Litcius/Paper detail

Synthesis, α-glucosidase inhibition, α-amylase inhibition, and molecular docking studies of 3,3-di(indolyl)indolin-2-ones

Mardi Santoso, Li Lin Ong, Nur Pasca Aijijiyah, First Ambar Wati, Azminah Azminah, Rose Malina Annuur, Arif Fadlan, Zaher M. A. Judeh

2022Heliyon45 citationsDOIOpen Access PDF

Abstract

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.

Topics & Concepts

AcarboseChemistryAmylaseDocking (animal)StereochemistryInhibitory postsynaptic potentialIC50Enzyme inhibitionEnzymeActive siteAlpha-amylaseBiochemistryIn vitroBiologyMedicineNursingNeuroscienceSynthesis of Indole DerivativesCarbohydrate Chemistry and SynthesisSynthesis and biological activity