Yigitkan, SerkanErtas, AbdulselamSalmas, Ramin EkhteiariFirat, MehmetOrhan, Ilkay Erdogan2025-05-102025-05-1020221424-824710.3390/ph150201982-s2.0-85124225150https://doi.org/10.3390/ph15020198https://hdl.handle.net/20.500.14720/14392Firat, Mehmet/0000-0001-5814-614X; Ertas, Abdulselam/0000-0002-2193-8386; Erdogan Orhan, Ilkay/0000-0002-7379-5436; Ekhteiari Salmas, Ramin/0000-0003-3888-50703-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 mu g/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 mu g/mL). The molecular docking experiments on 7-acetoxyhorminone and horminone indicated that both compounds strongly bind to the active site of the enzyme.eninfo:eu-repo/semantics/openAccessHypercholesterolemiaHmg-Coa ReductaseEnzyme InhibitionSalviaTerpenoidsArticle152Q2Q235215310WOS:000826760300001