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

Article Details

Citation

Medina-Franco JL, Lopez-Vallejo F, Rodriguez-Morales S, Castillo R, Chamorro G, Tamariz J

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

Bioorg Med Chem Lett. 2005 Feb 15;15(4):989-94.

PubMed ID
15686898 [ View in PubMed
]
Abstract

Docking experiments using a number of published crystal structures of HMG-CoA reductase with the potent hypocholesterolemic agent alpha-asarone are described. The results indicate that alpha-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 alpha-asarone. The docking results will be valuable for the structure-based design of novel hypolipidemic agents.

DrugBank Data that Cites this Article

Binding Properties
DrugTargetPropertyMeasurementpHTemperature (°C)
Meglutol3-hydroxy-3-methylglutaryl-coenzyme A reductaseIC 50 (nM)4000N/AN/ADetails
Meglutol3-hydroxy-3-methylglutaryl-coenzyme A reductaseKi (nM)23.5N/AN/ADetails
Rosuvastatin3-hydroxy-3-methylglutaryl-coenzyme A reductaseIC 50 (nM)5.4N/AN/ADetails
Rosuvastatin3-hydroxy-3-methylglutaryl-coenzyme A reductaseKi (nM)0.9N/AN/ADetails
Rosuvastatin3-hydroxy-3-methylglutaryl-coenzyme A reductaseKi (nM)71000N/AN/ADetails
Simvastatin3-hydroxy-3-methylglutaryl-coenzyme A reductaseKi (nM)68000N/AN/ADetails
Simvastatin3-hydroxy-3-methylglutaryl-coenzyme A reductaseKi (nM)2.6N/AN/ADetails
Simvastatin3-hydroxy-3-methylglutaryl-coenzyme A reductaseIC 50 (nM)11.2N/AN/ADetails