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myelin membrane dopc bsm dope pi dops cholesterol  (Avanti Polar)


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    Avanti Polar myelin membrane dopc bsm dope pi dops cholesterol
    a) GUVs labeled with Rhodamine PE (red channel) were incubated with Aβ-40 doped with Hylite-488 Aβ-40 (green channel) to monitor binding of the peptide within 1 hour (early phase). Early binding of Aβ-40 was observed in the case of PI, DOPG, <t>DOPC/BSM,</t> and DOPC/PIP2 membrane. No binding of Aβ-40 seen on <t>DOPS</t> and <t>DOPC/DOPE</t> membranes. b) Average fluorescence binding intensity of Aβ-40 on membranes with different head groups. The number of GUVs screened for each condition in the box plots is n= 35 from three independent experiments. The symbol **** indicates p values of ≤ 0.0001, calculated by one-way ANOVA followed by Bonferroni’s multiple comparison test. c) ThT fluorescence assay to monitor the effect of lipid head groups on the aggregation kinetics of Aβ-40. d) Effect of lipid head groups on the growth rate of Aβ-40 aggregation quantified within in the early phase of aggregation time scales i.e., 30 minutes). e) Effect of lipid head groups on the sustained aggregation of Aβ-40 during the late phase (saturation phase) of aggregation kinetics, i.e., 6 hours). +/- refer to the net charge on the membrane (i.e, negative or zwitterionic). The scale bar for confocal microscopy images is 10 μm.
    Myelin Membrane Dopc Bsm Dope Pi Dops Cholesterol, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 99/100, based on 7889 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/myelin+membrane/bio_rxiv__2021__08__13__456302-245-41-33?v=Avanti+Polar
    Average 99 stars, based on 7889 article reviews
    myelin membrane dopc bsm dope pi dops cholesterol - by Bioz Stars, 2026-08
    99/100 stars

    Images

    1) Product Images from "In vitro reconstitution demonstrates the amyloid-beta mediated myelin membrane deformation"

    Article Title: In vitro reconstitution demonstrates the amyloid-beta mediated myelin membrane deformation

    Journal: bioRxiv

    doi: 10.1101/2021.08.13.456302

    a) GUVs labeled with Rhodamine PE (red channel) were incubated with Aβ-40 doped with Hylite-488 Aβ-40 (green channel) to monitor binding of the peptide within 1 hour (early phase). Early binding of Aβ-40 was observed in the case of PI, DOPG, DOPC/BSM, and DOPC/PIP2 membrane. No binding of Aβ-40 seen on DOPS and DOPC/DOPE membranes. b) Average fluorescence binding intensity of Aβ-40 on membranes with different head groups. The number of GUVs screened for each condition in the box plots is n= 35 from three independent experiments. The symbol **** indicates p values of ≤ 0.0001, calculated by one-way ANOVA followed by Bonferroni’s multiple comparison test. c) ThT fluorescence assay to monitor the effect of lipid head groups on the aggregation kinetics of Aβ-40. d) Effect of lipid head groups on the growth rate of Aβ-40 aggregation quantified within in the early phase of aggregation time scales i.e., 30 minutes). e) Effect of lipid head groups on the sustained aggregation of Aβ-40 during the late phase (saturation phase) of aggregation kinetics, i.e., 6 hours). +/- refer to the net charge on the membrane (i.e, negative or zwitterionic). The scale bar for confocal microscopy images is 10 μm.
    Figure Legend Snippet: a) GUVs labeled with Rhodamine PE (red channel) were incubated with Aβ-40 doped with Hylite-488 Aβ-40 (green channel) to monitor binding of the peptide within 1 hour (early phase). Early binding of Aβ-40 was observed in the case of PI, DOPG, DOPC/BSM, and DOPC/PIP2 membrane. No binding of Aβ-40 seen on DOPS and DOPC/DOPE membranes. b) Average fluorescence binding intensity of Aβ-40 on membranes with different head groups. The number of GUVs screened for each condition in the box plots is n= 35 from three independent experiments. The symbol **** indicates p values of ≤ 0.0001, calculated by one-way ANOVA followed by Bonferroni’s multiple comparison test. c) ThT fluorescence assay to monitor the effect of lipid head groups on the aggregation kinetics of Aβ-40. d) Effect of lipid head groups on the growth rate of Aβ-40 aggregation quantified within in the early phase of aggregation time scales i.e., 30 minutes). e) Effect of lipid head groups on the sustained aggregation of Aβ-40 during the late phase (saturation phase) of aggregation kinetics, i.e., 6 hours). +/- refer to the net charge on the membrane (i.e, negative or zwitterionic). The scale bar for confocal microscopy images is 10 μm.

