A hallmark of Alzheimer’s, Parkinson’s, and other amyloid diseases is the assembly of amyloid proteins into amyloid aggregates or fibrils. In many cases, the formation and cytotoxicity of amyloid assemblies are associated with their interaction with cell membranes. Despite studied for many years, the characterization of the interaction is challenged for reasons on the multiple aggregation states of amyloid-forming proteins, transient and weak interactions in the complex system. Although several strategies such as computation biology, spectroscopy, and imaging methods have been performed, there is an urgent need to detail the molecular mechanism in different time scales and high resolutions. This review highlighted the recent applications of fluorescence, solution and solid-state NMR in exploring the interactions between amyloid protein and membranes attributing to their advantages of high sensitivity and atomic resolution.

阿尔茨海默氏症、帕金森氏症和其他淀粉样蛋白疾病的一个标志是淀粉样蛋白组装成淀粉样蛋白聚集体或原纤维。在许多情况下，淀粉样蛋白组装体的形成和细胞毒性与其与细胞膜的相互作用有关。尽管研究了多年，但由于形成淀粉样蛋白的多种聚集状态、复杂系统中的瞬时和弱相互作用，相互作用的表征受到挑战。尽管已经执行了几种策略，例如计算生物学、光谱学和成像方法，但迫切需要在不同时间尺度和高分辨率下详细说明分子机制。这篇综述强调了荧光的最新应用，