title: Interactions between quercetin and warfarin for albumin binding: A new eye on food/drug interference.
abstract: 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.
authors.affiliation: Dipartimento di Chimica e Chimica Industriale, University of Pisa, Pisa, Italy.
authors.forename: Lorenzo
authors.initials: L
authors.lastname: Di Bari
authors.forename: Silvia
authors.initials: S
authors.lastname: Ripoli
authors.forename: Sanghamitra
authors.initials: S
authors.lastname: Pradhan
authors.forename: Piero
authors.initials: P
authors.lastname: Salvadori
mesh_terms: D000975:Antioxidants / Q000378:metabolism*; D002942:Circular Dichroism; D019587:Dietary Supplements; D018565:Food-Drug Interactions; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D011485:Protein Binding; D011794:Quercetin / Q000378:metabolism*; D012709:Serum Albumin / Q000378:metabolism*; D014859:Warfarin / Q000378:metabolism*
chemical_list: D000975:Antioxidants; D012709:Serum Albumin; D014859:Warfarin; D011794:Quercetin