squalene and ellagitannin

squalene has been researched along with ellagitannin* in 1 studies

Other Studies

1 other study(ies) available for squalene and ellagitannin

Article	Year
Ellagitannins and hexahydroxydiphenoyl esters as inhibitors of vertebrate squalene epoxidase. Journal of natural products, 2001, Volume: 64, Issue:8 Ellagitannins isolated from various plant sources as well as newly synthesized n-alkyl (C(1)-C(18)) esters of hexahydroxydiphenyl (HHDP) dicarboxylic acid were evaluated as enzyme inhibitors of recombinant rat squalene epoxidase, a rate-limiting enzyme of cholesterol biosynthesis. Among the ellagitannins tested, pedunculagin (IC(50) = 2.0 microM) and eugeniin (IC(50) = 1.6 microM), both containing (S)-HHDP ester group(s), showed remarkable inhibition, which was more potent than those of previously reported substrate analogue inhibitors. Furthermore, ellagic acid (IC(50) = 2.0 microM), a bislactone formed by hydrolytic release of a HHDP group from ellagitannins, was also a good inhibitor of the enzyme. On the other hand, the synthetic HHDP esters with C(6) (IC(50) = 0.93 microM) and C(8) alkyl side chains (IC(50) = 0.83 microM) showed potent enzyme inhibition at the submicromolar concentration range, while esters with shorter chain lengths (C(1)-C(4)) and a C(18) ester exhibited moderate inhibition (IC(50) = 8-47 microM). Topics: Animals; Biphenyl Compounds; Chromatography, Thin Layer; Enzyme Inhibitors; Esters; Farnesyl-Diphosphate Farnesyltransferase; Hydrolyzable Tannins; Molecular Structure; Rats; Recombinant Proteins; Squalene; Structure-Activity Relationship; Substrate Specificity; Tannins	2001

Article

Year

Ellagitannins and hexahydroxydiphenoyl esters as inhibitors of vertebrate squalene epoxidase.

Journal of natural products, 2001, Volume: 64, Issue:8

Ellagitannins isolated from various plant sources as well as newly synthesized n-alkyl (C(1)-C(18)) esters of hexahydroxydiphenyl (HHDP) dicarboxylic acid were evaluated as enzyme inhibitors of recombinant rat squalene epoxidase, a rate-limiting enzyme of cholesterol biosynthesis. Among the ellagitannins tested, pedunculagin (IC(50) = 2.0 microM) and eugeniin (IC(50) = 1.6 microM), both containing (S)-HHDP ester group(s), showed remarkable inhibition, which was more potent than those of previously reported substrate analogue inhibitors. Furthermore, ellagic acid (IC(50) = 2.0 microM), a bislactone formed by hydrolytic release of a HHDP group from ellagitannins, was also a good inhibitor of the enzyme. On the other hand, the synthetic HHDP esters with C(6) (IC(50) = 0.93 microM) and C(8) alkyl side chains (IC(50) = 0.83 microM) showed potent enzyme inhibition at the submicromolar concentration range, while esters with shorter chain lengths (C(1)-C(4)) and a C(18) ester exhibited moderate inhibition (IC(50) = 8-47 microM).

Topics: Animals; Biphenyl Compounds; Chromatography, Thin Layer; Enzyme Inhibitors; Esters; Farnesyl-Diphosphate Farnesyltransferase; Hydrolyzable Tannins; Molecular Structure; Rats; Recombinant Proteins; Squalene; Structure-Activity Relationship; Substrate Specificity; Tannins

2001