Heliyon · 2022 · 45 citations · 29 references
PharmacyMedicinal ChemistryPharmacologyDrug DesignDrug DiscoveryEnzymologyEnzyme DiscoveryEnzyme FunctionEnzyme InhibitionEnzyme StructureEnzyme-substrate RecognitionStructure-activity Relationship AnalysisActive SitesCarbohydrate-active EnzymesCarbohydrate-derived Enzyme InhibitorsEnzyme Inhibition ScreeningEnzyme Inhibitor SynthesisGlycosidase InhibitionMolecular Docking For EnzymesMolecular Docking Of Inhibitors
showed favorable higher α-glucosidase % inhibition of 67 ± 13 and lower α-amylase % inhibition of 51 ± 4 in comparison to acarbose with % inhibition activities of 19 ± 5 and 90 ± 2, respectively. Docking studies of selected 3,3-di(indolyl)indolin-2-ones revealed key interactions with the active sites of both α-glucosidase and α-amylase, further supporting the observed % inhibitory activities. Furthermore, the binding energies are consistent with the % inhibition values. The results suggest that 3,3-di(indolyl)indolin-2-ones may be developed as suitable Alpha Glucosidase Inhibitors (AGIs) and the lower α-amylase activities should be advantageous to reduce the side effects exhibited by commercial AGIs.
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