Lipid Dynamics and Phase Transition within ?-Synuclein Amyloid Fibrils.

ABSTRACT: The deposition of coassemblies made of the small presynaptic protein, ?-synuclein, and lipids in the brains of patients is the hallmark of Parkinson's disease. In this study, we used natural abundance ¹³C and ³¹P magic-angle spinning nuclear magnetic resonance spectroscopy together with cryo-electron microscopy and differential scanning calorimetry to characterize the fibrils formed by ?-synuclein in the presence of vesicles made of 1,2-dimyristoyl-sn-glycero-3-phospho-L-serine or 1,2-dilauroyl-sn-glycero-3-phospho-L-serine. Our results show that these lipids coassemble with ?-synuclein molecules to give thin and curly amyloid fibrils. The coassembly leads to slower and more isotropic reorientation of lipid molecular segments and a decrease in both the temperature and enthalpy of the lipid chain-melting compared with those in the protein-free lipid lamellar phase. These findings provide new insights into the properties of lipids within protein-lipid assemblies that can be associated with Parkinson's disease.

SUBMITTER: Galvagnion C 

PROVIDER: S-EPMC6937551 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature