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A reactivity-based probe for off-on fluorescent detection, labeling, and profiling of protein S-sulfenylation in cells

Protein S-sulfenylation modulates protein functions, redox homeostasis, various signaling pathways and cellular functions, and is thus associated with many diseases. However, the dynamic nature, transient fate of protein sulfenic acids, and the lack of probes which enable the spatial and temporal pr...

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Published in:Sensors and actuators. B, Chemical Chemical, 2022-03, Vol.354, p.131235, Article 131235
Main Authors: Li, Man, Wang, Bing, Li, Mengzhao, Li, Xiang, Wang, Li, Li, Na, Rao, Li, Wan, Cuihong, Liu, Changlin, Liu, Chunrong
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Language:English
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Summary:Protein S-sulfenylation modulates protein functions, redox homeostasis, various signaling pathways and cellular functions, and is thus associated with many diseases. However, the dynamic nature, transient fate of protein sulfenic acids, and the lack of probes which enable the spatial and temporal profiling of intracellular S-sulfenylation have hindered our understanding of this redox PTM. Herein, we reported a novel reaction of sulfenic acid towards arylhydrazine with high efficiency, and a multifunctional probe SA-HYD based on this reaction which enables “off-on” fluorescent detection, labeling and profiling of protein S-sulfenylation within cells. SA-HYD was applied successfully in “off-on” fluorescent imaging, in situ fluorescent labeling of intracellular protein sulfenic acids and LPA-mediated signaling research in prostate cancer cells. We expect this probe could provide a convenient and robust tool for better understanding the physiological and pathological roles of protein S-sulfenylation. [Display omitted] •A novel recognition reaction of sulfenic acid towards arylhydrazine with high efficiency was reported.•An “off-on” fluorescent sensor SA-HYD for protein sulfenic acid with excellent selectivity and sensitivity was reported.•SA-HYD could assessed directly the dynamic transient protein sulfenic acid in cells as well as the cellular redox state.•SA-HYD possessed the ability to label sulfenylated proteins in situ.
ISSN:0925-4005
1873-3077
DOI:10.1016/j.snb.2021.131235