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Wiedendiol-A inhibits cholesteryl ester binding to its transfer protein.

   
@article{APS8944,
	author = {Suke Wang and Anthony Clemmons and Samuel Chacklamannil and Stephen J Coval and Edmund Sybertz and Robert Burrier},
	title = {Wiedendiol-A inhibits cholesteryl ester binding to its transfer protein.},
	journal = {Acta Pharmacologica Sinica},
	volume = {19},
	number = {5},
	year = {2016},
	keywords = {},
	abstract = {AIM: To study the wiedendiol-A (W-A) inhibition mechanism of plasma cholesteryl ester (CE) transfer protein (CETP) on the transfer of CE. METHODS: Using gel filtration method. RESULTS: W-A at 30 mumol.L-1 inhibited association of CE with CETP by 76% and CETP transfer activity by 81%. In addition, W-A enhanced binding of TP2, a monoclonal antibody with a CETP C-terminal epitope which is involved in CE binding, to CETP, suggesting a W-A-induced conformational change at the epitope for increased TP2 binding. When CETP activity was measured by varying high-density lipoproteins (HDL) concentration, the apparent Vmax of CE transfer was inhibited by 74% and 83% in the presence of W-A at 14 and 25 mumol.L-1, respectively, while the apparent K(m) of HDL for CETP did not change. CONCLUSION: W-A action is mediated through interaction between W-A and CETP, but not through those between W-A and lipoproteins.},
	issn = {1745-7254},	url = {http://www.chinaphar.com/article/view/8944}
}