Abstract
Dipeptidyl peptidase 4 (DPP4) and α-glucosidase inhibitors have been developed as anti-diabetic agents for the treatment of diabetes mellitus. In the present study, the anti-diabetic effects of the lupinalbin A compound isolated from Apios americana was investigated by measuring its inhibitory activity against DPP4 and α-glucosidase. To detect the inhibitory effect of lupinalbin A, DPP4 and α-glucosidase assays were performed in vitro. Molecular docking analysis was performed using AutoDock 4.2. The IC(50) values of lupinalbin A against DPP4 and α-glucosidase were 45.2 and 53.4 µM, respectively. Analysis of the enzyme kinetics revealed that lupinalbin A interacted with the active site of DPP4 in a competitive manner, with an inhibition constant (Ki) value of 35.1±2.0 µM, whereas the lupinalbin A interaction with α-glucosidase was non-competitive, with a Ki value of 45.0 µM. Molecular docking analysis revealed a binding pose between the DPP4 enzyme and lupinalbin A. Taken together, these data suggest lupinalbin A is more effective against DPP4 than α-glucosidase, with regard to its anti-diabetic effects.