Inhibition effects of isoproterenol, chlorpromazine, carbamazepine, tamoxifen drugs on glutathione S-transferase, cholinesterases enzymes and molecular docking studies

Creative Commons License

Turkan F., Calimli M. H. , Kanberoğlu G. S. , Karaman M.

JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, 2020 (Peer-Reviewed Journal) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume:
  • Publication Date: 2020
  • Doi Number: 10.1080/07391102.2020.1763200
  • Journal Indexes: Science Citation Index Expanded, Scopus, BIOSIS, Chemical Abstracts Core, EMBASE, MEDLINE


Nowadays, inhibition of acetylcholinesterase (AChE), butyrylcholinesterase (BChE) and glutathione S-transferases (GSTs) have been a very crucial issue for pharmacological treatments of several disasters. Herein, we investigated inhibition effects of Tamoxifen (TAM), Isoprenaline (ISO), Chlorpromazines (CPZ) and Carbamazepine (CBZ) on GST, AChE, BChE and then molecular structures and active sides of the tested drugs by molecular docking process. The enzyme activity results showed that nearly the whole tested drugs inhibited GST, BChE, AChE efficiently. Chlorpromazine was found to be the best inhibitor for the GST enzyme and the Ki value of this drug was found to be 42.83 +/- 8.52 nM. Besides, Isoproterenol drug with the Ki value of 51.80 +/- 9.44 nM was found to be the most effective inhibitor on the AChE enzyme. Molecular docking studies showed that the receptor-binding sites of GST, AChE, and BChE were found to 1.069, 1.090, and 1.15 of Sitecore and 0.992, 1.113, and 1.217 of Dscore, respectively. The method was validated by doing validation studies and these validations revealed that re-docked ligands located a very closed position with co-crystallized ligand into the active site for all receptors. Calculation studies for determining the possible enzyme inhibition mechanism with the used drugs revealed that amino and aromatic ring in the structure of the drugs used are effective in inhibition reactions. Communicated by Ramaswamy H. Sarma