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

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Yigitkan S., ERTAŞ A., Salmas R. E., Fırat M., ERDOĞAN ORHAN İ.

PHARMACEUTICALS, cilt.15, sa.2, 2022 (SCI-Expanded) identifier identifier identifier

  • 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
  • Anahtar Kelimeler: hypercholesterolemia, HMG-CoA reductase, enzyme inhibition, Salvia, terpenoids, ESSENTIAL OILS, STATINS, DITERPENOIDS, LONGIFOLIA, DISCOVERY, LAMIACEAE
  • Gazi 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 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.