4.4 Article

Synthesis and Characterization of Azo Dye Complexes as Potential Inhibitors of Acetylcholinesterase, Butyrylcholinesterase, and Glutathione S-Transferase

Journal

CHEMISTRYSELECT
Volume 7, Issue 40, Pages -

Publisher

WILEY-V C H VERLAG GMBH
DOI: 10.1002/slct.202203365

Keywords

Azo dye; m-substitute; M(II) complexes; biological studies; enzyme inhibition

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Metal complexes of an azo dye ligand (ADL) were synthesized, characterized, and evaluated for their biological activities. The Co(II) complex exhibited the most effective enzyme inhibition against GST, AChE, and BChE enzymes, indicating its potential as a pharmaceutical agent.
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)), H-1-C-13 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 K-i values of Co(II) complex against all three GST (19.48 +/- 2.17 mu M), AChE (22.14 +/- 3.74 mu M), and BChE (26.39 +/- 3.19 mu M) 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.

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