lysineacetylationinhibitsasynucleinfibrillation
文献类型：期刊论文
| 作者 | Zhai Zining; Wu Qiong; Li Conggang |
| 刊名 | 波谱学杂志
 |
| 出版日期 | 2016 |
| 卷号 | 33期号:2页码:179 |
| ISSN号 | 1000-4556 |
| 英文摘要 | Fibrils of intrinsically disordered protein α-synuclein (α-syn) are hallmarks of Parkinson's disease. Electrostatic interactions are known to contribute significantly on α-syn aggregation. Here we studied how α-syn conformation and fibrillation were affected by changing the net charge of the protein via acetylation of lysine side chains. NMR spectroscopy results showed that lysine-acetylated α-syn remained disordered, and showed a more extended conformation, relative to wild-type protein. Acetylation inhibited α-syn fibrillation, revealed by thioflavin (ThT) fluorescence assay. The N- and C-terminals of the acetylated protein were highly negative charged, causing increased exposure of the non-amyloid-β component (NAC) region. It is proposed that, with the charge distribution in the acetylated protein, electrostatic repulsion, instead of hydrophobic effect, may contribute predominately to the aggregation. This charge-effect mechanism may constitute a new strategy to inhibit α-syn fibrillation. |
| 语种 | 英语 |
| 源URL | [http://ir.wipm.ac.cn/handle/112942/17581]  |
| 专题 | 中国科学院武汉物理与数学研究所 |
| 作者单位 | 中国科学院武汉物理与数学研究所 |
| 推荐引用方式 GB/T 7714 | Zhai Zining,Wu Qiong,Li Conggang. lysineacetylationinhibitsasynucleinfibrillation[J]. 波谱学杂志,2016,33(2):179. |
| APA | Zhai Zining,Wu Qiong,&Li Conggang.(2016).lysineacetylationinhibitsasynucleinfibrillation.波谱学杂志,33(2),179. |
| MLA | Zhai Zining,et al."lysineacetylationinhibitsasynucleinfibrillation".波谱学杂志 33.2(2016):179. |
入库方式： OAI收割
来源：武汉物理与数学研究所
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