Predicted affinity and kinetic analysis of myricetin, quercetin, kaempferol and acarbose binding to α-glucosidase.
| Inhibitors | Affinitya (kcal mol−1) | K i b (μmol L−1) | K is c (μmol L−1) | Inhibitory type |
|---|---|---|---|---|
| Myricetin | −9.2 | 15.56 | 31.64 | Mixed-type |
| Quercetin | −9.0 | 16.83 | 37.13 | Mixed-type |
| Kaempferol | −8.8 | 18.75 | 33.67 | Mixed-type |
| Acarbose | −8.7 | 109.95 | — | Competitive |
a
Affinity is predicted by molecular docking in silico.
b
K i represents the dissociation constant for inhibitors binding to free enzyme.
c
K is represents the dissociation constant for inhibitors binding to enzyme–substrate complex.