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

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.