The Journal of Physical Chemistry Letters · 2019 · 60 citations · 25 references
Life SciencesBiochemistryBiophysicsLipid BiochemistryNeurodegenerationStructural BiologyAmyloid FormationLipid ChemistryLipid StructureMacromolecular AssemblyParkinson DiseaseProtein-lipid InteractionsAlpha-synuclein AggregationAlpha-synuclein MisfoldingAmyloid Fibril FormationAmyloid FibrillogenesisAmyloid FibrilsAmyloid StructureNuclear Magnetic Resonance SpectroscopyPhase Transition Enthalpy
-glycero-3-phospho-L-serine. Our results show that these lipids coassemble with α-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.
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Alexander K. Buell, Céline Galvagnion, Ricardo Gaspar et al. · Proceedings of the National Academy of Sciences · 2014 · 687 citations · Full text
Acceleration of α-Synuclein Aggregation by Exosomes
Marie Grey, Christopher J.R. Dunning, Ricardo Gaspar et al. · Journal of Biological Chemistry · 2014 · 377 citations · Full text