Buldurun, Kenan; Aras, Abdülmelik; Turan, Nevin; Turkan, Fikret; Adiguzel, Ragip; Bursal, Ercan

In this study, several metal(II) complexes (Fe, Co, Zn, and Ru) of an azo dye ligand (ADL) that, apart from pyrazole ring (PR), include anisole having (−OCH3) group at the m-substitue of the phenyl (L: (E)-4-((3-methoxyphenyl)diazenyl)-3-methyl-1H-pyrazol-5-amine) were prepared, characterized, and the biological activity studies were carried out. The structures of complexes were identified by elemental analysis, FTIR, UV-vis, mass spectra (Fe(II) and Co(II)), 1H-13C NMR spectra, and TGA-DTA. The azo ligand and its metal complexes were evaluated for their biological properties according to the enzyme inhibitory activities. The lowest Ki values of Co(II) complex against all three GST (19.48±2.17 μM), AChE (22.14±3.74 μM), and BChE (26.39±3.19 μM) enzymes were verified as the most effective enzyme inhibition. The biological activity results suggest that the obtained complexes have good potentials to be used in further analyses to explore new pharmaceutical agents.

AtıfScopus20·WoS19·OpenAlex18

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Turan, Nevin; Buldurun, Kenan; Adiguzel, Ragip; Aras, Abdülmelik; Turkan, Fikret; Bursal, Ercan

In this study, the novel azo dye FeII, CoII, ZnII, and RuII complexes with an azo dye ligand (L: (E)-4-((4-methoxyphenyl)diazenyl)-3-methyl-1H-pyrazol-5-amine) were synthesized. The structures of the complexes were characterized by FT-IR, elemental analysis, UV-Vis, mass spectra (FeII and CoII), NMR spectra (only diamagnetic ZnII and RuII), thermogravimetric and differential thermal analysis (TGA-DTA). All of the newly synthesized compounds were tested for their biochemical properties, including enzyme inhibitory and antioxidant activities. According to the in vitro ABTS, DPPH, CUPRAC, and FRAP antioxidant methods, the ligand and its metal complexes showed close antioxidant activities to the standards (BHA, BHT, ascorbic acid, and α-tocopherol). Enzyme inhibitions of the metal complexes were investigated against glutathione S-transferase (GST), acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) enzymes. The best inhibition values (Ki) were observed for Ru(II) complex against GST (14.36 ± 2.16 µM), AChE (16.86 ± 2.74 µM), and BChE (14.12 ± 2.04 µM).

AtıfScopus45·WoS45·OpenAlex45

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