Spectroscopic overview of Quercetin and its Cu(II) complex interaction with serum albumins

Flavonoids are widely used as a dietary supplement and thus occupy a significant role in the research field. In recent time interaction of flavonoid-metal complexes with serum, albumins (SAs) are widely studied among researchers since the complexation have a significant impact on the biological activities. Additionally, the binding nature of flavonoids with serum albumins gets modified in the presence of metal ions. In the present review we have studied every interaction of Quercetin (Qu), a well-known flavonoid, and its Cu2+ complexes with SA to provide sufficient information about the beneficial role of metal-flavonoid complexes over free flavonoids. Complexation with Cu(II) ion more or less altered the mode of binding of Qu with SAs. The strength of binding increased in the presence of Cu(II) as evident from the binding constant calculation. But 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 molecule one may use Qu-Cu(II) complex for development and delivery of the small molecule into the serum albumins.