Molecular docking of the highly hypolipidemic agent α-asarone with the catalytic portion of HMG-CoA reductase

Docking experiments using a number of published crystal structures of HMG-CoA reductase with the potent hypocholesterolemic agent α-asarone are described. The results indicate that α-asarone binds in the enzyme’s active site. The methoxy groups play a key role in the binding and probably also in its biological activity, as shown by extensive SAR studies reported for analogues of α-asarone. The docking results will be valuable for the structure-based design of novel hypolipidemic agents.