Amyloid Transition of Ubiquitin on Silver Nanoparticles Produced by Pulsed Laser Ablation in Liquid as a Function of Stabilizer and Single-Point Mutations
Amyloid Transition of Ubiquitin on Silver Nanoparticles Produced by Pulsed Laser Ablation in Liquid as a Function of Stabilizer and Single-Point Mutations
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DOI：
10.1002/chem.201402934
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发表时间：
2014-08-18
影响因子：
4.3
通讯作者：
Arnesano, Fabio
中科院分区：
文献类型：
--
作者：
Mangini, Vincenzo;Dell'Aglio, Marcella;Arnesano, Fabio
纳米颗粒与蛋白质的相互作用已经成为解决纳米毒性问题的关键问题。我们研究了银纳米颗粒（AgNPs），通过激光消融与人泛素（Ub），在细胞中的降解过程中必不可少的蛋白质的相互作用。银纳米颗粒的表面等离子体共振峰表明，Ub被迅速吸附在银纳米颗粒表面产生蛋白质冠; Ub包被的银纳米颗粒然后演变成由淀粉样蛋白形式的蛋白质保持在一起的簇，如通过硫磺素T荧光染料的结合所揭示的。甲状腺素运载蛋白，淀粉样蛋白型聚集的抑制剂，阻碍聚集体的形成和破坏预先形成的AgNP簇。在柠檬酸钠（一种赋予纳米颗粒整体负电荷的常见稳定剂）存在下，Ub仍然吸附在AgNP表面上，但没有观察到聚集。在β链的一个边缘（即Glu 16 Val）或环内（Glu 18 Val）携带单个突变的Ub突变体以完全不同的方式表现。
The interaction of nanoparticles with proteins has emerged as a key issue in addressing the problem of nanotoxicity. We investigated the interaction of silver nanoparticles (AgNPs), produced by laser ablation with human ubiquitin (Ub), a protein essential for degradative processes in cells. The surface plasmon resonance peak of AgNPs indicates that Ub is rapidly adsorbed on the AgNP surface yielding a protein corona; the Ub-coated AgNPs then evolve into clusters held together by an amyloid form of the protein, as revealed by binding of thioflavin T fluorescent dye. Transthyretin, an inhibitor of amyloid-type aggregation, impedes aggregate formation and disrupts preformed AgNP clusters. In the presence of sodium citrate, a common stabilizer that confers an overall negative charge to the NPs, Ub is still adsorbed on the AgNP surface, but no clustering is observed. Ub mutants bearing a single mutation at one edge beta strand (i.e. Glu16Val) or in loop (Glu18Val) behave in a radically different manner.