title: Lipid matrix plays a role in Abeta fibril kinetics and morphology.
abstract: While neuronal membranes are proposed to be the primary target of amyloid plaques, the effect of phospholipids on fibril formation kinetics and morphology has not yet been resolved. We report that interaction of various compositions with neuronal mimics promoted different processes of fibril formation: negatively charged surfaces increased the lag time and elongation rate in thioflavin T assays, while brain total lipid extract had an opposite effect compared to that in the absence of lipid. Electron microscopy showed thin and elongated fibrils when the peptide was incubated with anionic lipids, while neutral surfaces promoted coarse and small fibrils. Circular dichroism and thioflavin T assays confirmed an initially unstructured peptide, and measured its transition to an aggregated beta-sheet conformation.
authors.affiliation: School of Chemistry, Bio21 Institute, University of Melbourne, VIC 3010, Australia.
authors.forename: Marc-Antoine
authors.initials: MA
authors.lastname: Sani
authors.forename: John D
authors.initials: JD
authors.lastname: Gehman
authors.forename: Frances
authors.initials: F
authors.lastname: Separovic
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000648:ultrastructure*; D002942:Circular Dichroism; D007700:Kinetics; D008055:Lipids / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012996:Solutions; D013997:Time Factors; D053835:Unilamellar Liposomes / Q000737:chemistry
chemical_list: D016229:Amyloid beta-Peptides; D008055:Lipids; D012996:Solutions; D053835:Unilamellar Liposomes