7-Acetoxyhorminone from Salvia multicaulis Vahl. as Promising Inhibitor of 3-Hydroxy-3-methylglutaryl Coenzyme A (HMG-CoA) Reductase

Yiğitkan S., Ertaş A., Ekhteiari Salmas R., Fırat M., Erdoğan Orhan İ.

PHARMACEUTICALS, cilt.15, sa.2, ss.1-14, 2022 (SCI-Expanded)

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 15 Sayı: 2
  • Basım Tarihi: 2022
  • Doi Numarası: 10.3390/ph15020198
  • Dergi Adı: PHARMACEUTICALS
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, CAB Abstracts, EMBASE, Veterinary Science Database, Directory of Open Access Journals
  • Sayfa Sayıları: ss.1-14
  • Van Yüzüncü Yıl Üniversitesi Adresli: Evet

Özet

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.