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  Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts.

Strohäker, T., Jung, B. C., Liou, S. H., Fernandez, C. O., Riedel, D., Becker, S., et al. (2019). Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts. Nature Communications, 10: 5535. doi:10.1038/s41467-019-13564-w.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-5568-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-556E-1
Genre: Journal Article

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 Creators:
Strohäker, T.1, Author              
Jung, B. C., Author
Liou, S. H.2, Author              
Fernandez, C. O., Author
Riedel, D.3, Author              
Becker, S.4, Author              
Halliday, G. M., Author
Bennati, M.2, Author              
Kim, W. S., Author
Lee, S. J., Author
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society, ou_578571              
2Research Group of Electron Paramagnetic Resonance, MPI for Biophysical Chemistry, Max Planck Society, ou_578606              
3Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578615              
4Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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 Abstract: Parkinson's disease (PD) and Multiple System Atrophy (MSA) are clinically distinctive diseases that feature a common neuropathological hallmark of aggregated α-synuclein. Little is known about how differences in α-synuclein aggregate structure affect disease phenotype. Here, we amplified α-synuclein aggregates from PD and MSA brain extracts and analyzed the conformational properties using fluorescent probes, NMR spectroscopy and electron paramagnetic resonance. We also generated and analyzed several in vitro α-synuclein polymorphs. We found that brain-derived α-synuclein fibrils were structurally different to all of the in vitro polymorphs analyzed. Importantly, there was a greater structural heterogeneity among α-synuclein fibrils from the PD brain compared to those from the MSA brain, possibly reflecting on the greater variability of disease phenotypes evident in PD. Our findings have significant ramifications for the use of non-brain-derived α-synuclein fibrils in PD and MSA studies, and raise important questions regarding the one disease-one strain hypothesis in the study of α-synucleinopathies.

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Language(s): eng - English
 Dates: 2019-12-04
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-019-13564-w
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Title: Nature Communications
Source Genre: Journal
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Pages: 12 Volume / Issue: 10 Sequence Number: 5535 Start / End Page: - Identifier: -