lysineacetylationinhibitsasynucleinfibrillation

	lysineacetylationinhibitsasynucleinfibrillation
	Zhai Zining; Wu Qiong; Li Conggang
刊名	波谱学杂志
	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
内容类型	期刊论文
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.