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Amyloid Beta Aggregation in the Presence of Temperature-Sensitive Polymers

机译：存在温度敏感性聚合物的淀粉样β聚集体

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The formation of amyloid fibrils is considered to be one of the main causes for many neurodegenerative diseases, such as Alzheimer’s, Parkinson’s or Huntington’s disease. Current knowledge suggests that amyloid-aggregation represents a nucleation-dependent aggregation process in vitro , where a sigmoidal growth phase follows an induction period. Here, we studied the fibrillation of amyloid β 1-40 (Aβ 40 ) in the presence of thermoresponsive polymers, expected to alter the Aβ 40 fibrillation kinetics due to their lower critical solution behavior. To probe the influence of molecular weight and the end groups of the polymer on its lower critical solution temperature (LCST), also considering its concentration dependence in the presence of buffer-salts needed for the aggregation studies of the amyloids, poly(oxazolines) (POx) with LCSTs ranging from 14.2–49.8 °C and poly(methoxy di(ethylene glycol)acrylates) with LCSTs ranging from 34.4–52.7 °C were synthesized. The two different polymers allowed the comparison of the influence of different molecular structures onto the fibrillation process. Mixtures of Aβ 40 with these polymers in varying concentrations were studied via time-dependent measurements of the thioflavin T (ThT) fluorescence. The studies revealed that amyloid fibrillation was accelerated in, accompanied by an extension of the lag phase of Aβ 40 fibrillation from 18.3 h in the absence to 19.3 h in the presence of the poly(methoxy di(ethylene glycol)acrylate) (3600 g/mol).
机译：淀粉样蛋白原纤维的形成被认为是许多神经退行性疾病的主要原因之一，例如阿尔茨海默氏症，帕金森氏症或亨廷顿氏病。目前的知识表明，淀粉样蛋白的聚集代表了体外成核依赖性的聚集过程，其中S形生长阶段在诱导期之后。在这里，我们研究了在热响应性聚合物存在下淀粉样蛋白β1-40（Aβ40）的原纤化，由于其较低的临界溶液行为，有望改变Aβ40的原纤化动力学。为了探讨聚合物的分子量和端基对其较低的临界溶液温度（LCST）的影响，还考虑了在淀粉样物质聚恶唑啉的聚集研究所需的缓冲盐存在下的浓度依赖性（合成了LCST范围为14.2–49.8°C的POx）和LCST范围为34.4–52.7°C的聚（甲氧基二（乙二醇）丙烯酸酯）。两种不同的聚合物可以比较不同分子结构对原纤化过程的影响。通过硫黄素T（ThT）荧光的时间依赖性测量研究了Aβ40与这些聚合物在不同浓度下的混合物。研究表明，在聚（甲氧基二（乙二醇）丙烯酸酯）（3600 g /摩尔）。

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