Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils
(2019) In Journal of Physical Chemistry Letters 10(24). p.7872-7877- 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... (More)
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.
(Less)
- author
- Galvagnion, Céline ; Topgaard, Daniel LU ; Makasewicz, Katarzyna LU ; Buell, Alexander K. ; Linse, Sara LU ; Sparr, Emma LU and Dobson, Christopher M.
- organization
- publishing date
- 2019-12-19
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Physical Chemistry Letters
- volume
- 10
- issue
- 24
- pages
- 6 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- scopus:85076779245
- pmid:31790267
- ISSN
- 1948-7185
- DOI
- 10.1021/acs.jpclett.9b03005
- language
- English
- LU publication?
- yes
- id
- 75636894-eb0e-4cbe-acc4-3c31a5706126
- date added to LUP
- 2020-01-10 10:44:35
- date last changed
- 2024-09-18 16:34:51
@article{75636894-eb0e-4cbe-acc4-3c31a5706126, abstract = {{<p>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 <sup>13</sup>C and <sup>31</sup>P 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.</p>}}, author = {{Galvagnion, Céline and Topgaard, Daniel and Makasewicz, Katarzyna and Buell, Alexander K. and Linse, Sara and Sparr, Emma and Dobson, Christopher M.}}, issn = {{1948-7185}}, language = {{eng}}, month = {{12}}, number = {{24}}, pages = {{7872--7877}}, publisher = {{The American Chemical Society (ACS)}}, series = {{Journal of Physical Chemistry Letters}}, title = {{Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils}}, url = {{http://dx.doi.org/10.1021/acs.jpclett.9b03005}}, doi = {{10.1021/acs.jpclett.9b03005}}, volume = {{10}}, year = {{2019}}, }