Dipartimento di Chimica e Chimica Industriale, University of Pisa, Pisa, Italy.
Chirality. 2010 Jun;22(6):593-6. doi: 10.1002/chir.20794.
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.
通过诱导圆二色性和饱和转移差 NMR 研究和表征了一种流行的抗氧化黄酮类化合物槲皮素与人体血清白蛋白（HSA）之间的相互作用。这些技术证明了槲皮素与载体蛋白的可逆结合，这是其在水介质中溶解的原因。与两种用于 HSA 结合位点的经典探针（布洛芬和华法林（一种常见的抗凝香豆素））的竞争实验表明，槲皮素具有位于亚域 IIA 中的主要结合位点，香豆素位于该亚域中。该位点的亲和力很大，我们发现槲皮素可以有效地将华法林从 HSA 中置换出来。这可能会对合理化常见饮食化合物和膳食补充剂对抗凝治疗的干扰产生相关影响。
