α-Synuclein (α-syn) is a key protein in the etiology of Parkinson’s disease. In a disease state, α-syn accumulates as insoluble amyloid fibrils enriched in β-sheet structure. However, in its functional state, α-syn adopts an amphipathic helix upon membrane association and plays a role in synaptic vesicle docking, fusion, and clustering. In this Account, we describe our contributions made in the past decade toward developing a molecular understanding of α-syn membrane interactions, which are crucial for function and have pathological implications. Three topics are covered: α-syn membrane binding probed by neutron reflectometry (NR), the effects of membrane on α-syn amyloid formation, and interactions of α-syn with cellular membranes.

中文翻译：

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中子和光子探测的α-突触核蛋白的膜相互作用

α-突触核蛋白 (α-syn) 是帕金森病病因学中的关键蛋白。在疾病状态下，α-syn 积累为富含 β-折叠结构的不溶性淀粉样蛋白原纤维。然而，在其功能状态下，α-syn 在膜结合时采用两亲螺旋，并在突触小泡对接、融合和聚集中发挥作用。在这个帐户中，我们描述了我们在过去十年中为发展对 α-syn 膜相互作用的分子理解所做的贡献，这对功能至关重要并具有病理学意义。涵盖三个主题：通过中子反射法 (NR) 探测的 α-syn 膜结合、膜对 α-syn 淀粉样蛋白形成的影响以及 α-syn 与细胞膜的相互作用。