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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
    (Taylor & Francis Inc, 2023) Akman, Ebru; Sirinzade, Hanif; Ozguven, Serap Yilmaz; Dilek, Esra; Suzen, Sibel
    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.{GRAPHIACAL ABSTRACT}