title: α-Synuclein insertion into supported lipid bilayers as seen by in situ X-ray reflectivity.
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.
authors.affiliation: †Department of Chemistry, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.
authors.forename: Hendrik
authors.initials: H
authors.lastname: Hähl
authors.affiliation: †Department of Chemistry, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.
authors.forename: Isabelle
authors.initials: I
authors.lastname: Möller
authors.affiliation: ‡Fakultät Physik/DELTA, Technische Universität Dortmund, 44221 Dortmund, Germany.
authors.forename: Irena
authors.initials: I
authors.lastname: Kiesel
authors.affiliation: §Laboratory of Physical Chemistry, Department of Chemistry and Applied Biosciences, Swiss Federal Institute of Technology Zurich, Wolfgang-Pauli-Str. 10, 8093 Zurich, Switzerland.
authors.forename: Silvia
authors.initials: S
authors.lastname: Campioni
authors.affiliation: §Laboratory of Physical Chemistry, Department of Chemistry and Applied Biosciences, Swiss Federal Institute of Technology Zurich, Wolfgang-Pauli-Str. 10, 8093 Zurich, Switzerland.
authors.forename: Roland
authors.initials: R
authors.lastname: Riek
authors.affiliation: †Department of Chemistry, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.
authors.forename: Dorinel
authors.initials: D
authors.lastname: Verdes
authors.affiliation: †Department of Chemistry, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.
authors.forename: Stefan
authors.initials: S
authors.lastname: Seeger
mesh_terms: D000818:Animals; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry*; D008958:Models, Molecular; D009154:Mutation / Q000235:genetics; D017433:Protein Structure, Secondary; D014965:X-Rays; D051844:alpha-Synuclein / Q000737:chemistry* / Q000235:genetics
chemical_list: D008051:Lipid Bilayers; D051844:alpha-Synuclein
keywords: Parkinson’s disease; X-ray reflectivity; supported lipid bilayer; α-Synuclein