Low-Toxicity Sulfonium-Based Probes for Cysteine-Specific Profiling in Live Cells
2022
Wang, Rui | Yang, Dongyan | Tian, Tian | An, Yuhao | Wan, Chuan | Chang, Qi | Liang, Mingchan | Hou, Zhanfeng | Wang, Ying | Zhang, Liang | Li, Zigang
Despite being a low-abundance amino acid, cysteine plays an essential role in regulating protein function and serves as a satisfactory target of post-translational modifications and drug developments. To comprehensively assess reactive-cysteine-containing proteins, the development of chemical proteomic probes to label cysteine residues in human cells is an important objective. Cysteine modification using sulfonium-based probes is a novel method to identify reactive cysteine residues in proteins. Herein, we reported a set of “cysteine-reactive sulfonium-based (C-Sul)” probes to label the reactive cysteine sites in cellular proteins. Notably, water-soluble C-Sul probes have a significantly enhanced stability and cellular uptakes, displaying a high specificity toward reactive cysteines and compatibility with quantitative proteomic profiling. In comparison to the conventional iodoacetamide-based probe, C-Sul particularly has no inhibitory effects on cell viability, enabling its application in proteomic profiling of reactive cysteine residues under biorelevant conditions. We propose C-Sul probes as optimal tools of cysteine profiling for further broadly basic research.
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Эту запись предоставил National Agricultural Library