A Series of Novel Rare Earth Molybdotungstosilicate Heteropolyoxometalates Binding to Bovine Serum Albumin: Spectroscopic Approach

Abstract

Heteropolyoxometalate complexes have been widely applied in many fields. In this paper, the interaction between a series of novel rare earth molybdotungstosilicate heteropolyoxometalates, K(10)H(3)[Ln(SiMo(6)W(5)O(39))(2)].xH(2)O (abbr. LnW(5), Ln = Pr (x = 30), Gd (x = 29), Dy (x = 28), and Yb (x = 31)), and bovine serum albumin (BSA) was investigated by spectroscopic approach under the physiological conditions. In the mechanism discussion, it was proved that the fluorescence quenching of BSA by LnW(5) is a result of the formation of LnW(5)-BSA complex. Fluorescence quenching constants were determined using the Stern-Volmer equation to provide a measure of the binding affinity between LnW(5) and BSA. The binding affinity ranked in the order GdW(5) > DyW(5) > PrW(5) > YbW(5). The results of thermodynamic parameters DeltaG, DeltaH, and DeltaS at different temperatures indicate that van der Waals interactions and hydrogen bonds play a major role for LnW(5)-BSA association. Furthermore, the distance r between donor (BSA) and acceptor (LnW(5)) was obtained according to fluorescence resonance energy transfer.