Journal
ANALYTICAL CHEMISTRY
Volume 92, Issue 6, Pages 4371-4378Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.9b05232
Keywords
-
Categories
Funding
- National Natural Science Foundation of China [21778028]
- Ministry of Science and Technology National Key RD Project [2018YFE0205100]
- Natural Science Foundation of Gansu Province [18JR4RA003]
- 111 project
Ask authors/readers for more resources
Vicinal dithiol-containing proteins (VDPs) play an important role in maintaining the structures and functions of proteins mainly through the conversion between dithiols and disulfide bonds. The content of VDPs also reflects the redox status of an organism. To specifically and expediently detect VDPs, we developed a turn-on monoarsenical fluorescent probe (NEP) based on the intramolecular charge transfer mechanism. Naphthalimide was chosen as a fluorophore and linked with the receptor moiety (cyclic dithiarsolane) via carbamate segment. In the presence of VDPs, NEP displays a strong green fluorescence signal produced by the cyclic dithiarsolane cleavage and subsequent intramolecular cyclization to liberate the fluorophore. Furthermore, NEP exhibits high selectivity toward VDPs over other protein thiols and low molecular weight thiols. The favorable properties of NEP enable it readily to detect 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available