Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 523, Issue 2, Pages 144-150Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2012.04.021
Keywords
Trehalose; Parkinson's disease; Alpha-synuclein; Protein conformation; Aggregate morphologies
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Funding
- Natural Science Foundation of China [30600663, 81071018, 20673022, 21074025]
- Project of Pujiang Talents at Shanghai [10PJ1401700]
- Project Science and Technology Innovation Action Plan [09411960900, 11DZ1971802]
- Science and Technology Commission of Shanghai Municipality
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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 beta-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. (C) 2012 Elsevier Inc. All rights reserved.
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