This research uncovers a novel method for real-time detection and simultaneous labeling of sulfhydryl residues, indicating potential in proteomics.
Real-time detection and identification of modified cysteine sulfhydryl (Cys-SH) residues are important because supersulfidation (S-sulfhydrylation) alters protein function and thereby modulates the activity of biological systems. Although fluorescence probes for rapid, sensitive detection and biotin tag-switch methods for comprehensive labeling of modified residues at the proteome level have been developed, simultaneous detection and labeling have not been achieved in a single system. Herein, we describe dinitrobenzene-based fluorogenic probes with tunable electrophilicity, which react rapidly and selectively with highly nucleophilic supersulfides such as cysteine persulfide (Cys-SSH) and Na2S2 and simultaneously label Cys-SSH itself with a dinitrobenzene tag.
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Kawaguchi et al. (2025) studied this question.
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