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Decrease of protein vicinal dithiols in Parkinsonism disclosed by a mono-arsenical fluorescent probe.

Vicinal dithiol-containing proteins (VDPs) play an important role in maintaining the structures and functions of proteins through the conversion between dithiols and disulfide bonds. The content of VDPs reflects the redox status of an organism. To specifically and expediently detecting VDPs, we developed a turn-on mono-arsenical fluorescent probe (NEP) based on the intramolecular charge transfer mechanism. The naphthalimide was chosen as a fluorophore and linked with the receptor moiety (cyclic dithi-aarsane) via carbamate segment. In the presence of VDPs, NEP displays a strong green fluorescence signal produced by the cyclic dithiaarsane cleavage and subsequent intramolecular cyclization to liberate fluorophore. Furthermore, NEP exhibits high selectivity towards VDPs over other protein thiols and low molecular weight thiols. The favorable properties of NEP enable it readily to de-tect VDPs in live cells and in vivo. In addition, a remarkable decrease of VDPs in Parkinsonism was disclosed for the first time, highlighting that regulating VDPs level has a therapeutic potential for Parkinsonism.