Donmez, Melike; Sekerci, Memet; Adiguzel, Ragip; Oğuz, Ercan; Türkan, Fikret; Yildiko, Umit; Colak, Naki

In this study, firstly, bis(thiosemicarbazone) ligand [L: 2,2′-(2-(2-(4-methoxyphenyl)hydrazineylidene)cyclohexane-1,3-diylidene)bis(hydrazine-1-carbothioamide)] was synthesized by the condensation reaction of thiosemicarbazide and ketone compound (2-(2-(4-methoxyphenyl)hydrazone)cyclohexane-1,3-dione). The metal complexes were synthesized by the reaction of obtained ligand (L) with CuCl2·2H2O, NiCl2·6H2O, CoCl2·6H2O, and MnCl2·4H2O salts. The structures of synthesized ligand and their complexes were characterized using elemental analysis, IR, UV–Vis, 1H-NMR spectra, 13C-NMR spectra, magnetic susceptibility, mass spectra (LC–MS), thermogravimetry analysis-differential thermal analysis (TGA-DTA), and differential scanning calorimetry techniques. According to the results of the analysis, square plane geometry was suggested for Cu and Co complexes. However, the structures of Ni and Mn complexes were in agreement with octahedral geometry. Molecular docking analysis and pharmacological potential of the compound were evaluated to determine the inhibitory potential against acetylcholinesterase (AChE) and Glutathione-S-transferases (GST) enzymes. The compound exhibited strong binding/docking indices of − 5.708 and − 5.928 kcal/mol for the respective receptors. In addition, L–Ni(II) complex was found to be the most effective inhibitor for AChE enzyme with a Ki value of 0.519. However, with a Ki value of 1.119, L–Cu(II) complex was also found to be an effective inhibitor for the GST enzyme.

AtıfScopus21·OpenAlex19

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Adiguzel, Ragip; Türkan, Fikret; Yildiko, Ümit; Aras, Abdülmelik; Evren, Enes; Onkol, Tijen

Novel Ru(II) complexes of Shiff base derivatives of 3-[(4-amino-5-thioxo-1,2,4-triazole-3-yl)methyl]-2(3H)-benzoxazolone were synthesized. The ligands (1a-e) were confirmed by IR, 1H NMR, and 13C NMR spectra (only 1b and 1c). Structures of the synthesized Ru(II) complexes (2a-e) were illuminated by elemental analysis, IR, 1H NMR, 13C NMR, and mass spectra. As the biological studies, the inhibitory potency of the ligands and the novel synthesized complexes were evaluated against the glutathione S-transferase (GST), acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzymes in vitro conditions. Ki values in the range of 26.87-47.63 µM for AChE, 23.51-42.81 µM for BChE, and 33.14-51.73 µM for GST, respectively. The free binding energy of most active inhibitors against AChE, BChE, and GST enzymes were detected as -10.183 kcal/mol, -9.111 kcal/mol, and -6.097 kcal/mol, respectively. All compounds docked were observed to bind in the active site of the enzymes with similar binding orientation and binding interactions with the surrounding amino acids.

AtıfScopus31·OpenAlex34

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