Effect of Zinc (II) on the interactions of bovine serum albumin with flavonols bearing different number of hydroxyl substituent on B-ring.

The impact of Zn(2+) ion on interactions of flavonols galangin (Gal), kaempferol (Kae), quercetin (Que) and myricetin (Myr) with bovine serum albumin (BSA) in aqueous solution were studied by fluorescence quenching technique. The results exhibited that Zn(2+) ion affected significantly the interactions and the effect was distinct for the flavonol bearing different number of B-ring hydroxyl. Each flavonol can quench the fluorescence of BSA, displaying a quenching extent of Myr>Que>Kae>Gal, which is in good agreement with the number variation of the B-ring hydroxyl. The presence of Zn(2+) ion promoted the quenching for the flavonols, exhibiting an extent of Que>Myr>Kae>Gal. The values of K(a) for Kae, Que and Myr decreased whereas K(SV) and k(q) for Gal, Kae and Que increased with the number of B-ring hydroxyl. The type of BSA fluorescence quenching for Gal, Kae and Que hardly changed but the preference of static quenching increased. The values of K(SV) and k(q) for Myr remarkably decreased and the fluorescence quenching of BSA alternatively occurred via both static and dynamic type instead of only one (static or dynamic). The results suggest the key role of the B-ring hydroxyl and the distinct effect of its number in the interactions. Each flavonol may capture the BSA-bound Zn(II) in the solution, forming Zn(II)-flavonol complex that is possibly responsible for BSA fluorescence quenching. The B-ring hydroxyl could establish hydrogen bonds with BSA in the absence of Zn(2+) and act as donors for chelating in the presence of Zn(2+). The formation of dinuclear Zn(II)-Myr complex together with the hydrogen bonds between the free B-ring hydroxyl and BSA may contribute to the exceptional behavior of Myr.