期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 142, 期 13, 页码 6051-6059出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.9b12116
关键词
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资金
- National Key R&D Program of China [2019YFC1711000]
- National Natural Science Foundation of China [81803389, 21877050]
- Science and Technology Program of Guangdong Province [2017A050506028, 2019B151502025]
- Science and Technology Program of Guangzhou [201704030060, 201805010007]
- China Postdoctoral Science Foundation [2017M622923]
- Natural Science Foundation of Guangdong Province, China [2018A030310651]
Protein modification by chemical reagents has played an essential role in the treatment of human diseases. However, the reagents currently used are limited to the covalent modification of cysteine and lysine residues. It is thus desirable to develop novel methods that can covalently modify other residues. Despite the fact that the carboxyl residues are crucial for maintaining the protein function, few selective labeling reactions are currently available. Here, we describe a novel reactive probe, 3-phenyl-2H-azirine, that enables chemoselective modification of carboxyl groups in proteins under both in vitro and in situ conditions with excellent efficiency. Furthermore, proteome-wide profiling of reactive carboxyl residues was performed with a quantitative chemoproteomic platform.
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