11 research outputs found

    Changes in lipid membranes may trigger amyloid toxicity in Alzheimer's disease - Fig 2

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    <p><b>Ion currents observed across the membrane: healthy model (A), D1 model (B), and D2 model (C).</b> Lipid membranes were suspended between symmetric aqueous solutions of 150 mM NaCl, 2 mM CaCl<sub>2</sub>, 10 mM Tris pH 7.4. The left panel for each section shows average current at the voltage amplitude of 50 mV under control conditions (no additions), in 5 min after induction of conductance by the Aβ, in 15 min after induction of conductance by the Aβ. Representative currents at 50 mV are shown in the right panel. * indicates significantly lower current.</p

    Complex lipid models mimicking healthy and AD neuronal membranes.

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    <p>Lipid mixtures are all comprised of the same components but differ in their ratios (by weight) based on documented changes in membrane composition as a result of AD.</p

    Schematic of Aβ interacting with a model membrane (not to scale).

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    <p>Arrangement of lipids present model bilayer system and phase separation leads to membrane nonhomogeneity, i.e., the presence of nanodomains, both topographical (Δh) and electrostatic (ΔV).</p

    Properties of lipids studied.

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    <p>This table outlines information about the five constituents of the models studied: DPPC, POPC, SM, Chol, and GM1. Phospholipid phase at ambient room temperature is indicated as samples were studied under these conditions. Dipole moment value is included due to its relevance in the KPFM study portion of this work.</p

    Comparison of monolayer topography and electrical surface potential for three models.

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    <p>AFM topography (in gold) and KPFM electrical surface potential (in blue) images are shown for healthy (A/D), diseased: D1 (B/E), and D2 (C/F) model systems in monolayer form. Samples were deposited and studied at ambient room temperature (22°C).</p

    High resolution images of AFM topography of Aß aggregates formed on modified surfaces: CH<sub>3</sub>- (A–C), COOH- (D–F), and NH<sub>2</sub>- (G–I) modified surfaces, after incubation with Aβ (1–42) solution (500 µg/ml) for 1 hour at 37°C.

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    <p>High resolution images of AFM topography of Aß aggregates formed on modified surfaces: CH<sub>3</sub>- (A–C), COOH- (D–F), and NH<sub>2</sub>- (G–I) modified surfaces, after incubation with Aβ (1–42) solution (500 µg/ml) for 1 hour at 37°C.</p

    Summary of results.

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    <p>AFM/KPFM study on topographical and electrical surface potential features of the models in monolayer form; Black Lipid Membrane analysis on the permeability of each model and the effect of Aβ on this conductance; and AFM liquid imaging of Aβ accumulation over time on each model membrane.</p

    AFM topography images (5×5 µm) of the amyloid fibrils formed on CH<sub>3</sub>, NH<sub>2</sub>, and COOH –modified surfaces.

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    <p>Aß peptide solution was incubated for 22 hours at 37°C on: (A) CH<sub>3</sub>-, (B) NH<sub>2</sub>-, and (C) COOH-modified surfaces.</p

    Statistical analysis of Aß small aggregates shown in <b>figure 3</b>.

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    <p>Histograms of aggregate unit area size (A, C, E) and height of each aggregate (B, D, F) for each surface type; (Red) CH<sub>3</sub>-modified surface; (green) COOH-modified surface; (blue) NH<sub>2</sub>-modified surface.</p
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