Several diseases share misfolding of different peptides and proteins as a key feature for their development. This is the case of important neurodegenerative diseases such as Alzheimer's and Parkinson's diseases and type II diabetes mellitus. Even more, metal ions such as copper and zinc might play an important role upon interaction with amyloidogenic peptides and proteins, which could impact their aggregation and toxicity abilities. In this review, the different coordination modes proposed for copper and zinc with amyloid-β, α-synuclein and IAPP will be reviewed as well as their impact on the aggregation, and ROS production in the case of copper. In addition, a special focus will be given to the mutations that affect metal binding and lead to familial cases of the diseases. Different modifications of the peptides that have been observed in vivo and could be relevant for the coordination of metal ions are also described.

中文翻译：

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铜和锌与淀粉样肽的配位：从迷人的化学到有争议的病理学相关性。

几种疾病共享不同肽和蛋白质的错误折叠，这是它们发展的关键特征。重要的神经退行性疾病如阿尔茨海默病和帕金森病以及 II 型糖尿病就是这种情况。更重要的是，铜和锌等金属离子可能在与淀粉样肽和蛋白质相互作用时发挥重要作用，这可能会影响它们的聚集和毒性能力。在这篇综述中，将回顾铜和锌与淀粉样蛋白-β、α-突触核蛋白和 IAPP 的不同配位模式，以及它们对铜的聚集和 ROS 产生的影响。此外，将特别关注影响金属结合并导致疾病家族性病例的突变。