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Qian X.-K.,Institute of Cancer Stem Cell | Wang P.,CAS Dalian Institute of Chemical Physics | Xia Y.-L.,CAS Dalian Institute of Chemical Physics | Dou T.-Y.,CAS Dalian Institute of Chemical Physics | And 6 more authors.
Sensors and Actuators, B: Chemical | Year: 2016

Catechol-O-methyltransferase (COMT), one of the most important phase II drug metabolizing enzymes, plays important roles in the metabolism of endogenous and xenobiotic catechols. In this study, a highly selective fluorescent probe for sensing activities of catechol-O-methyltransferase in complex biological samples was discovered and well characterized. Under physiological conditions, COMT selectively catalyzes the conversion of the probe (7,8-dihydroxy-4-methylcoumarin, DHMC) to 7-hydroxy-8-methoxy-4-methylcoumarin (HMMC), which brings a strong turn-on fluorescence signal at 520 nm. The probe substrate has been used for monitoring the real activities of COMT in complex biological samples, as well as for rapid screening of potential COMT inhibitors which are useful in the treatment of Parkinson's diseases Furthermore, the probe has been successfully used to monitor endogenous COMT in living cells for the first time, and the results demonstrate that DHMC is cell membrane permeable and low toxic to the cells. All these features of DHMC suggested that this probe holds great promise for COMT-related regulation and inhibition assays in drug discovery, as well as for further investigation on the biological functions of COMT in living cells. © 2016 Elsevier B.V.

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