3-Hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase is a key enzyme involved
in cholesterol biosynthesis and one of the most important targets for the treatment of hypercholesterolemia.
A limited number of studies on the HMG-CoA reductase inhibitory potential
of natural products are available. Thus, in the current study, we aimed to test the HMG-CoA reductase
inhibitory capacity of extracts from the roots and aerial parts of Salvia multicaulis Vahl.,
through activity-guided isolation. Our findings revealed that the root extract prepared with dichloromethane–
acetone (1:1) showed the highest inhibition (71.97 ± 0.37%) at 100 μg/mL. The
extract was then initially fractionated by column chromatography and the obtained fractions were
monitored by thin layer chromatography. Fractions which were similar to each other were combined
and a total of 15 fractions were obtained. Further conventional chromatographic studies
were carried out on the active fractions. Based on these fractions, 10 known compounds, comprising
9 terpenes and 1 steroid derivative in total, were isolated and their structures were verified by a
combination of IT-TOF-MS, and 1D and 2D NMR techniques. According to the enzyme inhibition
data of the identified compounds, 7-acetoxyhorminone exerted the highest inhibition (84.15 ±
0.10%, IC50 = 63.6 ± 1.21 μg/mL). The molecular docking experiments on 7-acetoxyhorminone and
horminone indicated that both compounds strongly bind to the active site of the enzyme.