    Techniques Used: Labeling, Incubation, Binding Assay, Fluorescence, Confocal Microscopy

    a) GUVs of DOPC lipid doped with 1% Rhodamine PE (Red channel) incubated with Aβ-40 doped with Hylite-488 Aβ-40 (Green channel) and monitored temporally at 1, 4, 12 and 24 hours for changes in binding intensity. Tube profile was extracted at the 24-hour time point to visualize the deformations induced by Aβ-40 over time. b) Box plot showing weak to no binding of Aβ-40 to the DOPC GUV population observed at an early time point (1 hour), whereas, at later time points the binding increased and reached a plateau. c) Temporal monitoring of GUVs of DOPC/BSM/Chol lipid in the ratio 4:4:2 doped with 1% Rhodamine PE (Red channel) and incubated with Aβ-40 doped with Hylite-488 Aβ-40 (Green channel) at 1, 4, 12 and 24 hours for changes in binding intensity. The tube profile was extracted at the 24 hour time point to visualize the deformations induced by Aβ-40 over time. d) No binding was seen at the early time point (1 hour) for the DOPC/BSM/Chol (4:4:2) GUV population, with a steady rise in intensity at later time points. e) GUVs of DOPC/BSM/Chol/PIP 2 lipids in the ratio 2:4:3:1 doped with 1% Rhodamine PE (Red channel) incubated with Aβ-40 doped with Hylite-488 Aβ-40 (Green channel) and monitored temporally at 1, 4, 12 and 24 hours for changes in binding intensity. The tube profile was extracted at the 24-hour time point to visualize the deformations induced by Aβ-40 over time. f) Box Plot of the binding intensity of Aβ-40 to the GUV population of DOPC/BSM/Chol/PIP 2 (2:4:3:1) showing a strong early binding sustained till longer time points. g) Temporal monitoring of DOPC/BSM/Chol/DOPG (2:4:3:1) GUVs doped with 1% Rhodamine PE (Red channel) incubated with Aβ-40 doped with Hylite-488 Aβ-40 (Green channel) at 4 and 24 hours showed no binding at early and late time points. The number of GUVs screened at each time point for each condition in the box plots is n= 35 from three independent experiments. The symbols *, **, ***, **** indicate p values of ≤ 0.05, 0.01, 0.001, 0.0001, respectively, calculated by one-way ANOVA followed by Bonferroni’s multiple comparison test. The scale bar for confocal microscopy images is 10 μm.
    Figure Legend Snippet: a) GUVs of DOPC lipid doped with 1% Rhodamine PE (Red channel) incubated with Aβ-40 doped with Hylite-488 Aβ-40 (Green channel) and monitored temporally at 1, 4, 12 and 24 hours for changes in binding intensity. Tube profile was extracted at the 24-hour time point to visualize the deformations induced by Aβ-40 over time. b) Box plot showing weak to no binding of Aβ-40 to the DOPC GUV population observed at an early time point (1 hour), whereas, at later time points the binding increased and reached a plateau. c) Temporal monitoring of GUVs of DOPC/BSM/Chol lipid in the ratio 4:4:2 doped with 1% Rhodamine PE (Red channel) and incubated with Aβ-40 doped with Hylite-488 Aβ-40 (Green channel) at 1, 4, 12 and 24 hours for changes in binding intensity. The tube profile was extracted at the 24 hour time point to visualize the deformations induced by Aβ-40 over time. d) No binding was seen at the early time point (1 hour) for the DOPC/BSM/Chol (4:4:2) GUV population, with a steady rise in intensity at later time points. e) GUVs of DOPC/BSM/Chol/PIP 2 lipids in the ratio 2:4:3:1 doped with 1% Rhodamine PE (Red channel) incubated with Aβ-40 doped with Hylite-488 Aβ-40 (Green channel) and monitored temporally at 1, 4, 12 and 24 hours for changes in binding intensity. The tube profile was extracted at the 24-hour time point to visualize the deformations induced by Aβ-40 over time. f) Box Plot of the binding intensity of Aβ-40 to the GUV population of DOPC/BSM/Chol/PIP 2 (2:4:3:1) showing a strong early binding sustained till longer time points. g) Temporal monitoring of DOPC/BSM/Chol/DOPG (2:4:3:1) GUVs doped with 1% Rhodamine PE (Red channel) incubated with Aβ-40 doped with Hylite-488 Aβ-40 (Green channel) at 4 and 24 hours showed no binding at early and late time points. The number of GUVs screened at each time point for each condition in the box plots is n= 35 from three independent experiments. The symbols *, **, ***, **** indicate p values of ≤ 0.05, 0.01, 0.001, 0.0001, respectively, calculated by one-way ANOVA followed by Bonferroni’s multiple comparison test. The scale bar for confocal microscopy images is 10 μm.

    Techniques Used: Incubation, Binding Assay, Confocal Microscopy

    a) An illustration to provide a lateral view of shallow, deep, and no defects at the membrane surface. b) Histogram of the defect constant for deep, shallow, and all (both deep and shallow defects) defects for each of the four conditions, namely, DOPC (red), DOPC/BSM/Chol (green), DOPC/BSM/Chol/PIP 2 (blue), Myelin membrane (cyan).
    Figure Legend Snippet: a) An illustration to provide a lateral view of shallow, deep, and no defects at the membrane surface. b) Histogram of the defect constant for deep, shallow, and all (both deep and shallow defects) defects for each of the four conditions, namely, DOPC (red), DOPC/BSM/Chol (green), DOPC/BSM/Chol/PIP 2 (blue), Myelin membrane (cyan).

