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Interactions between quercetin and Warfarin for albumin binding: A new eye on food/drug interference
Author(s) -
Di Bari Lorenzo,
Ripoli Silvia,
Pradhan Sanghamitra,
Salvadori Piero
Publication year - 2010
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.20794
Subject(s) - chemistry , quercetin , circular dichroism , coumarin , human serum albumin , warfarin , flavonoid , binding site , stereochemistry , antioxidant , biochemistry , organic chemistry , medicine , cardiology , atrial fibrillation
The interaction between quercetin, a popular antioxidant flavonoid, and human serum albumin (HSA) is investigated and characterized by means of induced circular dichroism and saturation transfer difference NMR. These techiques demonstrate the reversible binding of quercetin to the carrier protein, which is responsible for its dissolution in aqueous medium. Competition experiments with two classical probes for HSA binding sites, namely Ibuprofen and Warfarin (a common anticoagulant coumarin), demonstrate that quercetin has a primary binding site located in the subdomain IIA, where coumarins are hosted. The affinity for this site is large and we found that quercetin may effectively displace warfarin from HSA. This may have relevant consequences in rationalizing the interferences of common dietary compounds and food supplements to anticoagulant treatments. Chirality, 2010. © 2009 Wiley‐Liss, Inc.