Synthesis and characterization of novel bis(thiosemicarbazone) complexes and investigation of their acetylcholinesterase and glutathione S-transferase activities with in silico and in vitro studies
Özet
In this study, firstly, bis(thiosemicarbazone) ligand [L: 2,2′-(2-(2-(4-methoxyphenyl)hydrazineylidene)cyclohexane-1,3-diylidene)bis(hydrazine-1-carbothioamide)] was synthesized by the condensation reaction of thiosemicarbazide and ketone compound (2-(2-(4-methoxyphenyl)hydrazone)cyclohexane-1,3-dione). The metal complexes were synthesized by the reaction of obtained ligand (L) with CuCl2·2H2O, NiCl2·6H2O, CoCl2·6H2O, and MnCl2·4H2O salts. The structures of synthesized ligand and their complexes were characterized using elemental analysis, IR, UV–Vis, 1H-NMR spectra, 13C-NMR spectra, magnetic susceptibility, mass spectra (LC–MS), thermogravimetry analysis-differential thermal analysis (TGA-DTA), and differential scanning calorimetry techniques. According to the results of the analysis, square plane geometry was suggested for Cu and Co complexes. However, the structures of Ni and Mn complexes were in agreement with octahedral geometry. Molecular docking analysis and pharmacological potential of the compound were evaluated to determine the inhibitory potential against acetylcholinesterase (AChE) and Glutathione-S-transferases (GST) enzymes. The compound exhibited strong binding/docking indices of − 5.708 and − 5.928 kcal/mol for the respective receptors. In addition, L–Ni(II) complex was found to be the most effective inhibitor for AChE enzyme with a Ki value of 0.519. However, with a Ki value of 1.119, L–Cu(II) complex was also found to be an effective inhibitor for the GST enzyme.
Anahtar Kelimeler
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- OpenAlex
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Tam Kayıt
| Alan | Değer | Dil |
|---|---|---|
| dc.contributor.author | Donmez, Melike | |
| dc.contributor.author | Sekerci, Memet | |
| dc.contributor.author | Adiguzel, Ragip | |
| dc.contributor.author | Oğuz, Ercan | |
| dc.contributor.author | Türkan, Fikret | |
| dc.contributor.author | Yildiko, Umit | |
| dc.contributor.author | Colak, Naki | |
| dc.date.accessioned | 2026-10-28T14:53:46.642430924Z | |
| dc.date.available | 2026-10-28T14:53:46.642430924Z | |
| dc.date.issued | 2025 | |
| dc.description.abstract | In this study, firstly, bis(thiosemicarbazone) ligand [L: 2,2′-(2-(2-(4-methoxyphenyl)hydrazineylidene)cyclohexane-1,3-diylidene)bis(hydrazine-1-carbothioamide)] was synthesized by the condensation reaction of thiosemicarbazide and ketone compound (2-(2-(4-methoxyphenyl)hydrazone)cyclohexane-1,3-dione). The metal complexes were synthesized by the reaction of obtained ligand (L) with CuCl2·2H2O, NiCl2·6H2O, CoCl2·6H2O, and MnCl2·4H2O salts. The structures of synthesized ligand and their complexes were characterized using elemental analysis, IR, UV–Vis, 1H-NMR spectra, 13C-NMR spectra, magnetic susceptibility, mass spectra (LC–MS), thermogravimetry analysis-differential thermal analysis (TGA-DTA), and differential scanning calorimetry techniques. According to the results of the analysis, square plane geometry was suggested for Cu and Co complexes. However, the structures of Ni and Mn complexes were in agreement with octahedral geometry. Molecular docking analysis and pharmacological potential of the compound were evaluated to determine the inhibitory potential against acetylcholinesterase (AChE) and Glutathione-S-transferases (GST) enzymes. The compound exhibited strong binding/docking indices of − 5.708 and − 5.928 kcal/mol for the respective receptors. In addition, L–Ni(II) complex was found to be the most effective inhibitor for AChE enzyme with a Ki value of 0.519. However, with a Ki value of 1.119, L–Cu(II) complex was also found to be an effective inhibitor for the GST enzyme. | |
| dc.description.sponsorship | Türkiye Bilimsel ve Teknolojik Araştırma Kurumu, TÜBİTAK | |
| dc.description.sponsorship | Firat University Scientific Research Projects Management Unit, FÜBAP | |
| dc.description.sponsorship | FUBAP, (FF.1938) | |
