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A microplate-based platform with immobilized human glutathione transferase A1-1 for high-throughput inhibitor screening.
Current Pharmaceutical Biotechnology 2018 October 29
Glutathione transferases (GSTs) catalyze the conjugation of glutathione (GSH) to endogenous and xenobiotic electrophilic compounds and have been involved in the development of resistance toward cancer chemotherapeutic drugs and in the etiology, pathology and progression of several other diseases. In the present work, the human isoenzyme GSTA1-1 (hGSTA1-1) was used to assemble a microplate-based platform for high-throughput screening of inhibitors from plant extracts. The enzyme was immobilized using sol-gel chemistry and deposited as a layer at the bottom surface of 96-well format ELISA microplate. The sensing signal, was based on the inhibition of the colorimetric reaction between 1-chloro-dinitrobenzene (CDNB) and GSH, catalyzed by the sol-gel entrapped enzyme. As a proof of concept, the system was used for screening aqueous extracts from medicinal and aromatic plants with excellent reproducibility. The operational simplicity and the accuracy of this system, suggest that it can be explored as bioanalytical tool with potential use in drug design and development efforts.
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