Effects of Trehalose on Thermodynamic Properties of Alpha-synuclein Revealed through Synchrotron Radiation Circular Dichroism.

Many neurodegenerative diseases, including Huntington's, Alzheimer's and Parkinson's diseases, are characterized by protein misfolding and aggregation. The capability of trehalose to interfere with protein misfolding and aggregation has been recently evaluated by several research groups. In the present work, we studied, by means of synchrotron radiation circular dichroism (SRCD) spectroscopy, the dose-effect of trehalose on alpha-synuclein conformation and/or stability to probe the capability of this osmolyte to interfere with alpha-synuclein's aggregation. Our study indicated that a low trehalose concentration stabilized alpha-synuclein folding much better than at high concentration by blocking in vitro alpha-synuclein's polymerisation. These results suggested that trehalose could be associated with other drugs leading to a new approach for treating Parkinson's and other brain-related diseases.