Mondal Prasenjit, Bose Adity
Department of Chemistry, Presidency University, 86/1 College Street, Kolkata 700073, India.
Bioimpacts. 2019;9(2):115-121. doi: 10.15171/bi.2019.15. Epub 2019 Mar 25.
Flavonoids are widely used as dietary supplements, and thus, play a significant role in the research field. In recent time, the interaction of flavonoid-metal complexes with serum albumin (SA) has widely been studied since the complexation poses a significant impact on biological activities. Additionally, the binding nature of flavonoids with SA gets modified in the presence of metal ions. In the present review, we studied the interaction of quercetin (Qu), a well-known flavonoid, and its Cu complexes with SA to provide sufficient information about the beneficial role of metal-flavonoid complexes over free flavonoids. Complexation with Cu(II) ion may alter the mode of binding of Qu with SAs. The strength of binding might be increased in the presence of Cu(II) as evidenced by the binding constant calculation. However, the drug binding site in bovine serum albumin (BSA) and human serum albumin (HSA) are not altered during the complexation process. To enhance the pharmaceutical outcomes of Qu molecules, one may use Qu-Cu(II) complex for the development and delivery of the small molecules.
黄酮类化合物作为膳食补充剂被广泛使用，因此在研究领域发挥着重要作用。近年来，由于黄酮类金属配合物的络合作用对生物活性有重大影响，其与血清白蛋白（SA）的相互作用得到了广泛研究。此外，在金属离子存在下，黄酮类化合物与SA的结合性质会发生改变。在本综述中，我们研究了著名的黄酮类化合物槲皮素（Qu）及其铜配合物与SA的相互作用，以提供有关金属 - 黄酮类配合物相对于游离黄酮类化合物有益作用的充分信息。与Cu（II）离子络合可能会改变Qu与SA的结合模式。结合常数计算表明，在Cu（II）存在下结合强度可能会增加。然而，在络合过程中牛血清白蛋白（BSA）和人血清白蛋白（HSA）中的药物结合位点并未改变。为了提高Qu分子的药物疗效，可以使用Qu - Cu（II）配合物来开发和递送小分子。
