Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils
Publikation: Bidrag til tidsskrift › Letter › Forskning › fagfællebedømt
Dokumenter
- acs.jpclett.9b03005
Forlagets udgivne version, 5,29 MB, PDF-dokument
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.
Originalsprog | Engelsk |
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Tidsskrift | The Journal of Physical Chemistry Letters |
Vol/bind | 10 |
Udgave nummer | 24 |
Sider (fra-til) | 7872-7877 |
Antal sider | 6 |
ISSN | 1948-7185 |
DOI | |
Status | Udgivet - 19 dec. 2019 |
Eksternt udgivet | Ja |
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ID: 232912682