A chemical approach for the specific generation of cysteine sulfinylation

Oxidative modifications of protein cysteines play a crucial role in regulating redox homeostasis, redox signaling, and protein function. One of the modifications involves the oxidation of a cysteine thiol to a sulfinic acid (R-SO2H) which has been considered a marker for oxidative stress and an impo...

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Bibliographic Details
Published in:Tetrahedron letters 2022-12, Vol.114
Main Authors: Day, Jacob J., Zhang, Tong, Hamsath, Akil, Neill, Deshka L., Xu, Shi, Qian, Wei-Jun, Xian, Ming
Format: Article
Language:English
Subjects:
INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
Post-translational modification
Sulfinylation
Thiol-blocking
Thiols
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Summary:Oxidative modifications of protein cysteines play a crucial role in regulating redox homeostasis, redox signaling, and protein function. One of the modifications involves the oxidation of a cysteine thiol to a sulfinic acid (R-SO2H) which has been considered a marker for oxidative stress and an important activator for certain proteins. Here, in this study, we report a protocol for the selective formation of sulfinic acids on cysteine residues in a simple 3-step operation under mild conditions: thiol-blocking, oxidation, and reduction. The specificity and efficiency of the method were demonstrated by using both small molecule substrates and a protein model.
ISSN:0040-4039
1873-3581