Trehalose inhibits fibrillation of A53T mutant alpha-synuclein and disaggregates existing fibrils

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• 作者：Wen-Bo Yu^a ; ¹ ; ² ; Teng Jiang^c ; ² ; Dan-Mei Lan^a ; ^b ; ² ; Jia-Hong Lu^a ; ^b ; Zhen-Yu Yue^d ; Jian Wang^a ; ^b ; ^{wangjian336@hotmail.com} ; Ping Zhou^c ; ^{pingzhou@fudan.edu.cn}
• 关键词：Trehalose ; Parkinson&rsquo ; s disease ; Alpha-synuclein ; Protein conformation ; Aggregate morphologies
• 刊名：Archives of Biochemistry and Biophysics
• 出版年：2012
• 期刊代码：116_00039861
• 类别：ch
• 出版时间：15 July, 2012
• 卷：523
• 期：2
• 页码：144-150
• 文件大小：1722 K

摘要

The aggregation of alpha-synuclein (AS) is pivotally implicated in the development of Parkinson鈥檚 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 尾-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.