期刊
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
卷 10, 期 24, 页码 7872-7877出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpclett.9b03005
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资金
- Marie Sklodowska-Curie Actions - Individual Fellowship (H2020-MSCA grant) [706551]
- European Soft Matter Infrastructure program
- Lundbeck Foundation
- Swedish Research Council [2014-07497, 2015-00142]
- Knut and Alice Wallenberg Foundation
- Cambridge Centre for Misfolding Diseases
- UK Biotechnology and Biochemical Sciences Research Council
- Wellcome Trust
- Novo Nordisk Foundation
- Marie Curie Actions (MSCA) [706551] Funding Source: Marie Curie Actions (MSCA)
- Swedish Research Council [2014-07497] Funding Source: Swedish Research Council
The deposition of coassemblies made of the small presynaptic protein, alpha-synuclein, and lipids in the brains of patients is the hallmark of Parkinson's disease. In this study, we used natural abundance C-13 and P-31 magic-angle spinning nuclear magnetic resonance spectroscopy together with cryo-electron microscopy and differential scanning calorimetry to characterize the fibrils formed by alpha-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 alpha-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.
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