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Aggregate Size Dependence of Amyloid Adsorption onto Charged Interfaces.
Langmuir ( IF 3.9 ) Pub Date : 2018-01-17 , DOI: 10.1021/acs.langmuir.7b03155
Giulio Tesei 1, 2 , Erik Hellstrand 1, 2 , Kalyani Sanagavarapu 1, 2 , Sara Linse 1, 2 , Emma Sparr 1, 2 , Robert Vácha 1, 2 , Mikael Lund 1, 2
Affiliation  

Amyloid aggregates are associated with a range of human neurodegenerative disorders, and it has been shown that neurotoxicity is dependent on aggregate size. Combining molecular simulation with analytical theory, a predictive model is proposed for the adsorption of amyloid aggregates onto oppositely charged surfaces, where the interaction is governed by an interplay between electrostatic attraction and entropic repulsion. Predictions are experimentally validated against quartz crystal microbalance-dissipation experiments of amyloid beta peptides and fragmented fibrils in the presence of a supported lipid bilayer. Assuming amyloids as rigid, elongated particles, we observe nonmonotonic trends for the extent of adsorption with respect to aggregate size and preferential adsorption of smaller aggregates over larger ones. Our findings describe a general phenomenon with implications for stiff polyions and rodlike particles that are electrostatically attracted to a surface.

中文翻译:

淀粉样蛋白吸附到带电界面上的聚集体尺寸依赖性。

淀粉样蛋白聚集体与一​​系列人类神经退行性疾病有关,并且已经表明神经毒性取决于聚集体的大小。将分子模拟与分析理论相结合,提出了一种预测模型,用于淀粉样蛋白聚集体吸附到带相反电荷的表面上,其中相互作用由静电引力和熵斥力之间的相互作用控制。在存在支持的脂质双层的情况下,通过对淀粉样蛋白 β 肽和碎片原纤维的石英晶体微量平衡耗散实验进行了实验验证。假设淀粉样蛋白是刚性的、细长的颗粒,我们观察到相对于聚集体大小的吸附程度的非单调趋势,以及较小聚集体对较大聚集体的优先吸附。
更新日期:2018-01-17
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