISTRY
OAAI
NATURE CHEMISTRYIF20.2
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