Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils

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Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils. / Galvagnion, Céline; Topgaard, Daniel; Makasewicz, Katarzyna; Buell, Alexander K.; Linse, Sara; Sparr, Emma; Dobson, Christopher M.

I: Journal of Physical Chemistry Letters, Vol. 10, Nr. 24, 19.12.2019, s. 7872-7877.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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TY - JOUR

T1 - Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils

AU - Galvagnion, Céline

AU - Topgaard, Daniel

AU - Makasewicz, Katarzyna

AU - Buell, Alexander K.

AU - Linse, Sara

AU - Sparr, Emma

AU - Dobson, Christopher M.

PY - 2019/12/19

Y1 - 2019/12/19

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85076779245&partnerID=8YFLogxK

U2 - 10.1021/acs.jpclett.9b03005

DO - 10.1021/acs.jpclett.9b03005

M3 - Article

C2 - 31790267

AN - SCOPUS:85076779245

VL - 10

SP - 7872

EP - 7877

JO - The Journal of Physical Chemistry Letters

JF - The Journal of Physical Chemistry Letters

SN - 1948-7185

IS - 24

ER -