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Enzyme inhibitory potential of some indole Schiff bases on acetylcholinesterase and human carbonic anhydrase isoforms I and II enzymes: an in vitro and molecular docking study

ArticleAçık Erişim

Özet

In this study, the in vitro effects of some indole Schiff bases on acetylcholinesterase and human carbonic anhydrase isoforms I and II were investigated. A series of N-methylindole hydrazide/hydrazone derivatives (1a-1t) were tested on these enzymes. The interactions of the synthesized indole derivatives with target enzymes were studied by molecular docking methodology. The results revealed that indole derivative Schiff base compounds inhibited the enzymes significantly. Ki values for hCAI isoenzyme were determined to be in the range of 36.18 ± 3.07–224.29 ± 5.78 nM; for the hCAII isoenzyme in the range of 31.30 ± 2.63–201.64 ± 7.25 nM; for acetylcholinesterase in the range of 6.82 ± 0.72–110.30 ± 9.26 nM. Compared to the control compound Acetazolamide (AZA), 1k and 1p were found to have the best inhibitory effect for hCAI; 1p was found to be the best inhibitory effect for hCAII. Compared to the control compound Tacrine (TAC), 1s showed the best inhibitory effect for AChE. In vitro results were verified with the results obtained by docking studies and interactions with enzymes were demonstrated. Communicated by Ramaswamy H. Sarma. © 2023 Informa UK Limited, trading as Taylor & Francis Group.

Anahtar Kelimeler

Acetylcholinesteraseenzyme inhibitionhuman carbonic anhydrase isoforms I and IIindole schiff basesmolecular dockingCarbonic Anhydrase ICarbonic Anhydrase IICarbonic Anhydrase InhibitorsCholinesterase InhibitorsHumansIndolesIsoenzymesKineticsMolecular Docking SimulationMolecular Dynamics SimulationProtein BindingSchiff BasesStructure-Activity Relationshipcarbonate dehydratase Icarbonate dehydratase IISchiff basecarbonate dehydratase inhibitorcholinesterase inhibitorindole derivativeisoenzymeAlzheimer diseaseArticlebinding affinitybinding sitecarbon nuclear magnetic resonance
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Tam Kayıt
AlanDeğerDil
dc.contributor.authorAkman, Ebru
dc.contributor.authorSirinzade, Hanif
dc.contributor.authorOzguven, Serap Yilmaz
dc.contributor.authorDilek, Esra
dc.contributor.authorSuzen, Sibel
dc.date.accessioned2026-10-18T20:26:45.750618865Z
dc.date.available2026-10-18T20:26:45.750618865Z
dc.date.issued2024
dc.description.abstractIn this study, the in vitro effects of some indole Schiff bases on acetylcholinesterase and human carbonic anhydrase isoforms I and II were investigated. A series of N-methylindole hydrazide/hydrazone derivatives (1a-1t) were tested on these enzymes. The interactions of the synthesized indole derivatives with target enzymes were studied by molecular docking methodology. The results revealed that indole derivative Schiff base compounds inhibited the enzymes significantly. Ki values for hCAI isoenzyme were determined to be in the range of 36.18 ± 3.07–224.29 ± 5.78 nM; for the hCAII isoenzyme in the range of 31.30 ± 2.63–201.64 ± 7.25 nM; for acetylcholinesterase in the range of 6.82 ± 0.72–110.30 ± 9.26 nM. Compared to the control compound Acetazolamide (AZA), 1k and 1p were found to have the best inhibitory effect for hCAI; 1p was found to be the best inhibitory effect for hCAII. Compared to the control compound Tacrine (TAC), 1s showed the best inhibitory effect for AChE. In vitro results were verified with the results obtained by docking studies and interactions with enzymes were demonstrated. Communicated by Ramaswamy H. Sarma. © 2023 Informa UK Limited, trading as Taylor & Francis Group.
dc.description.sponsorshipThis work was supported by the Scientific Research Council of Erzincan Binali Yildirim University (Project No: TSA-2020-663).
dc.identifier.doi10.1080/07391102.2023.2266500
dc.identifier.eissn1538-0254
dc.identifier.endpage12020
dc.identifier.issn0739-1102
dc.identifier.issue22
dc.identifier.pmid37861657
dc.identifier.scopus2-s2.0-85174424388
dc.identifier.startpage12011
dc.identifier.urihttps://rdlopen.rawdatalibrary.net/r/ebyu/11760
dc.identifier.volume42
dc.identifier.wosWOS:001090203900001
dc.language.isoen
dc.publisherTaylor and Francis Ltd.
dc.relation.ispartofJournal of Biomolecular Structure and Dynamics
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectAcetylcholinesterase
dc.subjectenzyme inhibition
dc.subjecthuman carbonic anhydrase isoforms I and II
dc.subjectindole schiff bases
dc.subjectmolecular docking
dc.subjectCarbonic Anhydrase I
dc.subjectCarbonic Anhydrase II
dc.subjectCarbonic Anhydrase Inhibitors
dc.subjectCholinesterase Inhibitors
dc.subjectHumans
dc.subjectIndoles
dc.subjectIsoenzymes
dc.subjectKinetics
dc.subjectMolecular Docking Simulation
dc.subjectMolecular Dynamics Simulation
dc.subjectProtein Binding
dc.subjectSchiff Bases
dc.subjectStructure-Activity Relationship
dc.subjectcarbonate dehydratase I
dc.subjectcarbonate dehydratase II
dc.subjectSchiff base
dc.subjectcarbonate dehydratase inhibitor
dc.subjectcholinesterase inhibitor
dc.subjectindole derivative
dc.subjectisoenzyme
dc.subjectAlzheimer disease
dc.subjectArticle
dc.subjectbinding affinity
dc.subjectbinding site
dc.subjectcarbon nuclear magnetic resonance
dc.titleEnzyme inhibitory potential of some indole Schiff bases on acetylcholinesterase and human carbonic anhydrase isoforms I and II enzymes: an in vitro and molecular docking study
dc.typeArticle
dspace.entity.typePublication
rdl.citation.scopus10
rdl.citation.wos9
rdl.departmentDepartment of Pharmaceutical Sciences, Institute of Health Sciences, Erzincan Binali Yıldırım University, Erzincan, Turkey. | Department of Biochemistry, Faculty of Pharmacy, Erzincan Binali Yıldırım University, Erzincan, Turkey.
rdl.oa.statusgreen
rdl.source.indexSCOPUS
rdl.source.indexWOS
rdl.source.indexPUBMED
rdl.wos.indexScience Citation Index Expanded (SCI-EXPANDED)