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Pyrroloquinoline quinone inhibits the fibrillation of amyloid proteins

机译:吡咯并喹啉醌抑制淀粉样蛋白的原纤化

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Several neurodegenerative diseases involve the selective damage of neuron cells resulting from the accumulation of amyloid fibril formation. Considering that the formation of amyloid fibrils as well as their precursor oligomers is cytotoxic, the agents that prevent the formation of oligomers and/or fibrils might allow the development of a novel therapeutic approach to neurodegenerative diseases. Here, we show pyrroloquinoline quinone (PQQ) inhibits the amyloid fibril formation of the amyloid proteins, amyloid β (1-42) and mouse prion protein. The fibril formation of mouse prion protein in the presence of PQQ was dramatically prevented. Similarly, the fibril formation of amyloid β (1-42) also decreased. With further advanced pharmacological approaches, PQQ may become a leading anti-neurodegenerative compound in the treatment of neurodegenerative diseases.
机译:几种神经退行性疾病涉及由于淀粉样蛋白原纤维形成的积累而导致的神经元细胞的选择性损伤。考虑到淀粉样蛋白原纤维及其前体低聚物的形成具有细胞毒性,因此防止低聚物和/或原纤维形成的试剂可能允许开发一种新的神经退行性疾病治疗方法。在这里,我们显示吡咯并喹啉醌(PQQ)抑制淀粉样蛋白,淀粉样β(1-42)和小鼠mouse病毒蛋白的淀粉样原纤维形成。在PQQ存在下,小鼠mouse病毒蛋白的原纤维形成得到了显着的阻止。同样,淀粉样蛋白β(1-42)的原纤维形成也减少。随着进一步先进的药理学方法,PQQ可能成为治疗神经退行性疾病的领先抗神经退行性化合物。

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