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- W2016473952 abstract "Significance The proper functioning of multilayer membrane systems, such as myelin, requires the multilamellar membranes to be tightly wrapped around the axon fibers, thereby allowing efficient electric signal transmission. Slight changes in lipid composition in myelin membranes will alter their domain sizes and distributions, and the intermembrane adhesive properties. Using the surface forces apparatus and atomic force microscope, we studied the adsorption of myelin basic protein (MBP) to model myelin lipid bilayer membranes of varying compositions, and their effects on the structure, equilibrium spacing (swelling), and adhesion force between them. We find that MBP preferentially adsorbs to “disordered” submicron domains, affecting regular spacing and adhesion. These findings provide insights into lipid–protein interactions and membrane-associated (e.g., demyelinating) diseases." @default.
- W2016473952 created "2016-06-24" @default.
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- W2016473952 date "2014-02-10" @default.
- W2016473952 modified "2023-10-14" @default.
- W2016473952 title "Lipid domains control myelin basic protein adsorption and membrane interactions between model myelin lipid bilayers" @default.
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- W2016473952 doi "https://doi.org/10.1073/pnas.1401165111" @default.
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