Bioactivity, crystal and molecular structure of vanadyl(III) complex with N-salicyloyl - N'(3,5-ditertbutyl-2-hydroxy)benzylidene hydrazine

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dc.authoridBAYRAMOV, MAHAMMAD/0000-0002-9396-8971
dc.authoridSadeghian, nastaran/0009-0004-2966-9231
dc.contributor.authorFatullayeva, Perizad Amrulla
dc.contributor.authorMedjidov, Ajdar Akper
dc.contributor.authorSafronenko, Marina Gennadievna
dc.contributor.authorKhrustalev, Victor Nikolaevic
dc.contributor.authorIsmayilov, Rayyat Huseyn
dc.contributor.authorBayramov, Mahammad Allahverdi
dc.contributor.authorYalcin, Bahattin
dc.date.accessioned2024-10-26T18:11:20Z
dc.date.available2024-10-26T18:11:20Z
dc.date.issued2024
dc.departmentSivas Cumhuriyet Üniversitesi
dc.description.abstractN-salicyloyl-N'-(3,5-ditertbutyl-2-hydroxy)benzylidene hydrazine (H3sahz) and its complex with VO(III) have been synthesized. The molecular and crystal structure of the [(VO)2(sahz)2(C2H5O)2(C2H5OH)] complex by X-ray diffraction, as well as IR and electronic spectra, EPR spectrum etc., have been studied. The structure of the investigated VO(III) complex consists of binuclear units in which the monomeric complex molecules are linked to each other through vanadyl oxygen atom. Monomeric complexes differ between themselves in the character of coordination. Both vanadium atoms have a distorted octahedral environment. The biological activity of this compound has been studied. Lastly, the activities of the studied ligand against various enzyme proteins including acetylcholinesterase (AChE), butrylcholinesterase (BChE) and alpha-glycosidase (alpha-Gly) enzyme were compared. ChE inhibitory activities of the new complex against alpha-Gly, AChE and BChE were determined by Tao and Ellman's methods. The new complex was shown to have IC50 values of 42.60 mu M for BChE, 91.43 mu M for AChE, and 196.49 mu M for alpha-glycosidase.
dc.description.sponsorshipMinistry of Science and Higher Education of the Russian Federation [075-03-2020-223 (FSSF- 2020-0017)]; RUDN University Strategic Academic Leadership Program
dc.description.sponsorshipThis work was funded by the Ministry of Science and Higher Education of the Russian Federation (award no. 075-03-2020-223 (FSSF- 2020-0017) ) . The publication has been prepared with support of the RUDN University Strategic Academic Leadership Program.
dc.identifier.doi10.1016/j.poly.2024.117024
dc.identifier.issn0277-5387
dc.identifier.issn1873-3719
dc.identifier.scopus2-s2.0-85192819142
dc.identifier.scopusqualityQ2
dc.identifier.urihttps://doi.org/10.1016/j.poly.2024.117024
dc.identifier.urihttps://hdl.handle.net/20.500.12418/30631
dc.identifier.volume257
dc.identifier.wosWOS:001242055400001
dc.identifier.wosqualityN/A
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.subjectHydrazones
dc.subjectSalicylic acid hydrazide
dc.subjectThermal analysis
dc.subjectComplexes VO(III)
dc.subjectX-ray diffraction
dc.subjectMolecular docking
dc.titleBioactivity, crystal and molecular structure of vanadyl(III) complex with N-salicyloyl - N'(3,5-ditertbutyl-2-hydroxy)benzylidene hydrazine
dc.typeArticle

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