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

MakaleAçık ErişimScopus SJRQ2

Özet

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.

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https://rdlopen.rawdatalibrary.net/r/munzur/2808Resmi atıflarda kullanılan kalıcı adres
DOI
https://doi.org/10.1002/slct.202203365Yayıncı resmi DOI adresi
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20
WoS
19
OpenAlex
18
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Tam Kayıt
AlanDeğerDil
dc.contributor.authorBuldurun, Kenan
dc.contributor.authorAras, Abdülmelik
dc.contributor.authorTuran, Nevin
dc.contributor.authorTurkan, Fikret
dc.contributor.authorAdiguzel, Ragip
dc.contributor.authorBursal, Ercan
dc.date.accessioned2026-10-28T14:55:50.074685643Z
dc.date.available2026-10-28T14:55:50.074685643Z
dc.date.issued2022
dc.description.abstractIn 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.
dc.description.sponsorshipCatalysis Research and Application Center of Inonu University
dc.description.sponsorshipDepartment of Chemistry of Faculty of Arts and Sciences of Mus Alparslan University
dc.description.sponsorshipDepartment of Pharmaceutical Chemistry of Faculty of Pharmacy of Gazi University
dc.identifier.articlenumbere202203365
dc.identifier.doi10.1002/slct.202203365
dc.identifier.issn2365-6549
dc.identifier.issue40
dc.identifier.scopus2-s2.0-85141193270
dc.identifier.urihttps://rdlopen.rawdatalibrary.net/r/munzur/2808
dc.identifier.volume7
dc.identifier.wosWOS:000871744600001
dc.language.isoen
dc.publisherJohn Wiley and Sons Inc
dc.relation.ispartofChemistrySelect
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectAzo dye
dc.subjectbiological studies
dc.subjectenzyme inhibition
dc.subjectM(II) complexes
dc.subjectm-substitute
dc.subject.classificationChemistry, Multidisciplinary
dc.subject.classificationChemistry
dc.subject.otherCARBONIC-ANHYDRASE
dc.subject.otherALZHEIMERS-DISEASE
dc.subject.otherZN(II) COMPLEXES
dc.subject.otherACID
dc.subject.otherNI(II)
dc.subject.otherCU(II)
dc.subject.otherLACTOPEROXIDASE
dc.subject.otherFE(III)
dc.subject.otherCO(II)
dc.titleSynthesis and Characterization of Azo Dye Complexes as Potential Inhibitors of Acetylcholinesterase, Butyrylcholinesterase, and Glutathione S-Transferase
dc.typeArticle
rdl.citation.openalex18
rdl.citation.scopus20
rdl.citation.wos19
rdl.oa.statusgreen
rdl.oa.statuspreprint
rdl.oa.urlhttps://hdl.handle.net/20.500.12639/4953
rdl.scopus.quartileQ2
rdl.source.indexSCOPUS
rdl.source.indexWOS
rdl.wos.indexScience Citation Index Expanded (SCI-EXPANDED)