My watch list  

Molecules, Vol. 22, Pages 1153: Warfarin and Flavonoids Do Not Share the Same Binding Region in Binding to the IIA Subdomain of Human Serum Albumin

Human serum albumin (HSA) binds a variety of xenobiotics, including flavonoids and warfarin. The binding of another ligand to the IIA binding site on HSA can cause warfarin displacement and potentially the elevation of its free concentration in blood. Studies dealing with flavonoid-induced warfarin displacement from HSA provided controversial results: estimated risk of displacement ranged from none to serious. To resolve these controversies, in vitro study of simultaneous binding of warfarin and eight different flavonoid aglycons and glycosides to HSA was carried out by fluorescence spectroscopy as well as molecular docking. Results show that warfarin and flavonoids do not share the same binding region in binding to HSA. Interactions were only observed at high warfarin concentrations not attainable under recommended dosing regimes. Docking experiments show that flavonoid aglycons and glycosides do not bind at warfarin high affinity sites, but rather to different regions within the IIA HSA subdomain. Thus, the risk of clinically significant warfarin–flavonoid interaction in binding to HSA should be regarded as negligible.

Authors:   Rimac, Hrvoje ; Dufour, Claire ; Debeljak, Željko ; Zorc, Branka ; Bojić, Mirza
Journal:   Molecules
Volume:   22
edition:   7
Year:   2017
Pages:   1153
DOI:   10.3390/molecules22071153
Publication date:   11-Jul-2017
Facts, background information, dossiers
  • serum albumin
  • molecules
  • interactions
  • blood
  • Binding Site
More about Molecular Diversity Preservation International
Your browser is not current. Microsoft Internet Explorer 6.0 does not support some functions on Chemie.DE