Development of an Efficient Protocol for Cimifugin Isolation from Peucedanum schottii and Evaluation of Enzyme Inhibitory Activity

Creative Commons License

Koziol E., ERDOĞAN ORHAN İ., ŞENOL DENİZ F. S. , Alipieva K., Georgiev M., Skalicka-Wozniak K.

NATURAL PRODUCT COMMUNICATIONS, vol.11, no.8, pp.1107-1110, 2016 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 11 Issue: 8
  • Publication Date: 2016
  • Doi Number: 10.1177/1934578x1601100819
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.1107-1110
  • Gazi University Affiliated: Yes


The dichloromethane (DCM) extract of the fruits of Peucedanum schottii Besser ex DC. (Apiaceae) was subjected to high-performance counter-current chromatography (HPCCC) for the efficient and fast separation (30 min) and isolation of cimifugin using an ethyl acetate: water (1:1 v/v, K = 1.01) system. The analytical scale-optimized separation was easily scaled to semi-preparative conditions. Cimifugin (11.25% yield, 96.5% purity) was isolated for the first time from P. schottii and characterized by NMR spectroscopy. Cimifugin and the crude DCM extract were evaluated using ELISA microtiter assays for their inhibitory potential against the cholinesterases (acetylcholinesterase - AChE and butyrylcholinesterase - BChE), and tyrosinase (TYR), which are key enzymes for the treatment of some neurodegenerative diseases, i.e. Alzheimer's and Parkinson's. The crude extract exhibited a weak inhibitory activity against AChE, BChE, and TYR (4.2, 35.5, and 0% at 100 mu g mL(-1) and 10.3, 40.0, and 12.2% at 200 mu g mL(-1), respectively), while cimifugin displayed low to moderate inhibition towards AChE and BChE (3.1 and 21.6%, respectively) at 200 mu g mL(-1).