    Techniques Used:

    Representative images of GUVs of DOPC/BSM/Chol/PIP 2 (2:4:3:1) membrane without Aβ-40 at respective time points. Scale bar is 10 μm.
    Figure Legend Snippet: Representative images of GUVs of DOPC/BSM/Chol/PIP 2 (2:4:3:1) membrane without Aβ-40 at respective time points. Scale bar is 10 μm.

    Techniques Used:

    Steady-state anisotropy measurements were performed on different membrane conditions that include membranes with variable DOPC/BSM content keeping cholesterol constant (2:6:2, 4:4:2, 6:2:2), along with single lipid membrane compositions like DOPC, BSM, LPI, DPPC, and multicomponent membranes of myelin and DOPC/BSM/Chol/PIP 2 incubated with Aβ-40. Controls without Aβ-40 for each membrane condition were normalized to 100, denoted by the horizontal red line traversing the plot. The data shown represent the ± SEM extracted from three independent experiments.
    Figure Legend Snippet: Steady-state anisotropy measurements were performed on different membrane conditions that include membranes with variable DOPC/BSM content keeping cholesterol constant (2:6:2, 4:4:2, 6:2:2), along with single lipid membrane compositions like DOPC, BSM, LPI, DPPC, and multicomponent membranes of myelin and DOPC/BSM/Chol/PIP 2 incubated with Aβ-40. Controls without Aβ-40 for each membrane condition were normalized to 100, denoted by the horizontal red line traversing the plot. The data shown represent the ± SEM extracted from three independent experiments.

    Techniques Used: Incubation

    a) Representative fluorescence recovery after photobleaching (FRAP) images of the green channel (Aβ-40 doped with Hylite-488 Aβ-40) showing the Pre-bleach, bleach, and Recovery of the three conditions (DOPC/BSM/Chol (4:4:2), DOPC/BSM/Chol/PIP 2 (2:4:3:1) and Myelin membrane) marked with a white circle to denote the region of interest in each case at the 12 hour time point. b) Normalized fluorescence recovery curves after photobleaching for Aβ-40 bound (green channel - peptide) to the above mentioned three membrane conditions at the 12-hour time point. c) Normalized fluorescence recovery curves after photobleaching for Aβ-40 bound (red channel – lipid membrane) to the above mentioned three membrane conditions at the 12-hour time point. d) Representative fluorescence recovery after photobleaching (FRAP) images of the green channel (Aβ-40 doped with Hylite-488 Aβ-40) showing the Pre-bleach, bleach, and Recovery of the three conditions (DOPC/BSM/Chol (4:4:2), DOPC/BSM/Chol/PIP 2 (2:4:3:1) and Myelin membrane) marked with a white circle to denote the region of interest in each case at the 24 hour time point. e) Normalized fluorescence recovery curves after photobleaching for Aβ-40 bound (green channel - peptide) to the above mentioned three membrane conditions at the 24-hour time point. f) Normalized fluorescence recovery curves after photobleaching for Aβ-40 bound (red channel – lipid membrane) to the above mentioned three membrane conditions at the 24-hour time point. All FRAP curves in black lines are for DOPC/BSM/Chol (4:4:2), red lines are for DOPC/BSM/Chol/PIP 2 (2:4:3:1), and blue lines represent curves for the myelin membrane. Each curve is a mean of 5 independent experiments. The scale bar for FRAP images is 10 μm.
    Figure Legend Snippet: a) Representative fluorescence recovery after photobleaching (FRAP) images of the green channel (Aβ-40 doped with Hylite-488 Aβ-40) showing the Pre-bleach, bleach, and Recovery of the three conditions (DOPC/BSM/Chol (4:4:2), DOPC/BSM/Chol/PIP 2 (2:4:3:1) and Myelin membrane) marked with a white circle to denote the region of interest in each case at the 12 hour time point. b) Normalized fluorescence recovery curves after photobleaching for Aβ-40 bound (green channel - peptide) to the above mentioned three membrane conditions at the 12-hour time point. c) Normalized fluorescence recovery curves after photobleaching for Aβ-40 bound (red channel – lipid membrane) to the above mentioned three membrane conditions at the 12-hour time point. d) Representative fluorescence recovery after photobleaching (FRAP) images of the green channel (Aβ-40 doped with Hylite-488 Aβ-40) showing the Pre-bleach, bleach, and Recovery of the three conditions (DOPC/BSM/Chol (4:4:2), DOPC/BSM/Chol/PIP 2 (2:4:3:1) and Myelin membrane) marked with a white circle to denote the region of interest in each case at the 24 hour time point. e) Normalized fluorescence recovery curves after photobleaching for Aβ-40 bound (green channel - peptide) to the above mentioned three membrane conditions at the 24-hour time point. f) Normalized fluorescence recovery curves after photobleaching for Aβ-40 bound (red channel – lipid membrane) to the above mentioned three membrane conditions at the 24-hour time point. All FRAP curves in black lines are for DOPC/BSM/Chol (4:4:2), red lines are for DOPC/BSM/Chol/PIP 2 (2:4:3:1), and blue lines represent curves for the myelin membrane. Each curve is a mean of 5 independent experiments. The scale bar for FRAP images is 10 μm.

    Techniques Used: Fluorescence

    a) Illustration of a typical surface pressure ( π )– mean molecular area ( A ) isotherm with a visual representation of the molecular alignment of the lipid molecules at different phases of the isotherm. b) π - A isotherm for the different membrane conditions that include myelin membrane with and without Aβ-40 (blue and light blue), DOPC/BSM/Chol/PIP2 (2:4:3:1) membrane with and without Aβ-40 (green and light green), DOPC/BSM/Chol (4:4:2) membrane with and without Aβ-40 (pink and light pink) DOPC/BSM/Chol (3:3:4) membrane with and without Aβ-40 (orange and beige) at 25°C. c) Compressibility modulus ( C s -1 ) – surface pressure ( π ) curves for each control monolayer model as well as in the presence of Aβ-40 are shown in the graph following the same labelling order and color scheme for the membrane conditions as above. d) Compressibility moduli ( C s -1 ) at surface pressure of 30 mN/m (at the bilayer equivalence pressure) is shown in the graph with the same labelling order and color scheme for the membrane conditions as above. e) Surface pressure ( π )- Time plot for different membrane conditions that include myelin membrane (black line), DOPC/BSM/Chol/PIP2 (2:4:3:1) (red line), DOPC/BSM/Chol (5:5:0) (blue line), DOPC/BSM/Chol (4:4:2) (green line), DOPC/BSM/Chol (3:3:4) (purple line) at 25°C for 12 hours. f) Bending force (ΔF b ), a measure of deformability, of different membrane conditions is shown in the histogram.
    Figure Legend Snippet: a) Illustration of a typical surface pressure ( π )– mean molecular area ( A ) isotherm with a visual representation of the molecular alignment of the lipid molecules at different phases of the isotherm. b) π - A isotherm for the different membrane conditions that include myelin membrane with and without Aβ-40 (blue and light blue), DOPC/BSM/Chol/PIP2 (2:4:3:1) membrane with and without Aβ-40 (green and light green), DOPC/BSM/Chol (4:4:2) membrane with and without Aβ-40 (pink and light pink) DOPC/BSM/Chol (3:3:4) membrane with and without Aβ-40 (orange and beige) at 25°C. c) Compressibility modulus ( C s -1 ) – surface pressure ( π ) curves for each control monolayer model as well as in the presence of Aβ-40 are shown in the graph following the same labelling order and color scheme for the membrane conditions as above. d) Compressibility moduli ( C s -1 ) at surface pressure of 30 mN/m (at the bilayer equivalence pressure) is shown in the graph with the same labelling order and color scheme for the membrane conditions as above. e) Surface pressure ( π )- Time plot for different membrane conditions that include myelin membrane (black line), DOPC/BSM/Chol/PIP2 (2:4:3:1) (red line), DOPC/BSM/Chol (5:5:0) (blue line), DOPC/BSM/Chol (4:4:2) (green line), DOPC/BSM/Chol (3:3:4) (purple line) at 25°C for 12 hours. f) Bending force (ΔF b ), a measure of deformability, of different membrane conditions is shown in the histogram.

    Techniques Used:



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    95
    Avanti Polar myelin membrane
    Useful antibodies to characterize human Schwann cells (hSCs) and non-glial cells established in cell culture. These antibodies were validated using traditional adult nerve-derived hSC monocultures. Staining with NGFR, Sox10, and S100B antibodies, alone or together with fibronectin, SMA (α-smooth muscle actin), and FAP (fibroblast activation protein/seprase) antibodies, is recommended for the initial characterization of hSCs and non-glial cells. We have not found a ubiquitous non-glial cell marker. Protocol 1C is suitable for staining with all antibodies except for anti-O1 and anti-O4, which can be accomplished only in live cells (Protocol 1B). A 1:200–1:500 starting dilution is suitable for most antibodies; the optimal concentration should be determined by the end user in the target cells. (*) Indicates that the antibodies are produced from hybridoma cell lines. MBP: myelin basic protein; MAG: myelin-associated glycoprotein; MPZ: myelin protein zero; GFAP: glial fibrillary acidic protein.
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    a) GUVs labeled with Rhodamine PE (red channel) were incubated with Aβ-40 doped with Hylite-488 Aβ-40 (green channel) to monitor binding of the peptide within 1 hour (early phase). Early binding of Aβ-40 was observed in the case of PI, DOPG, DOPC/BSM, and DOPC/PIP2 membrane. No binding of Aβ-40 seen on DOPS and DOPC/DOPE membranes. b) Average fluorescence binding intensity of Aβ-40 on membranes with different head groups. The number of GUVs screened for each condition in the box plots is n= 35 from three independent experiments. The symbol **** indicates p values of ≤ 0.0001, calculated by one-way ANOVA followed by Bonferroni’s multiple comparison test. c) ThT fluorescence assay to monitor the effect of lipid head groups on the aggregation kinetics of Aβ-40. d) Effect of lipid head groups on the growth rate of Aβ-40 aggregation quantified within in the early phase of aggregation time scales i.e., 30 minutes). e) Effect of lipid head groups on the sustained aggregation of Aβ-40 during the late phase (saturation phase) of aggregation kinetics, i.e., 6 hours). +/- refer to the net charge on the membrane (i.e, negative or zwitterionic). The scale bar for confocal microscopy images is 10 μm.

