An alternate mode of binding of the polyphenol quercetin with serum albumins when complexed with Cu(II)

► Mode of binding of quercetin with SAs is altered after complexation with Cu(II). ► Hydrophobic forces play a key role in the binding of the copper complex with SAs. ► Negative ΔG° values indicate the spontaneity of the binding processes. ► Quercetin and its copper complex bind at the same site of the SAs.