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

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.     

“正常”膜蛋白取向的细菌视紫红质脂质体制备及其瞬态光学响应

细菌视紫红质 (bR)是嗜盐菌质膜上的一种跨膜蛋白质 ,有其独特的光驱质子泵功能 ,可以被定向组装到磷脂脂质体膜上 ,并且表现出和细胞膜上相反的取向。通过细菌培养和细胞膜分离 ,获得了含bR蛋白质的紫膜悬浮体系 ,在pH =2 .5时将bR悬浮液和两亲性的DPPC磷脂混合、通过自组装的方式形成了含bR膜蛋白的磷脂脂质体 ,并通过瞬态光学响应测量考察了bR的取向和质子泵生物活性。结果表明 ,bR膜蛋白可以被整合到DPPC的脂质体膜上 ;蛋白质的质子泵运行规律的测量进一步验证了在酸性条件下所制备的脂质体上bR保持了不寻常的择优取向 ,与细胞膜上的“正常”取向一致 ,而与绝大多数文献报道的中性条件下制备的脂质体质子泵取向相反。