Thermophoretic trap for single amyloid fibril and protein aggregation studies
Thermophoretic trap for single amyloid fibril and protein aggregation studies
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DOI：
10.1038/s41592-019-0451-6
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发表时间：
2019-07-01
期刊：
影响因子：
48
通讯作者：
Cichos, Frank
中科院分区：
文献类型：
--
作者：
Fraenzl, Martin;Thalheim, Tobias;Cichos, Frank
可溶性蛋白质聚集成高度有序的不溶性淀粉样纤维的研究是理解神经退行性疾病的基础。在这里，我们提出了一种方法，用于观察单个淀粉样纤维，允许调查纤维生长，二次成核或纤维破裂，通常隐藏在平均合奏。我们的热泳捕获和旋转扩散测量方法被证明是针对单个A β（40）、A β（42）和焦谷氨酰修饰的淀粉样蛋白-β变体（pGlu（3）-A β（3-40））淀粉样蛋白原纤维。
The study of the aggregation of soluble proteins into highly ordered, insoluble amyloid fibrils is fundamental for the understanding of neurodegenerative disorders. Here, we present a method for the observation of single amyloid fibrils that allows the investigation of fibril growth, secondary nucleation or fibril breakup that is typically hidden in the average ensemble. Our approach of thermophoretic trapping and rotational diffusion measurements is demonstrated for single A beta(40), A beta(42) and pyroglutamyl- modified amyloid-beta variant (pGlu(3)-A beta(3-40)) amyloid fibrils.