title: The mode of α-synuclein binding to membranes depends on lipid composition and lipid to protein ratio.
abstract: Interactions of the presynaptic protein α-synuclein with membranes are involved in its physiological action as well as in the pathological misfolding and aggregation related to Parkinsons's disease. We studied the conformation and orientation of α-synuclein bound to model vesicular membranes using multiparametric response polarity-sensitive fluorescent probes together with CD and EPR measurements. At low lipid to α-synuclein ratio the protein binds membranes through its N-terminal domain. When lipids are in excess, the α-helical content and the role of the C-terminus in binding increase. Highly rigid membranes also induce a greater α-helical content and a lower polarity of the protein microenvironment.
authors: Laboratory of Cellular Dynamics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany. vshvadc@gwdg.de
authors: Volodymyr V
authors: VV
authors: Shvadchak
authors: Dmytro A
authors: DA
authors: Yushchenko
authors: Roberta
authors: R
authors: Pievo
authors: Thomas M
authors: TM
authors: Jovin
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D002942:Circular Dichroism; D008051:Lipid Bilayers / Q000737:chemistry; D008567:Membranes, Artificial; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D051844:alpha-Synuclein / Q000737:chemistry*
chemical_list: D008051:Lipid Bilayers; D008567:Membranes, Artificial; D051844:alpha-Synuclein