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Structural characterisation of α-synuclein-membrane interactions and the resulting aggregation using small angle scattering
Univ Copenhagen, Dept Drug Design & Pharmacol, DK-2100 Copenhagen, Denmark..ORCID iD: 0000-0001-9753-3310
Univ Copenhagen, Niels Bohr Inst, DK-2100 Copenhagen, Denmark..
Lund Univ, Div Phys Chem, Ctr Chem & Chem Engn, POB 124, SE-22100 Lund, Sweden..
Univ Copenhagen, Dept Drug Design & Pharmacol, DK-2100 Copenhagen, Denmark..
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2024 (English)In: Physical Chemistry, Chemical Physics - PCCP, ISSN 1463-9076, E-ISSN 1463-9084, Vol. 26, no 14, p. 10998-11013Article in journal (Refereed) Published
Abstract [en]

The presence of amyloid fibrils is a hallmark of several neurodegenerative diseases. Some amyloidogenic proteins, such as alpha-synuclein and amyloid beta, interact with lipids, and this interaction can strongly favour 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 alpha-synuclein to model membranes formed from negatively charged lipids and their co-assembly into amyloid fibrils. We find that the model membranes take an active role in the reaction. The binding of alpha synuclein to the model membranes immediately induces a major structural change in the lipid assembly, which leads to a break-up into small and mostly disc- or rod-like lipid-protein particles. This transition can be reversed by temperature changes or proteolytic protein removal. Incubation of the small lipid-alpha-synuclein particles for several hours, however, leads to amyloid fibril formation, whereby the lipids are incorporated into the amyloid fibrils. alpha S binding to DLPS and DMPS leads to a ms fast reversible deformation into disks and rods. Upon further incubation, lipid rods elongate within the same time scale as that of amyloid formation confirming lipids co-assembly with alpha S into fibrils.

Place, publisher, year, edition, pages
Royal Society of Chemistry, 2024. Vol. 26, no 14, p. 10998-11013
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Physical Chemistry
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URN: urn:nbn:se:mau:diva-66875DOI: 10.1039/d3cp05928fISI: 001190257400001PubMedID: 38526443Scopus ID: 2-s2.0-85189684400OAI: oai:DiVA.org:mau-66875DiVA, id: diva2:1853690
Available from: 2024-04-23 Created: 2024-04-23 Last updated: 2024-04-29Bibliographically approved

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Roosen-Runge, Felix

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Galvagnion, CelineRoosen-Runge, FelixArleth, LiseBuell, Alexander K.
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