Oxidation-Induced Protein Cross-Linking in Mammalian Cells

被引:4
作者
Li, Huanhuan [1 ]
Lv, Langlang
Tang, Shuo [1 ]
Zang, Yiqi [1 ]
Wan, Tianyan [1 ]
Wang, Dexiang [2 ]
Cai, Lingchao [3 ]
Ye, Hui [2 ]
Tan, Renxiang [1 ,4 ]
Wang, Nanxi [1 ]
机构
[1] Nanjing Univ Chinese Med, Sch Pharm, State Key Lab Cultivat Base TCM Qual & Efficacy, Nanjing 210023, Jiangsu, Peoples R China
[2] China Pharmaceut Univ, Jiangsu Prov Key Lab Drug Metab & Pharmacokinet, State Key Lab Nat Med, Nanjing 210009, Jiangsu, Peoples R China
[3] Nanjing Forestry Univ, Coll Chem Engn, Jiangsu Coinnovat Ctr Efficient Proc & Utilizat Fo, Int Innovat Ctr Forest Chem & Mat,Jiangsu Prov Key, Nanjing 210037, Jiangsu, Peoples R China
[4] Nanjing Univ, Inst Funct Biomol, Sch Life Sci, State Key Lab Pharmaceut Biotechnol, Nanjing, Jiangsu, Peoples R China
来源
ACS SYNTHETIC BIOLOGY | 2023年 / 12卷 / 04期
基金
中国国家自然科学基金;
关键词
genetic code expansion; proximity-enabled cross-linking; oxidation-induced protein cross-linking; protein-protein interactions; CRYSTAL-STRUCTURE; THIOREDOXIN;
D O I
10.1021/acssynbio.3c00052
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
A proximity-enabled protein cross-linking strategy with additional spatiotemporal control is highly desirable. Here, we report an oxidation-induced protein cross-linking strategy involving the incorporation of a vinyl thioether group into proteins in both Escherichia coli and mammalian cells via genetic code expansion. We demonstrated that vinyl thioether can be selectively induced by exogenously added oxidant or by reactive oxygen species from the cellular environment, as well as by photocatalysts, and converted into a Michael acceptor, enabling fluorescence labeling and protein cross-linking.
引用
收藏
页码:984 / 992
页数:9
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