Vanadyl (III)-(E)-N′-(3,5-di-tert-butyl-2-hydroxybenzylidene)-nicotinohydrazide complex: Synthesis, characterization and in vitro and in silico cholinesterase and α-glucosidase inhibition studies

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dc.contributor.authorFatullayeva, Perizad Amrulla
dc.contributor.authorMedjidov, Ajdar Akper
dc.contributor.authorSenol, Halil
dc.contributor.authorTagiyev, Dilgam Babir
dc.contributor.authorIsmayilov, Rayyat Huseyn
dc.contributor.authorSahin, Onur
dc.contributor.authorKhrustalev, Victor Nikolaevic
dc.date.accessioned2026-04-25T14:20:01Z
dc.date.available2026-04-25T14:20:01Z
dc.date.issued2025
dc.departmentSinop Üniversitesi
dc.description.abstractA new ligand N-nicotinoyl-N '-(3,5-ditertbuthyl-2-hydroxy)benzylidene hidrazine (H2L) was synthesized and a complex [VO(L)CH3O & sdot;CH3OH] with this ligand was obtained and their structures investigated by X-ray crystallography. It was found that the methanol molecule in the complex is easily exchanged for a pyridine molecule. The effects of H2L and [VO(L)CH3O CH3OH] complexes against AChE, BChE and alpha-glucosidase enzymes were investigated using Ellman and Tao methods and the results were calculated as IC50 and Ki. Both compounds demonstrated effective inhibition of all three enzymes, with varying degrees of potency. For AChE, H2L exhibited the lowest IC50 value (8.45 mu M, r2 = 0.993) and a Ki of 5.53 +/- 0.73 mu M, outperforming both its vanadium complex (IC50 = 10.61 mu M, Ki = 7.38 +/- 1.14 mu M) and the reference drug tacrine (IC50 = 13.75 mu M, Ki = 11.90 +/- 1.01 mu M). Additionally, Molecular docking studies were performed to elucidate the possible inhibition mechanisms and binding modes of the ligand (H2L) and its vanadium complex [VO(L)(CH3O)& sdot;CH3OH] against three target enzymes: acetylcholinesterase (AChE, PDB ID: 4EY7), butyrylcholinesterase (BChE, PDB ID: 6EQP), and alpha-glucosidase (alpha-Glu, PDB ID: 3WY1). To achieve a more accurate prediction of ligand-protein interactions and account for conformational flexibility, Induced Fit Docking (IFD) protocols were employed. These two complexes were studied in vitro and in silico and it was determined that they may be used for drug design.
dc.identifier.doi10.1016/j.poly.2025.117783
dc.identifier.issn0277-5387
dc.identifier.issn1873-3719
dc.identifier.orcid0000-0003-0553-8873
dc.identifier.orcid0000-0002-8333-035X
dc.identifier.scopus2-s2.0-105015596471
dc.identifier.scopusqualityQ2
dc.identifier.urihttps://doi.org/10.1016/j.poly.2025.117783
dc.identifier.urihttps://hdl.handle.net/11486/8323
dc.identifier.volume282
dc.identifier.wosWOS:001573365200001
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherPergamon-Elsevier Science Ltd
dc.relation.ispartofPolyhedron
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzKA_WOS_20260420
dc.subjectMetal complexes
dc.subjectSchiff base
dc.subjectSpectroscopic
dc.subjectNicotinic acid hydrazide
dc.subjectVO-complexes
dc.titleVanadyl (III)-(E)-N′-(3,5-di-tert-butyl-2-hydroxybenzylidene)-nicotinohydrazide complex: Synthesis, characterization and in vitro and in silico cholinesterase and α-glucosidase inhibition studies
dc.typeArticle

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