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α-synuclein insertion into supported lipid bilayers as seen by in situ x-ray reflectivity


Hähl, Hendrik; Möller, Isabelle; Kiesel, Irena; Campioni, Silvia; Riek, Roland; Verdes, Dorinel; Seeger, Stefan (2015). α-synuclein insertion into supported lipid bilayers as seen by in situ x-ray reflectivity. ACS Chemical Neuroscience, 6(3):374-379.

Abstract

Large aggregates of misfolded α-synuclein inside neuronal cells are the hallmarks of Parkinson’s disease. The protein’s natural function and its supposed toxicity, however, are believed to be closely related to its interaction with cell and vesicle membranes. Upon this interaction, the protein folds into an α-helical structure and intercalates into the membrane. In this study, we focus on the changes in the lipid bilayer caused by this intrusion. In situ X-ray reflectivity was applied to determine the vertical density structure of the bilayer before and after exposure to α-synuclein. It was found that the α-synuclein insertion, wild type and E57K variant, caused a reduction in bilayer thickness. This effect may be one factor in the membrane pore formation ability of α-synuclein.

Abstract

Large aggregates of misfolded α-synuclein inside neuronal cells are the hallmarks of Parkinson’s disease. The protein’s natural function and its supposed toxicity, however, are believed to be closely related to its interaction with cell and vesicle membranes. Upon this interaction, the protein folds into an α-helical structure and intercalates into the membrane. In this study, we focus on the changes in the lipid bilayer caused by this intrusion. In situ X-ray reflectivity was applied to determine the vertical density structure of the bilayer before and after exposure to α-synuclein. It was found that the α-synuclein insertion, wild type and E57K variant, caused a reduction in bilayer thickness. This effect may be one factor in the membrane pore formation ability of α-synuclein.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Language:English
Date:2015
Deposited On:10 Feb 2015 15:14
Last Modified:18 Apr 2018 11:46
Publisher:American Chemical Society
ISSN:1948-7193
Funders:Swiss National Science Foundation (SNSF), German Federal Ministry of Education and Research (BMBF) (Project 05K10PEC), Cluster of Excellence RESOLV (EXC1069) funded by the German Research Foundation (DFG)
Additional Information:This document is the Accepted Manuscript version of a Published Work that appeared in final form in [ACS Chem. Neuroscience], copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see [http://pubs.acs.org/doi/abs/10.1021/cn5002683].
OA Status:Green
Publisher DOI:https://doi.org/10.1021/cn5002683
PubMed ID:25523270
Project Information:
  • : FunderSNSF
  • : Grant ID
  • : Project TitleSwiss National Science Foundation (SNSF)
  • : Funder
  • : Grant ID
  • : Project TitleGerman Federal Ministry of Education and Research (BMBF) (Project 05K10PEC)
  • : Funder
  • : Grant ID
  • : Project TitleCluster of Excellence RESOLV (EXC1069) funded by the German Research Foundation (DFG)

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