Browsing by Author "Asadove, Elsevar"

Now showing 1 - 1 of 1

Dual Inhibition of AChE and GST by 1,2,4-Triazine Integrated Biochemical, Computational, and Hepatotoxicity Insights
(Wiley, 2025) Oguz, Ercan; Tulek, Gizem Sertkaya; Asadove, Elsevar; Cetin, Adnan; Turkan, Fikret
1,2,4-Triazine-3-amines (TzAs) are a group of compounds having a triazine ring and generally have a heterocyclic structure containing three nitrogen atoms. Studies have revealed that these compounds may exhibit antitumor, antimicrobial, anti-inflammatory, and antiviral properties. For this reason, they are examined as potential drug candidates in pharmaceutical research. In this study, the cytotoxic effect of the TzA molecule on the human hepatocellular carcinoma cell line (HepG2) was examined at 24 and 48 h. TzA solutions were prepared at a concentration of 200-3.125 mu M using both 5% dimethyl sulphoxide (DMSO) and distilled water as solvents. MTT (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide) colorimetric assay was used for in vitro cytotoxicity study. When the results were evaluated, it was seen that cell viability decreased significantly in parallel with the concentration in both 24 and 48 h. In the other stage of the study, the inhibitory effect of the TzA molecule on glutathione S-transferase (GST) and acetylcholinesterase (AChE) enzymes was examined. IC50 values were found to be 9.365 and 10.043 mu M, respectively, while Ki values were determined as 4.369 +/- 0.121 and 3.356 +/- 1.669 mu M, respectively. Tacrin (Tac) and ethacrynic acid (INN) were used as standard drugs. Ki values of the standards for both enzymes were found to be 3.613 +/- 0.524 and 2.918 +/- 0.455 mu M, respectively. As a result, it was shown that TzA was a better inhibitor for the AChE enzyme. Furthermore, the binding energies, amino acid residues, and bond lengths of the complexes were determined by molecular docking of the TzA molecule with selected proteins.