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 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.
Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, Bat 34, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France.
Luc
L
Bousset
Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, Bat 34, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France.
Clémence
C
Brewee
Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, Bat 34, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France.
Ronald
R
Melki
Department of Physics and Earth Sciences, University of Messina, Viale D'Alcontres 31, 98166 Messina, Italy. Electronic address: fmigliardo@unime.it.
Federica
F
Migliardo
D006801:Humans; D008962:Models, Theoretical; D056004:Molecular Dynamics Simulation; D033363:Neutron Diffraction; D013696:Temperature; D014199:Trehalose / Q000737:chemistry; D014867:Water / Q000737:chemistry*; D051844:alpha-Synuclein / Q000737:chemistry* / Q000648:ultrastructure
D051844:alpha-Synuclein; D014867:Water; D014199:Trehalose
Flexibility; Molecular mechanism; Neurodegenerative disease; Stability; Thermal stress; Trehalose