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    Differing modes of interaction between monomeric A1–40 peptides and model lipid membranes: an AFM study


    Sheikh, Khizar and Giordani, Cristiano and McManus, Jennifer J. and Bruun Hovgaard, Mads and Jarvis, Suzanne P. (2012) Differing modes of interaction between monomeric A1–40 peptides and model lipid membranes: an AFM study. Chemistry and Physics of Lipids, 165 (2). pp. 142-150. ISSN 0009-3084

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    Abstract

    Membrane interactions with -amyloid peptides are implicated in the pathology of Alzheimer’s disease and cholesterol has been shown to be key modulator of this interaction, yet little is known about the mechanism of this interaction. Using atomic force microscopy, we investigated the interaction of monomeric A1–40 peptides with planar mica-supported bilayers composed of DOPC and DPPC containing varying concentrations of cholesterol. We show that below the bilayer melting temperature, A monomers adsorb to, and assemble on, the surface of DPPC bilayers to form layers that grow laterally and normal to the bilayer plane. Above the bilayer melting temperature, we observe protofibril formation. In contrast, in DOPC bilayers, A monomers exhibit a detergent-like action, forming defects in the bilayer structure. The kinetics of both modes of interaction significantly increases with increasing membrane cholesterol content. We conclude that the mode and rate of the interaction of A monomers with lipid bilayers are strongly dependent on lipid composition, phase state and cholesterol content

    Item Type: Article
    Additional Information: The definitive version of this article is available at doi:10.1016/j.chemphyslip.2011.11.011
    Keywords: β Amyloid peptide; Atomic force microscopy; Model phospholipid membranes; DOPC; DPPC; Cholesterol;
    Academic Unit: Faculty of Science and Engineering > Chemistry
    Item ID: 4286
    Depositing User: Jennifer McManus
    Date Deposited: 03 Apr 2013 16:08
    Journal or Publication Title: Chemistry and Physics of Lipids
    Publisher: Elsevier
    Refereed: Yes
    URI:

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