| Literature DB >> 22575388 |
Wen-Bo Yu1, Teng Jiang, Dan-Mei Lan, Jia-Hong Lu, Zhen-Yu Yue, Jian Wang, Ping Zhou.
Abstract
The aggregation of alpha-synuclein (AS) is pivotally implicated in the development of Parkinson's disease (PD), inhibiting this process might be effective in treating PD. Here, by using circular dichroism spectroscopy, thioflavin T fluorescence, and atomic force microscopy, we found that trehalose at low concentration disaggregates preformed A53T AS protofibrils and fibrils into small aggregates or even random coil structure, while trehalose at high concentration slows down the structural transition into β-sheet structure and completely prevents the formation of mature A53T AS fibrils. Further work in vivo will be needed to evaluate its potential as a novel strategy for treating PD.Entities:
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Year: 2012 PMID： 22575388 DOI： 10.1016/j.abb.2012.04.021
Source DB: PubMed Journal: Arch Biochem Biophys ISSN： 0003-9861 Impact factor: 4.013