Molecular Interactions between Wells−Dawson Type Polyoxometalates and Human Serum Albumin

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• 作者：Guangjin Zhang ; Bineta Keita ; Constantin T. Craescu ; Simona Miron ; Pedro de Oliveira ; Louis Nadjo
• 刊名：Biomacromolecules
• 出版年：2008
• 出版时间：March 2008
• 年：2008
• 卷：9
• 期：3
• 页码：812 - 817
• 全文大小：1698K
• 年卷期：v.9,no.3(March 2008)
• ISSN：1526-4602

文摘

Binding human serum albumin (HSA) of three polyoxometalates (POMs) with the Wells−Dawson structure, α₂-[P₂W₁₇O₆₁]¹⁰⁻ (abbreviated as α₂-P₂W₁₇) and two of its metal-substituted derivatives, α₂-[NiP₂W₁₇O₆₁]⁸⁻ and α₂-[CuP₂W₁₇O₆₁]⁸⁻ (α₂-P₂W₁₇Ni and α₂-P₂W₁₇Cu, respectively) was studied in an aqueous medium at pH 7.5. Fluorescence quenching, circular dichroism (CD), thermal denaturation, and isothermal titration calorimetry (ITC) were used for this purpose. The results were compared with those obtained previously with the Keggin structure POM, [H₂W₁₂O₄₀]⁶⁻ (H2W12), and the wheel-shaped structure, [NaP₅W₃₀O110]¹⁴⁻ (P5W30). All these POMs bind HSA mainly by electrostatic interactions. Comparison of the physical characteristics and HSA interaction parameters for the POMs of the present work and those studied previously showed that the overall charge of the clusters is not the single parameter governing the binding process and its consequences. In contrast, besides the influences of the structure, the dimension and/or weight of the POMs, the results have permitted highlighting of the importance of each POM atomic composition for its binding behavior.