Structural characterisation of α-synuclein-membrane interactions and the resulting aggregation using small angle scattering Article Swipe
Céline Galvagnion
,
Abigail Barclay
,
Katarzyna Makasewicz
,
Frederik Ravnkilde Marlet
,
Martine Moulin
,
Juliette M. Devos
,
Sara Linse
,
Anne Martel
,
Lionel Porcar
,
Emma Sparr
,
Martin Cramer Pedersen
,
Felix Roosen‐Runge
,
Lise Arleth
,
Alexander Büll
·
YOU?
·
· 2023
· Open Access
·
· DOI: https://doi.org/10.26434/chemrxiv-2023-6hsh2
YOU?
·
· 2023
· Open Access
·
· DOI: https://doi.org/10.26434/chemrxiv-2023-6hsh2
The presence of amyloid fibrils is a hallmark of several neurodegenerative diseases. Some amyloidogenic proteins, such as α-synuclein and amyloid β, can interact with lipids, and this interaction can strongly favor the formation of amyloid fibrils. In particular the primary nucleation step, i.e. the de novo formation of amyloid fibrils, has been shown to be accelerated by lipids. However, the exact mechanism of this acceleration is still mostly unclear. Here we use a range of scattering methods, such as dynamic light scattering (DLS) and small angle X-ray and neutron scattering (SAXS and SANS) to obtain structural information on the binding of α-synuclein to vesicles formed from negatively charged lipids and their co-assembly into amyloid fibrils. We find that the lipid vesicles do not simply act as a surface that catalyses the nucleation reaction, but that lipid molecules take an active role in the reaction. The binding of α-synuclein to the lipid vesicles immediately induces a major structural change in the lipid assembly, which leads to a break-up into small, cylindrical and disc-like lipid-protein particles. This transition can be largely reversed by temperature changes or proteolytic protein removal. Incubation of these small, cylindrical and disc-like lipid-α-synuclein particles for several hours, however, yields amyloid fibril formation, whereby the lipids are incorporated into the fibrils.
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- Type
- preprint
- Language
- en
- Landing Page
- https://doi.org/10.26434/chemrxiv-2023-6hsh2
- https://chemrxiv.org/engage/api-gateway/chemrxiv/assets/orp/resource/item/6404ef6b63e8d44e596c3b8e/original/structural-characterisation-of-synuclein-membrane-interactions-and-the-resulting-aggregation-using-small-angle-scattering.pdf
- OA Status
- gold
- Cited By
- 2
- References
- 26
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4323311775
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Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4323311775Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.26434/chemrxiv-2023-6hsh2Digital Object Identifier
- Title
-
Structural characterisation of α-synuclein-membrane interactions and the resulting aggregation using small angle scatteringWork title
- Type
-
preprintOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2023Year of publication
- Publication date
-
2023-03-06Full publication date if available
- Authors
-
Céline Galvagnion, Abigail Barclay, Katarzyna Makasewicz, Frederik Ravnkilde Marlet, Martine Moulin, Juliette M. Devos, Sara Linse, Anne Martel, Lionel Porcar, Emma Sparr, Martin Cramer Pedersen, Felix Roosen‐Runge, Lise Arleth, Alexander BüllList of authors in order
- Landing page
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https://doi.org/10.26434/chemrxiv-2023-6hsh2Publisher landing page
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https://chemrxiv.org/engage/api-gateway/chemrxiv/assets/orp/resource/item/6404ef6b63e8d44e596c3b8e/original/structural-characterisation-of-synuclein-membrane-interactions-and-the-resulting-aggregation-using-small-angle-scattering.pdfDirect link to full text PDF
- Open access
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YesWhether a free full text is available
- OA status
-
goldOpen access status per OpenAlex
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https://chemrxiv.org/engage/api-gateway/chemrxiv/assets/orp/resource/item/6404ef6b63e8d44e596c3b8e/original/structural-characterisation-of-synuclein-membrane-interactions-and-the-resulting-aggregation-using-small-angle-scattering.pdfDirect OA link when available
- Concepts
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Fibril, Vesicle, Small-angle X-ray scattering, Nucleation, Biophysics, Chemistry, Lipid bilayer, Amyloid (mycology), Small-angle neutron scattering, Protein aggregation, Crystallography, Membrane, Neutron scattering, Scattering, Biochemistry, Biology, Organic chemistry, Inorganic chemistry, Physics, OpticsTop concepts (fields/topics) attached by OpenAlex
- Cited by
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2Total citation count in OpenAlex
- Citations by year (recent)
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2024: 2Per-year citation counts (last 5 years)
- References (count)
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26Number of works referenced by this work
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10Other works algorithmically related by OpenAlex
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