    Journal: bioRxiv

    Article Title: In vitro reconstitution demonstrates the amyloid-beta mediated myelin membrane deformation

    doi: 10.1101/2021.08.13.456302

    Figure Lengend Snippet: a) GUVs labeled with Rhodamine PE (red channel) were incubated with Aβ-40 doped with Hylite-488 Aβ-40 (green channel) to monitor binding of the peptide within 1 hour (early phase). Early binding of Aβ-40 was observed in the case of PI, DOPG, DOPC/BSM, and DOPC/PIP2 membrane. No binding of Aβ-40 seen on DOPS and DOPC/DOPE membranes. b) Average fluorescence binding intensity of Aβ-40 on membranes with different head groups. The number of GUVs screened for each condition in the box plots is n= 35 from three independent experiments. The symbol **** indicates p values of ≤ 0.0001, calculated by one-way ANOVA followed by Bonferroni’s multiple comparison test. c) ThT fluorescence assay to monitor the effect of lipid head groups on the aggregation kinetics of Aβ-40. d) Effect of lipid head groups on the growth rate of Aβ-40 aggregation quantified within in the early phase of aggregation time scales i.e., 30 minutes). e) Effect of lipid head groups on the sustained aggregation of Aβ-40 during the late phase (saturation phase) of aggregation kinetics, i.e., 6 hours). +/- refer to the net charge on the membrane (i.e, negative or zwitterionic). The scale bar for confocal microscopy images is 10 μm.

    Article Snippet: 1,2-Dioleoyl-sn-glycero-3-phosphocholine (DOPC), 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE), L-α-phosphatidylinositol (liver PI), 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), 1,2-dioleoyl-sn-glycero-3-phospho-Lserine (DOPS) 1,2-dioleoyl-sn-glycero-3-phospho-(1′-rac-glycerol) (DOPG), L-α-phosphatidylinositol-4,5-bisphosphate (PIP2), sphingomyelin (Brain, Porcine) (BSM), L-α-phosphatidylinositol-4,5-bisphosphate (Brain, Porcine), 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-(lissamine rhodamine B sulfonyl) (Rhod PE) and cholesterol were purchased from (Avanti Polar Lipids, Alabaster, Alabama, U.S.A.) Composition of myelin membrane - DOPC/BSM/DOPE/PI/DOPS/Cholesterol (4:3:1:1:0.4:0.6).

    Techniques: Labeling, Incubation, Binding Assay, Fluorescence, Confocal Microscopy

    a) GUVs of DOPC lipid doped with 1% Rhodamine PE (Red channel) incubated with Aβ-40 doped with Hylite-488 Aβ-40 (Green channel) and monitored temporally at 1, 4, 12 and 24 hours for changes in binding intensity. Tube profile was extracted at the 24-hour time point to visualize the deformations induced by Aβ-40 over time. b) Box plot showing weak to no binding of Aβ-40 to the DOPC GUV population observed at an early time point (1 hour), whereas, at later time points the binding increased and reached a plateau. c) Temporal monitoring of GUVs of DOPC/BSM/Chol lipid in the ratio 4:4:2 doped with 1% Rhodamine PE (Red channel) and incubated with Aβ-40 doped with Hylite-488 Aβ-40 (Green channel) at 1, 4, 12 and 24 hours for changes in binding intensity. The tube profile was extracted at the 24 hour time point to visualize the deformations induced by Aβ-40 over time. d) No binding was seen at the early time point (1 hour) for the DOPC/BSM/Chol (4:4:2) GUV population, with a steady rise in intensity at later time points. e) GUVs of DOPC/BSM/Chol/PIP 2 lipids in the ratio 2:4:3:1 doped with 1% Rhodamine PE (Red channel) incubated with Aβ-40 doped with Hylite-488 Aβ-40 (Green channel) and monitored temporally at 1, 4, 12 and 24 hours for changes in binding intensity. The tube profile was extracted at the 24-hour time point to visualize the deformations induced by Aβ-40 over time. f) Box Plot of the binding intensity of Aβ-40 to the GUV population of DOPC/BSM/Chol/PIP 2 (2:4:3:1) showing a strong early binding sustained till longer time points. g) Temporal monitoring of DOPC/BSM/Chol/DOPG (2:4:3:1) GUVs doped with 1% Rhodamine PE (Red channel) incubated with Aβ-40 doped with Hylite-488 Aβ-40 (Green channel) at 4 and 24 hours showed no binding at early and late time points. The number of GUVs screened at each time point for each condition in the box plots is n= 35 from three independent experiments. The symbols *, **, ***, **** indicate p values of ≤ 0.05, 0.01, 0.001, 0.0001, respectively, calculated by one-way ANOVA followed by Bonferroni’s multiple comparison test. The scale bar for confocal microscopy images is 10 μm.

