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

• The dynamics of soluble and fibrillar forms of α-synuclein is characterized.
• The response of the protein to the thermal stress is determined.
• The α-synuclein conformational heterogeneity is reflected in its dynamical behavior.
• Trehalose affects the flexibility of both soluble and fibrillar forms of α-synuclein.

In the present paper, Quasi Elastic Neutron Scattering (QENS) results, gathered at different energy resolution values at the ISIS Facility (RAL, UK), on α-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 α-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 α-synuclein fibrillation, on both soluble and fibrillar forms of α-synuclein is discussed.

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