2026-10-19T01:04:45Zhttps://ebyu-rdlopen.rawdatalibrary.net/oai/requestoai:ebyu-rdlopen.rawdatalibrary.net:ebyu/117602026-10-18T21:13:18Zopenairedrivercom_ebyu_10000col_ebyu_10001Enzyme inhibitory potential of some indole Schiff bases on acetylcholinesterase and human carbonic anhydrase isoforms I and II enzymes: an in vitro and molecular docking studyAkman, EbruSirinzade, HanifOzguven, Serap YilmazDilek, EsraSuzen, SibelAcetylcholinesteraseenzyme 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 resonanceIn 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.Taylor and Francis Ltd.2024Articlehttps://rdlopen.rawdatalibrary.net/r/ebyu/11760https://doi.org/10.1080/07391102.2023.22665000739-1102enJournal of Biomolecular Structure and Dynamicsinfo:eu-repo/semantics/openAccessinfo:eu-repo/semantics/articlehttps://ebyu-rdlopen.rawdatalibrary.net/tr/items/ebyu/11760