Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils

Céline Galvagnion, Daniel Topgaard, Katarzyna Makasewicz, Alexander K. Buell, Sara Linse, Emma Sparr, Christopher M. Dobson

Research output: Contribution to journalArticlepeer-review

11 Citations (SciVal)

Abstract

The deposition of coassemblies made of the small presynaptic protein, α-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 α-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 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.

Original languageEnglish
Pages (from-to)7872-7877
Number of pages6
JournalJournal of Physical Chemistry Letters
Volume10
Issue number24
DOIs
Publication statusPublished - 2019 Dec 19

Subject classification (UKÄ)

  • Physical Chemistry
  • Biophysics

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