title: Copper(II) enhances membrane-bound α-synuclein helix formation.
abstract: Interactions of copper and membranes with α-synuclein have been implicated in pathogenic mechanisms of Parkinson's disease, yet work examining both concurrently is scarce. We have examined the effect of copper(ii) on protein/vesicle binding and found that both the copper(ii) affinity and α-helical content are enhanced for the membrane-bound protein.
authors.affiliation: Laboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
authors.forename: Heather R
authors.initials: HR
authors.lastname: Lucas
authors.forename: Jennifer C
authors.initials: JC
authors.lastname: Lee
mesh_terms: D003300:Copper / Q000378:metabolism*; D006801:Humans; D008051:Lipid Bilayers / Q000378:metabolism*; D008081:Liposomes / Q000378:metabolism; D010300:Parkinson Disease / Q000378:metabolism; D011485:Protein Binding; D017433:Protein Structure, Secondary; D051844:alpha-Synuclein / Q000737:chemistry / Q000378:metabolism*
chemical_list: D008051:Lipid Bilayers; D008081:Liposomes; D051844:alpha-Synuclein; D003300:Copper