Abstract
Cellular redox homeostasis is predominantly controlled by the ratio of thiols and disulfides, and reversible thiol-disulfide exchange reactions are fundamental of the biological redox regulation. However, due to the dynamic exchanges of thiols and disulfides, the detection, especially the in situ detection, of protein disulfides (PDS) is challenging. We employ the strategy, i.e., the increase of emission upon an environment-sensitive dye binding to proteins, to design PDS probes and discover a two-photon probe PDSTP590 (S6) that selectively recognizes PDS in live organisms. With the aid of the probe, we further disclose the elevation of PDS in brains of the mouse stroke model.
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