Using a combination of Small Angle X-ray and Neutron Scattering (SAXS/SANS) measurements, we show that the binding of α-synuclein, the protein involved in Parkinson’s Disease, to negatively charged membranes leads to the fast (<ms) and reversible breakage of vesicles into small, cylindrical and disc-like lipid-protein particles that is followed by a slower (days) and irreversible aggregation process consisting of the co-assembly of α-synuclein and lipid molecules into amyloid fibrils. We hope that these results will help providing a better understanding of the molecular mechanisms leading to the formation of complex protein-lipid assemblies such as the Lewy Bodies found in the brains of patients with Parkinson’s Disease.
Preprint: Structural characterisation of α-synuclein-membrane interactions and the resulting aggregation using small angle scattering.
Galvagnion Group 