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

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dc.authoridSirinzade, Hanif/0000-0001-9663-9199
dc.authorwosidYilmaz Ozguven, Serap/G-1553-2014
dc.authorwosidSirinzade, Hanif/AAH-8850-2019
dc.contributor.authorAkman, Ebru
dc.contributor.authorSirinzade, Hanif
dc.contributor.authorOzguven, Serap Yilmaz
dc.contributor.authorDilek, Esra
dc.contributor.authorSuzen, Sibel
dc.date.accessioned2024-06-12T10:50:20Z
dc.date.available2024-06-12T10:50:20Z
dc.date.issued2023
dc.departmentTrakya Üniversitesien_US
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.{GRAPHIACAL ABSTRACT}en_US
dc.description.sponsorshipScientific Research Council of Erzincan Binali Yildirim University [TSA-2020-663]en_US
dc.description.sponsorshipThis work was supported by the Scientific Research Council of Erzincan Binali Yildirim University (Project No: TSA-2020-663).en_US
dc.identifier.doi10.1080/07391102.2023.2266500
dc.identifier.issn0739-1102
dc.identifier.issn1538-0254
dc.identifier.pmid37861657en_US
dc.identifier.scopus2-s2.0-85174424388en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.urihttps://doi.org/10.1080/07391102.2023.2266500
dc.identifier.urihttps://hdl.handle.net/20.500.14551/17971
dc.identifier.wosWOS:001090203900001en_US
dc.identifier.wosqualityN/Aen_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherTaylor & Francis Incen_US
dc.relation.ispartofJournal Of Biomolecular Structure & Dynamicsen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectAcetylcholinesteraseen_US
dc.subjectEnzyme Inhibitionen_US
dc.subjectHuman Carbonic Anhydrase Isoforms I And IIen_US
dc.subjectIndole Schiff Basesen_US
dc.subjectMolecular Dockingen_US
dc.subjectAntioxidant Activityen_US
dc.subjectAlzheimers-Diseaseen_US
dc.subjectMelatonin Analogsen_US
dc.subjectDerivativesen_US
dc.subjectButyrylcholinesteraseen_US
dc.subjectBindingen_US
dc.subjectIsozymesen_US
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 studyen_US
dc.typeArticleen_US

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