Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils

Research output: Contribution to journal › Letter › Research › peer-review

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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.

In: The Journal of Physical Chemistry Letters, Vol. 10, No. 24, 19.12.2019, p. 7872-7877.

Research output: Contribution to journal › Letter › Research › peer-review

Harvard

Galvagnion, C, Topgaard, D, Makasewicz, K, Buell, AK, Linse, S, Sparr, E & Dobson, CM 2019, 'Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils', The Journal of Physical Chemistry Letters, vol. 10, no. 24, pp. 7872-7877. https://doi.org/10.1021/acs.jpclett.9b03005

APA

Galvagnion, C., Topgaard, D., Makasewicz, K., Buell, A. K., Linse, S., Sparr, E., & Dobson, C. M. (2019). Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils. The Journal of Physical Chemistry Letters, 10(24), 7872-7877. https://doi.org/10.1021/acs.jpclett.9b03005

Vancouver

Galvagnion C, Topgaard D, Makasewicz K, Buell AK, Linse S, Sparr E et al. Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils. The Journal of Physical Chemistry Letters. 2019 Dec 19;10(24):7872-7877. https://doi.org/10.1021/acs.jpclett.9b03005

Author

Galvagnion, Céline ; Topgaard, Daniel ; Makasewicz, Katarzyna ; Buell, Alexander K ; Linse, Sara ; Sparr, Emma ; Dobson, Christopher M. / Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils. In: The Journal of Physical Chemistry Letters. 2019 ; Vol. 10, No. 24. pp. 7872-7877.

Bibtex

@article{57ea074a4ceb4faabaafab9a409d7db7,
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 = "Journal of Physical Chemistry Letters",
issn = "1948-7185",
publisher = "American Chemical Society",
number = "24",

}

RIS

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.

U2 - 10.1021/acs.jpclett.9b03005

DO - 10.1021/acs.jpclett.9b03005

M3 - Letter

C2 - 31790267

VL - 10

SP - 7872

EP - 7877

JO - Journal of Physical Chemistry Letters

JF - Journal of Physical Chemistry Letters

SN - 1948-7185

IS - 24

ER -

ID: 232912682