Structural characterisation of α-synuclein–membrane interactions and the resulting aggregation using small angle scattering-Reference-Cited by-同舟云学术

Structural characterisation of α-synuclein–membrane interactions and the resulting aggregation using small angle scattering

Published:2024 Issue:14 Volume:26 Page:10998-11013
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Galvagnion Céline¹^ORCID,Barclay Abigail²,Makasewicz Katarzyna³^ORCID,Marlet Frederik Ravnkilde¹,Moulin Martine⁴,Devos Juliette M.⁴^ORCID,Linse Sara⁵^ORCID,Martel Anne⁴,Porcar Lionel⁴,Sparr Emma³^ORCID,Pedersen Martin Cramer²^ORCID,Roosen-Runge Felix³⁶^ORCID,Arleth Lise²^ORCID,Buell Alexander K.⁷^ORCID

Affiliation:

1. Department of Drug Design and Pharmacology, University of Copenhagen, 2100 Copenhagen, Denmark

2. Niels Bohr Institute, University of Copenhagen, 2100 Copenhagen, Denmark

3. Division of Physical Chemistry, Center for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-22100, Lund, Sweden

4. Institut Laue-Langevin, 71 avenue des Martyrs, 38042 Grenoble, France

5. Department of Biochemistry and Structural Biology, Lund University, SE22100 Lund, Sweden

6. Department of Biomedical Sciences and Biofilms Research Center for Biointerfaces, Malmö University, Malmö, Sweden

7. Department of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kgs. Lyngby, Denmark

Abstract

αS 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 αS into fibrils.

Funder

Novo Nordisk Fonden

Horizon 2020 Framework Programme

Lundbeck Foundation

Knut och Alice Wallenbergs Stiftelse

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/CP/D3CP05928F

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