Transition metal complexes of a multidentate Schiff base ligand containing pyridine: synthesis, characterization, enzyme inhibitions, antioxidant properties, and molecular docking studies

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dc.authoridMurahari, Manikanta / 0000-0002-5404-4426
dc.authoridBursal, Ercan / 0000-0001-7289-4507
dc.authorwosidMurahari, Manikanta / AAF-6158-2019
dc.contributor.authorBursal, Ercan
dc.contributor.authorTurkan, Fikret
dc.contributor.authorBuldurun, Kenan
dc.contributor.authorTuran, Nevin
dc.contributor.authorAras, Abdulmelik
dc.contributor.authorcolak, Naki
dc.contributor.authorYergeri, Mayur C.
dc.date.accessioned2021-11-01T15:06:08Z
dc.date.available2021-11-01T15:06:08Z
dc.date.issued2021
dc.department[Belirlenecek]
dc.description.abstractA series of Fe(II), Ni(II), and Pd(II) complexes were prepared with a novel Schiff base ligand containing pyridine moiety. The prepared compounds were characterized using FT-IR, H-1 and (13) C NMR, UV-Vis, powder XRD, thermogravimetric analysis, mass spectra, magnetic susceptibility, and elemental analysis. The coordination geometry of Fe(II) and Ni(II) complexes were octahedral, where Fe(II) and Ni(II) metal ions were coordinated by an oxygen atom of the carbonyl group, a nitrogen atom of the azomethine moiety, and a phenolic oxygen atom. The Pd(II) complex had square planar geometry. All of the synthesized compounds were tested for their biochemical properties, including enzyme inhibition and antioxidant activities. According to the in vitro DPPH and FRAP antioxidant methods, the Schiff base ligand and its Fe(II)/Pd(II) complexes showed close antioxidant activities against the standards (BHA, BHT, ascorbic acid, and alpha-tocopherol). Enzyme inhibitions of the metal complexes were investigated against glutathione S-transferase (GST), acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) enzymes. The best inhibition value (K-i) was observed for the Ni(II) complex against GST (2.63 +/- 0.04 mu M). Also, the Pd(II) complex showed the best inhibition value (10.17 +/- 1.88 mu M) against AChE. Molecular docking specified significant interactions at the active pockets of respective target enzymes. The Ni(II) complex exhibited good binding affinity against both BChE (- 9.0 kcal/mol and 9.36 +/- 2.03 mu M) and GST (- 7.0 kcal/mol and 2.63 +/- 0.04 mu M) enzymes. [GRAPHICS] .
dc.identifier.doi10.1007/s10534-021-00287-z
dc.identifier.endpage406en_US
dc.identifier.issn0966-0844
dc.identifier.issn1572-8773
dc.identifier.issue2en_US
dc.identifier.pmid33528765
dc.identifier.scopus2-s2.0-85100341907
dc.identifier.scopusqualityQ1
dc.identifier.startpage393en_US
dc.identifier.urihttps://doi.org/10.1007/s10534-021-00287-z
dc.identifier.urihttps://hdl.handle.net/11491/7498
dc.identifier.volume34en_US
dc.identifier.wosWOS:000613962000001
dc.identifier.wosqualityQ3
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.institutionauthor[Belirlenecek]
dc.language.isoen
dc.publisherSpringer
dc.relation.ispartofBiometals
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectSchiff baseen_US
dc.subjectMetal complexesen_US
dc.subjectMolecular dockingen_US
dc.subjectPyridineen_US
dc.subjectAntioxidant activityen_US
dc.subjectEnzyme inhibitionen_US
dc.titleTransition metal complexes of a multidentate Schiff base ligand containing pyridine: synthesis, characterization, enzyme inhibitions, antioxidant properties, and molecular docking studies
dc.typeArticle

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