CNR-NANO Research Center, Via Campi 213/a, 41125 Modena, Italy.
Department of Chemical and Geological Sciences, University of Modena and Reggio Emilia, Via Campi 103, 41125 Modena, Italy.
Int J Mol Sci. 2020 Dec 22;22(1):26. doi: 10.3390/ijms22010026.
Amyloid-β aggregation is one of the principal causes of amyloidogenic diseases that lead to the loss of neuronal cells and to cognitive impairments. The use of gold nanoparticles treating amyloidogenic diseases is a promising approach, because the chemistry of the gold surface can be tuned in order to have a specific binding, obtaining effective tools to control the aggregation. In this paper, we show, by means of Replica Exchange Solute Tempering Molecular Simulations, how electrostatic interactions drive the absorption of Amyloid-β monomers onto citrates-capped gold nanoparticles. Importantly, upon binding, amyloid monomers show a reduced propensity in forming β-sheets secondary structures that are characteristics of mature amyloid fibrils.
淀粉样蛋白-β聚集是导致神经元细胞丧失和认知障碍的淀粉样变性疾病的主要原因之一。使用金纳米粒子治疗淀粉样变性疾病是一种很有前途的方法，因为可以调整金表面的化学性质以实现特定的结合，从而获得控制聚集的有效工具。在本文中，我们通过复制交换溶剂化温度分子模拟表明静电相互作用如何驱动淀粉样蛋白-β单体吸收到柠檬酸根封端的金纳米粒子上。重要的是，在结合后，淀粉样蛋白单体形成成熟淀粉样原纤维特征的β-折叠二级结构的倾向降低。
