ja9b12116_si_001.pdf (5.67 MB)
2H‑Azirine-Based Reagents for Chemoselective Bioconjugation at Carboxyl Residues Inside Live Cells
journal contribution
posted on 2020-03-23, 11:43 authored by Nan Ma, Jun Hu, Zhi-Min Zhang, Wenyan Liu, Minhao Huang, Youlong Fan, Xingfeng Yin, Jigang Wang, Ke Ding, Wencai Ye, Zhengqiu LiProtein 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.
History
Usage metrics
Categories
Keywords
lysine residuesprotein functionchemical reagentsCarboxyl Residues3- phenyl -2 Hchemoselective modificationChemoselective Bioconjugationcarboxyl residuesnovel methodscovalent modificationreactive carboxyl residuesnovel reactive probecarboxyl groupschemoproteomic platformLive Cells Protein modification
Licence
Exports
RefWorks
BibTeX
Ref. manager
Endnote
DataCite
NLM
DC