Lanthanide Salts of Heteropoly Molybdotungstosilicate LnHSiMo10W2O40·xH2O (Ln = Pr, Nd, Sm, Gd, Tb, Dy, Yb) Binding to Bovine Serum Albumin: A Fluorescence Quenching Study

Abstract

In the present work, the interaction between a series of novel lanthanide salts of heteropoly molybdotungstosilicate LnHSiMo(10)W(2)O(40)·xH(2)O (LnW(2); Ln = Pr (x = 23), Nd (x = 24), Sm (x = 26), Gd (x = 20), Tb (x = 23), Dy (x = 21), Yb (x = 25)), and bovine serum albumin (BSA) was investigated by spectroscopic approach at different temperatures under imitated physiological conditions. In the mechanism discussion, it was proved that the fluorescence quenching of BSA by LnW(2) is a result of the formation of LnW(2)-BSA complex. Binding affinity between LnW(2) and BSA was determined using Scatchard equation and the modified Stern-Volmer equation, and the corresponding electronic structure-affinity relationship were discussed. The results of thermodynamic parameters ∆G, ∆H, ∆S at different temperatures indicate that the electrostatic interactions play a major role in LnW(2)-BSA binding process. Moreover, the enthalpy change (∆H) and entropy change (∆S) were in accordance with the "enthalpy-entropy compensation" equation obtained from this and previous work. Furthermore, the distance r between donor (BSA) and acceptor (LnW(2)) was obtained according to fluorescence resonance energy transfer.