ACAT Inhibition of Polyactylenes from Gymnaster koraiensis

  • Jung, Hyun-Ju (Department of Oriental Pharmacy, Wonkwang University) ;
  • Hung, Tran-Manh (College of Pharmacy, Catholic University of Daegu) ;
  • Na, Min-Kyun (College of Pharmacy, Yeungnam University) ;
  • Min, Byung-Sun (College of Pharmacy, Catholic University of Daegu) ;
  • Kwon, Byoung-Mog (Laboratory of Chemical Biology and Chemical Genomics, Korea Research Institute of Bioscience and Biotechnology) ;
  • Bae, Ki-Hwan (College of Pharmacy, Chungnam National University)
  • Published : 2009.06.30

Abstract

Acyl-coenzyme A: cholesterol acyltransferase (ACAT) catalyzes cholesterol esterification and plays important roles in intestinal absorption of cholesterol, hepatic production of lipoproteins and accumulation of cholesteryl ester within macrophages and smooth muscle cells. In our study, eight polyacetylenes (1 - 8), were isolated from the roots of Gymnaster koraiensis, and their chemical structures were identified on the basis of spectroscopic analysis and mass. Compound 2 with the (10S)-15,16-epoxy group in skeleton strongly inhibited ACAT enzyme with $IC_{50}$ value of 35.8 ${\mu}g$/mL, meanwhile the other compounds displayed significant inhibition of ACAT enzyme with the $IC_{50}$ values from 45.5 to 55.1 ${\mu}g$/mL.

Keywords

References

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