Evaluation of chalcones as inhibitors of glutathione S-transferase

ÖZASLAN M. S., DEMİR Y., ASLAN H. E., Beydemir S., KÜFREVİOĞLU Ö. İ.

JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY, cilt.32, sa.5, 2018 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 32 Sayı: 5
  • Basım Tarihi: 2018
  • Doi Numarası: 10.1002/jbt.22047
  • Dergi Adı: JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Anahtar Kelimeler: chalcone, glutathione S-transferase, inhibition, purification, ESTERASE-ACTIVITIES, IN-VITRO, BUTYRYLCHOLINESTERASE, ACETYLCHOLINESTERASE, LACTOPEROXIDASE, PURIFICATION, DERIVATIVES, AGENTS
  • Atatürk Üniversitesi Adresli: Evet

Özet

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 EUmg(-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. K-i constants of chalcones were found in the range of 7.76-41.93 M. 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.