Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils
| Autor: | Sara Linse, Daniel Topgaard, Katarzyna Makasewicz, Céline Galvagnion, Christopher M. Dobson, Alexander K. Buell, Emma Sparr |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Phase transition
Amyloid Letter Kinetics Lipid Bilayers chemistry [Lipid Bilayers] Plasma protein binding Fibril Phase Transition 03 medical and health sciences Structure-Activity Relationship 0302 clinical medicine Differential scanning calorimetry Lamellar phase chemistry [Serine] Serine chemistry [Amyloid] Transition Temperature General Materials Science ddc:530 Physical and Theoretical Chemistry 030304 developmental biology 0303 health sciences Molecular Structure Chemistry Vesicle Nuclear magnetic resonance spectroscopy chemistry [alpha-Synuclein] Biophysics alpha-Synuclein Thermodynamics lipids (amino acids peptides and proteins) 030217 neurology & neurosurgery Protein Binding |
| Zdroj: | The Journal of Physical Chemistry Letters 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 ', Journal of Physical Chemistry Letters, vol. 10, pp. 7872-7877 . https://doi.org/10.1021/acs.jpclett.9b03005 The journal of physical chemistry letters 10(24), 7872-7877 (2019). doi:10.1021/acs.jpclett.9b03005 |
| ISSN: | 1948-7185 |
| DOI: | 10.1021/acs.jpclett.9b03005 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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