To visualize amyloid β (Aβ) aggregates requires an uncontaminated and artifact-free interface. This paper demonstrates the interface between graphene and pure water (verified to be atomically clean using tunneling microscopy) as an ideal platform for resolving size, shape, and morphology (measured by atomic force microscopy) of Aβ-40 and Aβ-42 peptide assemblies from 0.5 to 150 hours at a 5-hour time interval with single-particle resolution. After confirming faster aggregation of Aβ-42 in comparison to Aβ-40, a stable set of oligomers with a diameter distribution of ~7 to 9 nm was prevalently observed uniquely for Aβ-42 even after fibril appearance. The interaction energies between a distinct class of amyloid aggregates (dodecamers) and graphene was then quantified using molecular dynamics simulations. Last, differences in Aβ-40 and Aβ-42 networks were resolved, wherein only Aβ-42 fibrils were aligned through lateral interactions over micrometer-scale lengths, a property that could be exploited in the design of biofunctional materials.

中文翻译：

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淀粉样蛋白β（1-40）和（1-42）的完整聚集途径在原子清洁界面上得到解析。

要显示淀粉样蛋白β（Aβ）聚集体，需要无污染且无伪影的界面。本文展示了石墨烯与纯水之间的界面（已通过隧道显微镜检查证实是原子清洁的），是解决Aβ-40和Aβ-42肽装配体的大小，形状和形态（通过原子力显微镜测量）的理想平台每5小时间隔0.5到150小时，单粒子分辨率。在确认Aβ-42比Aβ-40更快聚集之后，即使在原纤维出现后，也普遍观察到稳定的一组直径约7至9 nm的低聚物。然后使用分子动力学模拟对不同种类的淀粉样聚集体（十二聚体）和石墨烯之间的相互作用能进行定量。持续，