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Updated: Feb 14, 2026

Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases
Published on: October 10, 2020
Evaluation of chalcones as inhibitors of glutathione S-transferase
Muhammet Serhat Özaslan1, Yeliz Demir1, Hatice Esra Aslan1
1Faculty of Sciences, Department of Chemistry, Atatürk University, Erzurum, 25240, Turkey.
Abstract:
Glutathione S-transferases (GSTs) are the superfamily of multifunctional detoxification isoenzymes and play an important role in cellular signaling. In the present study, potential inhibition effects of chalcones were tested against human GST. For this purpose, GST was purified from human erythrocytes with 5.381 EU⋅mg-1 specific activity and 51.95% yield using a GSH-agarose affinity chromatographic method. The effects of chalcones on in vitro GST activity were tested at various concentrations. Ki constants of chalcones were found in the range of 7.76-41.93 μM. According to the results, 4-fluorochalcone showed a better inhibitory effect compared with the other compounds. The inhibition mechanisms of 2'-hydroxy-4-methoxychalcone and 4-methoxychalcone were noncompetitive, whereas the inhibition mechanisms of 4'- hydroxychalcone, 4- fluorochalcone, and 4,4'- diflurochalcone were competitive.
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