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镧系铕十钨酸盐与人血清白蛋白分子相互作用的多种技术研究。

A multitechnique study of europium decatungstate and human serum albumin molecular interaction.

机构信息

Beijing National Laboratory for Molecular Science, Institute of Chemistry, Chinese Academy of Science, 100190, Beijing, China.

出版信息

Phys Chem Chem Phys. 2010 Feb 14;12(6):1299-304. doi: 10.1039/b919952g. Epub 2009 Dec 10.

Abstract

Polyoxometalates (POMs) show promising biological activities, but the mechanism of these potential therapeutic effects remains to be elucidated at a molecular level. As a step in this direction, the interaction between the Eu-containing decatungstate EuW(10)O(36) and human serum albumin (HSA) has been studied by several techniques. Fluorescence/luminescence analysis showed the existence of a strong interaction between the POM and HSA. This interaction has key effects both on luminescence of the POM and on the behaviours of HSA. An enhancement of the POM luminescence is observed upon interaction. The presence of increasing concentrations of the POM results in the progressive quenching of the fluorescence of the single tryptophan of HSA. Circular dichroism led to the conclusion that the binding of the POM did not alter the secondary structure of HSA. Isothermal titration calorimetry revealed an enthalpy-driven binding reaction between HSA and the POM, resulting in the formation of a 1:1 complex. The present work is meaningful in finding novel solid state bio-image or fluorescence/luminescence labelling agents.

摘要

多金属氧酸盐(POMs)表现出有前景的生物活性,但这些潜在治疗效果的机制仍需在分子水平上阐明。作为朝这个方向迈出的一步,已经通过多种技术研究了含铕的十钨酸盐[EuW(10)O(36)](9-)与人血清白蛋白(HSA)之间的相互作用。荧光/发光分析表明 POM 与 HSA 之间存在强相互作用。这种相互作用对 POM 的发光以及 HSA 的行为都有重要影响。相互作用会观察到 POM 发光增强。随着 POM 浓度的增加,HSA 中单个色氨酸的荧光逐渐猝灭。圆二色性得出结论,POM 的结合并未改变 HSA 的二级结构。等温热滴定法表明 HSA 与 POM 之间存在焓驱动的结合反应,形成 1:1 复合物。这项工作对于寻找新型固态生物成像或荧光/发光标记剂具有重要意义。

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