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吡咯并喹啉醌抑制淀粉样蛋白的纤维形成。

Pyrroloquinoline quinone inhibits the fibrillation of amyloid proteins.

机构信息

Department of Biotechnology, Graduate School of Engineering, Tokyo University of Agriculture & Technology, Koganei-shi, Tokyo, Japan.

出版信息

Prion. 2010 Jan-Mar;4(1):26-31. doi: 10.4161/pri.4.1.10889. Epub 2010 Jan 4.

Abstract

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 beta (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 beta (1-42) also decreased. With further advanced pharmacological approaches, PQQ may become a leading anti-neurodegenerative compound in the treatment of neurodegenerative diseases.

摘要

几种神经退行性疾病涉及神经元细胞的选择性损伤,这是由于淀粉样纤维形成的积累。考虑到淀粉样纤维的形成以及它们的前体寡聚物是细胞毒性的,因此防止寡聚物和/或纤维形成的试剂可能允许开发针对神经退行性疾病的新的治疗方法。在这里,我们表明吡咯并喹啉醌(PQQ)抑制淀粉样蛋白,淀粉样β(1-42)和鼠朊蛋白的淀粉样纤维形成。在 PQQ 存在下,鼠朊蛋白的纤维形成被显著阻止。同样,淀粉样β(1-42)的纤维形成也减少。通过进一步的药理学方法,PQQ 可能成为治疗神经退行性疾病的主要抗神经退行性化合物。

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