    Journal: bioRxiv

    Article Title: In vitro reconstitution demonstrates the amyloid-beta mediated myelin membrane deformation

    doi: 10.1101/2021.08.13.456302

    Figure Lengend Snippet: a) GUVs of DOPC lipid doped with 1% Rhodamine PE (Red channel) incubated with Aβ-40 doped with Hylite-488 Aβ-40 (Green channel) and monitored temporally at 1, 4, 12 and 24 hours for changes in binding intensity. Tube profile was extracted at the 24-hour time point to visualize the deformations induced by Aβ-40 over time. b) Box plot showing weak to no binding of Aβ-40 to the DOPC GUV population observed at an early time point (1 hour), whereas, at later time points the binding increased and reached a plateau. c) Temporal monitoring of GUVs of DOPC/BSM/Chol lipid in the ratio 4:4:2 doped with 1% Rhodamine PE (Red channel) and incubated with Aβ-40 doped with Hylite-488 Aβ-40 (Green channel) at 1, 4, 12 and 24 hours for changes in binding intensity. The tube profile was extracted at the 24 hour time point to visualize the deformations induced by Aβ-40 over time. d) No binding was seen at the early time point (1 hour) for the DOPC/BSM/Chol (4:4:2) GUV population, with a steady rise in intensity at later time points. e) GUVs of DOPC/BSM/Chol/PIP 2 lipids in the ratio 2:4:3:1 doped with 1% Rhodamine PE (Red channel) incubated with Aβ-40 doped with Hylite-488 Aβ-40 (Green channel) and monitored temporally at 1, 4, 12 and 24 hours for changes in binding intensity. The tube profile was extracted at the 24-hour time point to visualize the deformations induced by Aβ-40 over time. f) Box Plot of the binding intensity of Aβ-40 to the GUV population of DOPC/BSM/Chol/PIP 2 (2:4:3:1) showing a strong early binding sustained till longer time points. g) Temporal monitoring of DOPC/BSM/Chol/DOPG (2:4:3:1) GUVs doped with 1% Rhodamine PE (Red channel) incubated with Aβ-40 doped with Hylite-488 Aβ-40 (Green channel) at 4 and 24 hours showed no binding at early and late time points. The number of GUVs screened at each time point for each condition in the box plots is n= 35 from three independent experiments. The symbols *, **, ***, **** indicate p values of ≤ 0.05, 0.01, 0.001, 0.0001, respectively, calculated by one-way ANOVA followed by Bonferroni’s multiple comparison test. The scale bar for confocal microscopy images is 10 μm.

    Article Snippet: 1,2-Dioleoyl-sn-glycero-3-phosphocholine (DOPC), 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE), L-α-phosphatidylinositol (liver PI), 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), 1,2-dioleoyl-sn-glycero-3-phospho-Lserine (DOPS) 1,2-dioleoyl-sn-glycero-3-phospho-(1′-rac-glycerol) (DOPG), L-α-phosphatidylinositol-4,5-bisphosphate (PIP2), sphingomyelin (Brain, Porcine) (BSM), L-α-phosphatidylinositol-4,5-bisphosphate (Brain, Porcine), 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-(lissamine rhodamine B sulfonyl) (Rhod PE) and cholesterol were purchased from (Avanti Polar Lipids, Alabaster, Alabama, U.S.A.) Composition of myelin membrane - DOPC/BSM/DOPE/PI/DOPS/Cholesterol (4:3:1:1:0.4:0.6).

    Techniques: Incubation, Binding Assay, Confocal Microscopy

    a) An illustration to provide a lateral view of shallow, deep, and no defects at the membrane surface. b) Histogram of the defect constant for deep, shallow, and all (both deep and shallow defects) defects for each of the four conditions, namely, DOPC (red), DOPC/BSM/Chol (green), DOPC/BSM/Chol/PIP 2 (blue), Myelin membrane (cyan).

