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首页> 外文期刊>Biochemistry >The parkinson's disease-associated H50Q mutation accelerates α-synuclein aggregation in vitro
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The parkinson's disease-associated H50Q mutation accelerates α-synuclein aggregation in vitro

机译：帕金森氏病相关的H50Q突变在体外促进α-突触核蛋白的聚集

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摘要

α-Synuclein (α-Syn) aggregation is directly linked with Parkinson's disease (PD) pathogenesis. Here, we analyzed the aggregation of newly discovered α-Syn missense mutant H50Q in vitro and found that this mutation significantly accelerates the aggregation and amyloid formation of α-Syn. This mutation, however, did not alter the overall secondary structure as suggested by two-dimensional nuclear magnetic resonance and circular dichroism spectroscopy. The initial oligomerization study by cross-linking and chromatographic techniques suggested that this mutant oligomerizes to an extent similar to that of the wild-type α-Syn protein. Understanding the aggregation mechanism of this H50Q mutant may help to establish the aggregation and phenotypic relationship of this novel mutant in PD.
机译：α-突触核蛋白（α-Syn）聚集与帕金森氏病（PD）发病机理直接相关。在这里，我们分析了新近发现的α-Syn错义突变体H50Q的聚集，发现该突变显着加速了α-Syn的聚集和淀粉样蛋白的形成。然而，这种突变并未改变二维核磁共振和圆二色性光谱学所表明的整体二级结构。最初通过交联和色谱技术进行的寡聚研究表明，该突变体的寡聚程度与野生型α-Syn蛋白相似。了解此H50Q突变体的聚集机制可能有助于建立该新型突变体在PD中的聚集和表型关系。

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