| Literature DB >> 19902529 |
Lorenzo Di Bari1, Silvia Ripoli, Sanghamitra Pradhan, Piero Salvadori.
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. (c) 2009 Wiley-Liss, Inc.Entities:
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Year: 2010 PMID: 19902529 DOI: 10.1002/chir.20794
Source DB: PubMed Journal: Chirality ISSN: 0899-0042 Impact factor: 2.437