    Journal: bioRxiv

    Article Title: In vitro reconstitution demonstrates the amyloid-beta mediated myelin membrane deformation

    doi: 10.1101/2021.08.13.456302

    Figure Lengend Snippet: a) An illustration to provide a lateral view of shallow, deep, and no defects at the membrane surface. b) Histogram of the defect constant for deep, shallow, and all (both deep and shallow defects) defects for each of the four conditions, namely, DOPC (red), DOPC/BSM/Chol (green), DOPC/BSM/Chol/PIP 2 (blue), Myelin membrane (cyan).

    Article Snippet: 1,2-Dioleoyl-sn-glycero-3-phosphocholine (DOPC), 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE), L-α-phosphatidylinositol (liver PI), 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), 1,2-dioleoyl-sn-glycero-3-phospho-Lserine (DOPS) 1,2-dioleoyl-sn-glycero-3-phospho-(1′-rac-glycerol) (DOPG), L-α-phosphatidylinositol-4,5-bisphosphate (PIP2), sphingomyelin (Brain, Porcine) (BSM), L-α-phosphatidylinositol-4,5-bisphosphate (Brain, Porcine), 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-(lissamine rhodamine B sulfonyl) (Rhod PE) and cholesterol were purchased from (Avanti Polar Lipids, Alabaster, Alabama, U.S.A.) Composition of myelin membrane - DOPC/BSM/DOPE/PI/DOPS/Cholesterol (4:3:1:1:0.4:0.6).

    Techniques:

    Representative images of GUVs of DOPC/BSM/Chol/PIP 2 (2:4:3:1) membrane without Aβ-40 at respective time points. Scale bar is 10 μm.

    Journal: bioRxiv

    Article Title: In vitro reconstitution demonstrates the amyloid-beta mediated myelin membrane deformation

    doi: 10.1101/2021.08.13.456302

    Figure Lengend Snippet: Representative images of GUVs of DOPC/BSM/Chol/PIP 2 (2:4:3:1) membrane without Aβ-40 at respective time points. Scale bar is 10 μm.

    Article Snippet: 1,2-Dioleoyl-sn-glycero-3-phosphocholine (DOPC), 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE), L-α-phosphatidylinositol (liver PI), 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), 1,2-dioleoyl-sn-glycero-3-phospho-Lserine (DOPS) 1,2-dioleoyl-sn-glycero-3-phospho-(1′-rac-glycerol) (DOPG), L-α-phosphatidylinositol-4,5-bisphosphate (PIP2), sphingomyelin (Brain, Porcine) (BSM), L-α-phosphatidylinositol-4,5-bisphosphate (Brain, Porcine), 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-(lissamine rhodamine B sulfonyl) (Rhod PE) and cholesterol were purchased from (Avanti Polar Lipids, Alabaster, Alabama, U.S.A.) Composition of myelin membrane - DOPC/BSM/DOPE/PI/DOPS/Cholesterol (4:3:1:1:0.4:0.6).

    Techniques:

    Steady-state anisotropy measurements were performed on different membrane conditions that include membranes with variable DOPC/BSM content keeping cholesterol constant (2:6:2, 4:4:2, 6:2:2), along with single lipid membrane compositions like DOPC, BSM, LPI, DPPC, and multicomponent membranes of myelin and DOPC/BSM/Chol/PIP 2 incubated with Aβ-40. Controls without Aβ-40 for each membrane condition were normalized to 100, denoted by the horizontal red line traversing the plot. The data shown represent the ± SEM extracted from three independent experiments.

    Journal: bioRxiv

    Article Title: In vitro reconstitution demonstrates the amyloid-beta mediated myelin membrane deformation

    doi: 10.1101/2021.08.13.456302

    Figure Lengend Snippet: Steady-state anisotropy measurements were performed on different membrane conditions that include membranes with variable DOPC/BSM content keeping cholesterol constant (2:6:2, 4:4:2, 6:2:2), along with single lipid membrane compositions like DOPC, BSM, LPI, DPPC, and multicomponent membranes of myelin and DOPC/BSM/Chol/PIP 2 incubated with Aβ-40. Controls without Aβ-40 for each membrane condition were normalized to 100, denoted by the horizontal red line traversing the plot. The data shown represent the ± SEM extracted from three independent experiments.

    Article Snippet: 1,2-Dioleoyl-sn-glycero-3-phosphocholine (DOPC), 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE), L-α-phosphatidylinositol (liver PI), 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), 1,2-dioleoyl-sn-glycero-3-phospho-Lserine (DOPS) 1,2-dioleoyl-sn-glycero-3-phospho-(1′-rac-glycerol) (DOPG), L-α-phosphatidylinositol-4,5-bisphosphate (PIP2), sphingomyelin (Brain, Porcine) (BSM), L-α-phosphatidylinositol-4,5-bisphosphate (Brain, Porcine), 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-(lissamine rhodamine B sulfonyl) (Rhod PE) and cholesterol were purchased from (Avanti Polar Lipids, Alabaster, Alabama, U.S.A.) Composition of myelin membrane - DOPC/BSM/DOPE/PI/DOPS/Cholesterol (4:3:1:1:0.4:0.6).

