This study synthesized a series of novel coumarin-isatin derivatives and evaluated them for α-glucosidase inhibitory activity. The majority of the screened compounds exhibited excellent inhibition activities with IC50 values of 2.56 ± 0.08-268.79 ± 3.04 μm, when compared to acarbose. Among the newly derivatives, compound 5p was found to be the most active compound in the library of coumarin-isatin derivatives. Furthermore, enzyme kinetic studies showed that compound 5p is a non-competitive inhibitor with a Ki of 2.14 μm. Molecular docking analysis revealed the existence of hydrophobic and hydrogen interactions between compound 5p and the active site of α-glucosidase. Our results indicate that coumarin-isatin derivatives as a new class of α-glucosidase inhibitors.
Keywords: coumarin; enzyme kinetic study; isatin; molecular docking; α-glucosidase inhibitor.
© 2016 John Wiley & Sons A/S.