Dynamical properties of α-synuclein in soluble and fibrillar forms by Quasi Elastic Neutron Scattering

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.