白金（Pt）（II）方平面配合物是已知的抗癌药物，其机制调节通过配体的极性、疏水性和芳香性特征精细调控。在试图将此可调节性转化为潜在的神经药物鉴定方面，本文探究了四个Pt（II）配合物对两种淀粉样蛋白原模型：Sup35p7-13和NPM1264-277肽的自聚集过程的调制能力。特别是苝金配合物在淀粉样蛋白聚集调节方面表现出最高效的药效：通过多种生物物理测定，如硫氟素T（ThT）、电喷雾质谱（ESI-MS）和紫外可见吸收光谱（UV-vis），该配合物表现出明显的聚集抑制作用并且可以解离小的可溶聚集体。这种效应是由苝金直接配位于淀粉样蛋白上引起的，损失了几个配体并形成π-π和π阳离子相互作用，这从分子动力学模拟结果得到证实。提供的数据支持一种不断增长的和最近的方法，也就是重复使用金属药物作为潜在的新型神经疗法药物。

Platinum (Pt)(II) square planar complexes are well-known anticancer drugs whose Mechanism of Action (MOA) are finely tuned by the polar, hydrophobic and aromatic features of the ligands. In the attempt to translate this tunability to the identification of potential neurodrugs, herein, four Pt(II) complexes were investigated in their ability to modulate the self-aggregation processes of two amyloidogenic models: Sup35p7-13 and NPM1264-277 peptides. In particular, phenanthriplatin revealed the most efficient agent in the modulation of amyloid aggregation: through several biophysical assays, as Thioflavin T (ThT), electrospray ionization mass spectrometry (ESI-MS) and ultraviolet-visible (UV-vis) absorption spectroscopy, this complex revealed able to markedly suppress aggregation and to disassemble small soluble aggregates. This effect was due to a direct coordination of phenanthriplatin to the amyloid, with the loss of several ligands and different stoichiometries, by the formation of π-π and π-cation interactions as indicated from molecular dynamic simulations. Presented data support a growing and recent approach concerning the repurposing of metallodrugs as potential novel neurotherapeutics.