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Photocaged activity-based probes for improved monitoring of protein s-sulfenylation in living cells

Chinese Chemical Letters 2024年第2期35卷 451-454页

作者： Jiahao Zhang Haiyue Peng Zi'an Chen Guorui Li Jing Huang state Key Laboratory of Chemo/Biosensing and Chemometrics Hunan Provincial Key Laboratory of Animal Models and Molecular MedicineSchool of Biomedical SciencesHunan UniversityChangsha 410082China

protein s-sulfenylation(protein sulfenic acid),as one of the most significant oxidative post-translational modifications(OxiPTMs),plays a vital role in regulating protein function.A variety of activity-based probes have been developed to profile sulfenic acid in living ***,due to the transient presence and low content of sulfenic acid in living cell,high doses of probes are needed to achieve efficient *** importantly,current probes have no temporal control over sulfenic acid *** overcome these limitations,two caged cysteine sulfenic acid probes DYn-2-ONB and DYn-2-Cou with either an o-nitrobenzyl or coumarin protecting group were developed in this *** probes can be efficiently uncaged via irradiation to produce the active C-nucleophile probe *** assay in living cells demonstrated DYn-2-ONB exhibited better labeling capacity compared with DYn-2,providing it as a powerful tool for improved monitoring of protein s-sulfenylation in living cells.

关键词： Cysteine sulfenic acid Activity-based probe Photocage Light activation protein s-sulfenylation

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An Active Based Multifunctional Probe for Off-On Fluorescent Detection,Labeling and Profiling of protein sulfenic Acid in Cells

An Active Based Multifunctional Probe for Off-On Fluorescent...

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第十一届全国化学生物学学术会议

作者： Man Li Chunrong Liu Key Laboratory of Pesticide and Chemical Biology Ministry of EducationSchool of ChemistryCentral China Normal University

As a significant post-translational modification, protein s-sulfenylation triggered by reactive oxygen species（ROs） could modulate the protein functions, redox homeostasis, various signaling pathways and cellular functions, and is also associated with many diseases. Thus, protein s-sulfenylation is thought as the center of redox biologies and pathologies.[1] However, the dynamic nature of protein s-sulfenylation, transient fate of protein sulfenic acids and the lack of probes which enable the spatial and temporal profiling of intracellular protein s-sulfenylation have hindered our understanding of such redox PTM. Herein we report an active based multifunctional probe（sA-HYD） which enables "off-on" fluorescent detection, labeling and profiling of protein s-sulfenylation within cells. We proved that sA-HYD was capable of not only tracking the intracellular protein s-sulfenylation spatially and temporally, but also capturing and identifying the s-sulfenylated proteins in complex cellular environments. Besides, sA-HYD has been applied successfully in studying the kinetics of protein s-sulfenylation in both physiological buffer and cell lysates. Therefore, we deem that this ABPP probe could provide a robust tool for better understanding the physiological and pathological roles of protein s-sulfenylation.

关键词： redox biology protein s-sulfenylation activity-based protein profiling probe naphthylhydrazine photo-crosslinker

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