title: Membrane bound α-synuclein is fully embedded in the lipid bilayer while segments with higher flexibility remain.
abstract: Cellular pathways involving α-synuclein (αS) seem to be causative for development of Parkinson's disease. Interactions between αS and lipid membranes appear to be important for the physiological function of the protein and influence the pathological aggregation of αS leading to the formation of amyloid plaques. Upon membrane binding the unstructured αS folds into amphipathic helices. In our work we characterized the penetration depth and probed the local environment of Trp-residues introduced along the αS sequence. We could show that while the entire helix is well embedded in the lipid bilayer, segments with a shallower penetration and supposable higher flexibility exist.
authors.affiliation: Department of Biology, Faculty of Mathematics and Natural Sciences I, Humboldt University Berlin, Invalidenstr. 42, 10115 Berlin, Germany.
authors.forename: Jonas
authors.initials: J
authors.lastname: Wietek
authors.forename: Ivan
authors.initials: I
authors.lastname: Haralampiev
authors.forename: Aouefa
authors.initials: A
authors.lastname: Amoussouvi
authors.forename: Andreas
authors.initials: A
authors.lastname: Herrmann
authors.forename: Martin
authors.initials: M
authors.lastname: Stöckl
mesh_terms: D020106:Acrylamide / Q000737:chemistry; D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000378:metabolism; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry*; D008055:Lipids / Q000737:chemistry; D008823:Micelles; D008969:Molecular Sequence Data; D010300:Parkinson Disease / Q000378:metabolism; D010713:Phosphatidylcholines / Q000737:chemistry; D010718:Phosphatidylserines / Q000737:chemistry; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D014364:Tryptophan / Q000737:chemistry; D051844:alpha-Synuclein / Q000737:chemistry*
chemical_list: D008051:Lipid Bilayers; D008055:Lipids; D008823:Micelles; D010713:Phosphatidylcholines; D010718:Phosphatidylserines; D051844:alpha-Synuclein; D020106:Acrylamide; C050294:1-palmitoyl-2-oleoylglycero-3-phosphoserine; D014364:Tryptophan; C028694:1-palmitoyl-2-oleoylphosphatidylcholine
keywords: Fluorescence spectroscopy; Lipid bilayer; Penetration depth; alpha-synuclein