Cyclometallated Pt(II) complexes possessing hydrophobic 2-phenylpyridine (ppy) ligands and hydrophilic acetonylacetone (acac) ligands have been investigated for their ability to detect amyloid fibrils via luminescence response. Using hen egg-white lysozyme (HEWL) as a model amyloid protein, Pt(II) complexes featuring benzanilide-substituted ppy ligands and ethylene glycol-functionalized acac ligands demonstrated enhanced luminescence in the presence of HEWL fibrils, whereas Pt(II) complexes lacking complementary hydrophobic/hydrophilic ligand sets displayed little to no emission enhancement. An amphiphilic Pt(II) complex incorporating a bis(ethylene glycol)-derivatized acac ligand was additionally found to trigger restructuring of HEWL fibrils into smaller spherical aggregates. Amphiphilic Pt(II) complexes were generally non-toxic to SH-SY5Y neuroblastoma cells, and several complexes also exhibited enhanced luminescence in the presence of Aβ₄₂ fibrils associated with Alzheimer's disease. This study demonstrates that easily prepared and robust (ppy)Pt^II(acac) complexes show promising reactivity toward amyloid fibrils and represent attractive molecular scaffolds for design of small-molecule probes targeting amyloid assemblies.

中文翻译：

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通过发光两亲性铂 (II) 络合物检测和分解淀粉样原纤维

具有疏水性 2-苯基吡啶 (ppy) 配体和亲水性丙酮基丙酮 (acac) 配体的环金属化 Pt( II ) 配合物已被研究用于通过发光响应检测淀粉样原纤维的能力。使用鸡蛋清溶菌酶 (HEWL) 作为淀粉样蛋白模型，具有苯甲酰苯胺取代的 ppy 配体和乙二醇功能化 acac 配体的 Pt( II ) 配合物在 HEWL 原纤维存在下表现出增强的发光，而缺乏 HEWL 原纤维的 Pt( II ) 配合物互补的疏水/亲水配体组显示出很少甚至没有发射增强。此外，还发现含有双（乙二醇）衍生的 acac 配体的两亲性 Pt( II ) 络合物能够触发 HEWL 原纤维重组为更小的球形聚集体。两亲性 Pt( II ) 复合物通常对 SH-SY5Y 神经母细胞瘤细胞无毒，并且几种复合物在与阿尔茨海默氏病相关的Aβ ₄₂原纤维存在下也表现出增强的发光。这项研究表明，易于制备且稳定的 (ppy)Pt ^II (acac) 复合物对淀粉样蛋白原纤维表现出良好的反应性，并为设计针对淀粉样蛋白组装体的小分子探针提供了有吸引力的分子支架。