Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils

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Bibtex

@article{75636894eb0e4cbeacc43c31a5706126,
title = "Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils",
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.",
author = "C{\'e}line Galvagnion and Daniel Topgaard and Katarzyna Makasewicz and Buell, {Alexander K.} and Sara Linse and Emma Sparr and Dobson, {Christopher M.}",
year = "2019",
month = dec,
day = "19",
doi = "10.1021/acs.jpclett.9b03005",
language = "English",
volume = "10",
pages = "7872--7877",
journal = "The Journal of Physical Chemistry Letters",
issn = "1948-7185",
publisher = "The American Chemical Society (ACS)",
number = "24",

}