Differing modes of interaction between monomeric Aβ1–40 peptides and model lipid membranes: an AFM study
Autor: | Suzanne P. Jarvis, Jennifer J. McManus, Cristiano Giordani, Mads Bruun Hovgaard, Khizar Sheikh |
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Rok vydání: | 2012 |
Předmět: |
1
2-Dipalmitoylphosphatidylcholine Lipid Bilayers Kinetics Microscopy Atomic Force 010402 general chemistry 01 natural sciences Biochemistry 03 medical and health sciences chemistry.chemical_compound Adsorption Alzheimer Disease Humans Lipid bilayer phase behavior Lipid bilayer Molecular Biology 030304 developmental biology 0303 health sciences Amyloid beta-Peptides Cholesterol Bilayer Organic Chemistry Cell Biology Peptide Fragments 0104 chemical sciences Chemistry Crystallography Monomer Membrane chemistry Phosphatidylcholines lipids (amino acids peptides and proteins) |
Zdroj: | Chemistry and Physics of Lipids. 165:142-150 |
ISSN: | 0009-3084 |
DOI: | 10.1016/j.chemphyslip.2011.11.011 |
Popis: | Membrane interactions with β-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 Aβ1–40 peptides with planar mica-supported bilayers composed of DOPC and DPPC containing varying concentrations of cholesterol. We show that below the bilayer melting temperature, Aβ 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, Aβ 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 Aβ monomers with lipid bilayers are strongly dependent on lipid composition, phase state and cholesterol content. |
Databáze: | OpenAIRE |
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