β-Carbonyl sulfonium enables cysteine-specific bioconjugation for activity-based protein profiling in live cells

被引:1
|
作者
Wan, Chuan [3 ]
Yang, Dongyan [4 ]
Guo, Xiaochun [1 ]
Zhang, Tuanjie [2 ]
Ruan, Zhijun [2 ]
Dai, Chuan [2 ]
Xing, Yun [1 ]
Yin, Feng [1 ,2 ]
Wang, Rui [2 ]
Li, Zigang [1 ,2 ]
机构
[1] Peking Univ, Sch Chem Biol & Biotechnol, State Key Lab Chem Oncogen, Shenzhen Grad Sch, Shenzhen 518055, Peoples R China
[2] Shenzhen Bay Lab, Pingshan Translat Med Ctr, Shenzhen 518055, Peoples R China
[3] Shenzhen Technol Univ, Coll Hlth Sci & Environm Engn, Shenzhen 518118, Peoples R China
[4] Zhongkai Univ Agr & Engn, Innovat Inst Plant Hlth, Coll Chem & Chem Engn, Guangzhou 510225, Peoples R China
关键词
PEPTIDE;
D O I
10.1039/d4cc00295d
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Chemical labeling methods for proteins are highly researched. Herein, we introduced beta-carbonyl sulfonium compounds for selective cysteine modification in proteins within biological systems. Structural tuning led to sulfonium-based probes with high reactivity and selectivity. These probes show excellent biocompatibility, cell uptake, and specificity towards cysteine profiling in live cells. Small electrophilic molecules have previously been reported to monitor different reactivities or covalent ligand abilities of nucleophilic residues in proteins. Herein, we develop beta-carbonyl sulfonium compounds to selectively modify cysteines in peptides and proteins in live cells.
引用
收藏
页码:3725 / 3728
页数:4
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