期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
卷 1844, 期 7, 页码 1307-1316出版社
ELSEVIER
DOI: 10.1016/j.bbapap.2014.04.010
关键词
Neurodegenerative disease; Molecular mechanism; Trehalose; Thermal stress; Stability; Flexibility
资金
- EU [RB1210067]
- Centre National de la Recherche Scientifique
- French Agence Nationale de la Recherche [ANR-11-BSV8-021-01]
In the present paper, Quasi Elastic Neutron Scattering (QENS) results, gathered at different energy resolution values at the ISIS Facility (RAL, UK), on alpha-synuclein in soluble and fibrillar forms as a function of temperature and exchanged wave-vector Q are shown. The measurements reveal a different dynamic behavior of the soluble and fibrillar forms of alpha-synuclein as a function of thermal stress. In more detail, the dynamics of each protein form reflects its own complex conformational heterogeneity. Furthermore, the effect of a well known bioprotectant, trehalose, that influences alpha-synuclein fibrillation, on both soluble and fibrillar forms of alpha-synuclein is discussed. (C) 2014 Elsevier B.V. All rights reserved.
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