| dc.identifier.articlenumber | 111134 | |
| dc.identifier.doi | 10.1007/s11030-024-10895-9 | |
| dc.identifier.eissn | 1573-501X | |
| dc.identifier.endpage | 1127 | |
| dc.identifier.issn | 1381-1991 | |
| dc.identifier.issue | 2 | |
| dc.identifier.pmcid | PMC11909086 | |
| dc.identifier.pmid | 38844741 | |
| dc.identifier.scopus | 2-s2.0-85195287597 | |
| dc.identifier.startpage | 1109 | |
| dc.identifier.uri | https://rdlopen.rawdatalibrary.net/r/munzur/952 | |
| dc.identifier.volume | 29 | |
| dc.identifier.wos | WOS:001243345600001 | |
| dc.language.iso | en | |
| dc.publisher | Springer Nature | |
| dc.relation.ispartof | Molecular Diversity | |
| dc.rights | info:eu-repo/semantics/openAccess | |
| dc.subject | Bis(thiosemicarbazone) ligands | |
| dc.subject | Enzyme inhibition | |
| dc.subject | Metal complexes | |
| dc.subject | Molecular docking | |
| dc.subject.other | Acetylcholinesterase | |
| dc.subject.other | Cholinesterase Inhibitors | |
| dc.subject.other | Computer Simulation | |
| dc.subject.other | Coordination Complexes | |
| dc.subject.other | Glutathione Transferase | |
| dc.subject.other | Ligands | |
| dc.subject.other | Molecular Docking Simulation | |
| dc.subject.other | Thiosemicarbazones | |
| dc.subject.other | metal complex | |
| dc.subject.other | thiosemicarbazone | |
| dc.subject.other | cholinesterase inhibitor | |
| dc.subject.other | coordination compound | |
| dc.subject.other | ligand | |
| dc.subject.other | thiosemicarbazone derivative | |
| dc.subject.other | Article | |
| dc.subject.other | carbon nuclear magnetic resonance | |
| dc.subject.other | chemical structure | |
| dc.subject.other | computer model | |
| dc.subject.other | crystal structure | |
| dc.subject.other | differential scanning calorimetry | |
| dc.subject.other | elemental analysis | |
| dc.subject.other | enzyme activity | |
| dc.subject.other | enzyme inhibition | |
| dc.subject.other | Fourier transform infrared spectroscopy | |
| dc.subject.other | geometry | |
| dc.subject.other | hydrogen bond | |
| dc.subject.other | IC50 | |
| dc.subject.other | in vitro study | |
| dc.subject.other | infrared spectroscopy | |
| dc.subject.other | liquid chromatography-mass spectrometry | |
| dc.subject.other | magnetism | |
| dc.subject.other | molecular docking | |
| dc.subject.other | nonhuman | |
| dc.subject.other | pharmacokinetics | |
| dc.subject.other | protein structure | |
| dc.subject.other | proton nuclear magnetic resonance | |
| dc.subject.other | synthesis | |
| dc.subject.other | thermal analysis | |
| dc.subject.other | thermogravimetry | |
| dc.subject.other | ultraviolet spectrophotometry | |
| dc.subject.other | chemistry | |
| dc.subject.other | metabolism | |
| dc.title | Synthesis and characterization of novel bis(thiosemicarbazone) complexes and investigation of their acetylcholinesterase and glutathione S-transferase activities with in silico and in vitro studies | |
| dc.type | Article | |
| rdl.citation.openalex | 19 | |
| rdl.citation.scopus | 21 | |
| rdl.department | Ankara Customs Accounting Directorate, 06590, Ankara, Turkey | |
| rdl.department | Department of Chemistry, Faculty of Science, Firat University, 23119, Elazıg, Turkey | |
| rdl.department | Department of Chemistry and Chemical Process Technologies, Vocational School of Tunceli, Munzur University, 62000, Tunceli, Turkey | |
| rdl.department | Department of Medical Services and Techniques, Health Services Vocational School, Igdır University, 76000, Igdır, Turkey | |
| rdl.department | Department of Basic Sciences, Faculty of Dentistry, Igdır University, 76000, Igdır, Turkey | |
| rdl.department | Department of Bioengineering, Architecture and Engineering Faculty, Kafkas University, 36100, Kars, Turkey | |
| rdl.department | Department of Chemistry, Faculty of Arts and Sciences, Hitit University, 19100, Corum, Turkey | |
| rdl.oa.status | hybrid | |
| rdl.oa.status | closed | |
| rdl.oa.status | green | |
| rdl.oa.url | https://doi.org/10.1007/s11030-024-10895-9 | |
| rdl.scopus.quartile | Q2 | |
| rdl.source.index | SCOPUS | |
| rdl.source.index | WOS | |
| rdl.source.index | PUBMED |
