Copper(II) monohelix complexes with pyrazine-modulated long-chain oligo-α-aminopyridine ligand: synthesis, crystal structures, and bioactivity studies

Basit Öğe Kaydı
dc.contributor.authorIsmayilova, Sabina Zahid
dc.contributor.authorIsmayilov, Rayyat Huseyn
dc.contributor.authorTagiyev, Dilgam Babir
dc.contributor.authorSenol, Halil
dc.contributor.authorMedjidov, Ajdar Akber
dc.contributor.authorHuseynova, Mansura Teyfur
dc.contributor.authorYalcin, Bahattin
dc.date.accessioned2026-04-25T14:19:58Z
dc.date.available2026-04-25T14:19:58Z
dc.date.issued2025
dc.departmentSinop Üniversitesi
dc.description.abstractUsing the pyrazine-modulated pentapyridyltetraamine ligand N-2,N-2 '-(pyridine-2,6-diyl)bis(N-6-(pyrazin-2-yl)pyridine-2,6-diamine) H4N9-2pz, three new mononuclear complexes [Cu(H4N9-2pz)](NO3)(2)center dot(CH3CN) 1, [Cu(H4N9-2pz)]Cl-2 center dot 2(H2O) 2 and [Cu(H3N9-2pz)] (CH3COO)center dot 2.5(H2O) 3 have been synthesized, structurally characterized, and their bioactivity properties studied. In vitro analysis of complexes 1-3 revealed that they inhibited AChE and BChE more effectively than the widely available inhibitor tacrine (IC50: 123.58 +/- 6.80 and 146.18 +/- 7.91 mu M). Additionally, their IC50 values for AChE and BChE ranged from 32.87 to 68.15 and 14.60 to 31.68 mu M, respectively. The g(
dc.description.abstract) and g(perpendicular to) components of the g factor have similar values in the EPR spectrum of complexes 1-3 (g(
dc.description.abstract) = 2.0179 and g(perpendicular to) = 2.1246 for 1; g(
dc.description.abstract) = 2.0044 and g(perpendicular to) = 2.1425 for 2; g(
dc.description.abstract) = 2.0118 and g(perpendicular to) = 2.1356 for 3). The single crystal X-ray approach revealed a distorted trigonal bipyramidal geometry of the complexes, which is consistent with the inverted type of EPR spectra (g(perpendicular to) > g(
dc.description.abstract)similar to ge), measured magnetic moment susceptibility, and electronic spectrum studies. The comparable structures of complexes 1-3 suggest that the H4N9-2pz ligand, rather than the nitrate, carboxylate, or chloride counterions, is critical for complex formation.
dc.identifier.doi10.1016/j.molstruc.2025.143295
dc.identifier.issn0022-2860
dc.identifier.issn1872-8014
dc.identifier.orcid0000-0002-8333-035X
dc.identifier.orcid0000-0002-3957-7996
dc.identifier.scopus2-s2.0-105010933277
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.1016/j.molstruc.2025.143295
dc.identifier.urihttps://hdl.handle.net/11486/8293
dc.identifier.volume1347
dc.identifier.wosWOS:001555985200003
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherElsevier
dc.relation.ispartofJournal of Molecular Structure
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzKA_WOS_20260420
dc.subjectModulated oligo-alpha-aminopyridine ligand
dc.subjectCopper complex
dc.subjectHydrogen bonds
dc.subjectSupramolecular networks
dc.subjectEnzyme inhibition
dc.titleCopper(II) monohelix complexes with pyrazine-modulated long-chain oligo-α-aminopyridine ligand: synthesis, crystal structures, and bioactivity studies
dc.typeArticle

Dosyalar

Koleksiyon

WoS İndeksli Yayınlar Koleksiyonu
Scopus İndeksli Yayınlar Koleksiyonu