    Techniques: Incubation

    a) Representative fluorescence recovery after photobleaching (FRAP) images of the green channel (Aβ-40 doped with Hylite-488 Aβ-40) showing the Pre-bleach, bleach, and Recovery of the three conditions (DOPC/BSM/Chol (4:4:2), DOPC/BSM/Chol/PIP 2 (2:4:3:1) and Myelin membrane) marked with a white circle to denote the region of interest in each case at the 12 hour time point. b) Normalized fluorescence recovery curves after photobleaching for Aβ-40 bound (green channel - peptide) to the above mentioned three membrane conditions at the 12-hour time point. c) Normalized fluorescence recovery curves after photobleaching for Aβ-40 bound (red channel – lipid membrane) to the above mentioned three membrane conditions at the 12-hour time point. d) Representative fluorescence recovery after photobleaching (FRAP) images of the green channel (Aβ-40 doped with Hylite-488 Aβ-40) showing the Pre-bleach, bleach, and Recovery of the three conditions (DOPC/BSM/Chol (4:4:2), DOPC/BSM/Chol/PIP 2 (2:4:3:1) and Myelin membrane) marked with a white circle to denote the region of interest in each case at the 24 hour time point. e) Normalized fluorescence recovery curves after photobleaching for Aβ-40 bound (green channel - peptide) to the above mentioned three membrane conditions at the 24-hour time point. f) Normalized fluorescence recovery curves after photobleaching for Aβ-40 bound (red channel – lipid membrane) to the above mentioned three membrane conditions at the 24-hour time point. All FRAP curves in black lines are for DOPC/BSM/Chol (4:4:2), red lines are for DOPC/BSM/Chol/PIP 2 (2:4:3:1), and blue lines represent curves for the myelin membrane. Each curve is a mean of 5 independent experiments. The scale bar for FRAP images is 10 μm.

    Journal: bioRxiv

    Article Title: In vitro reconstitution demonstrates the amyloid-beta mediated myelin membrane deformation

    doi: 10.1101/2021.08.13.456302

    Figure Lengend Snippet: a) Representative fluorescence recovery after photobleaching (FRAP) images of the green channel (Aβ-40 doped with Hylite-488 Aβ-40) showing the Pre-bleach, bleach, and Recovery of the three conditions (DOPC/BSM/Chol (4:4:2), DOPC/BSM/Chol/PIP 2 (2:4:3:1) and Myelin membrane) marked with a white circle to denote the region of interest in each case at the 12 hour time point. b) Normalized fluorescence recovery curves after photobleaching for Aβ-40 bound (green channel - peptide) to the above mentioned three membrane conditions at the 12-hour time point. c) Normalized fluorescence recovery curves after photobleaching for Aβ-40 bound (red channel – lipid membrane) to the above mentioned three membrane conditions at the 12-hour time point. d) Representative fluorescence recovery after photobleaching (FRAP) images of the green channel (Aβ-40 doped with Hylite-488 Aβ-40) showing the Pre-bleach, bleach, and Recovery of the three conditions (DOPC/BSM/Chol (4:4:2), DOPC/BSM/Chol/PIP 2 (2:4:3:1) and Myelin membrane) marked with a white circle to denote the region of interest in each case at the 24 hour time point. e) Normalized fluorescence recovery curves after photobleaching for Aβ-40 bound (green channel - peptide) to the above mentioned three membrane conditions at the 24-hour time point. f) Normalized fluorescence recovery curves after photobleaching for Aβ-40 bound (red channel – lipid membrane) to the above mentioned three membrane conditions at the 24-hour time point. All FRAP curves in black lines are for DOPC/BSM/Chol (4:4:2), red lines are for DOPC/BSM/Chol/PIP 2 (2:4:3:1), and blue lines represent curves for the myelin membrane. Each curve is a mean of 5 independent experiments. The scale bar for FRAP images is 10 μm.

    Article Snippet: 1,2-Dioleoyl-sn-glycero-3-phosphocholine (DOPC), 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE), L-α-phosphatidylinositol (liver PI), 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), 1,2-dioleoyl-sn-glycero-3-phospho-Lserine (DOPS) 1,2-dioleoyl-sn-glycero-3-phospho-(1′-rac-glycerol) (DOPG), L-α-phosphatidylinositol-4,5-bisphosphate (PIP2), sphingomyelin (Brain, Porcine) (BSM), L-α-phosphatidylinositol-4,5-bisphosphate (Brain, Porcine), 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-(lissamine rhodamine B sulfonyl) (Rhod PE) and cholesterol were purchased from (Avanti Polar Lipids, Alabaster, Alabama, U.S.A.) Composition of myelin membrane - DOPC/BSM/DOPE/PI/DOPS/Cholesterol (4:3:1:1:0.4:0.6).

    Techniques: Fluorescence

    a) Illustration of a typical surface pressure ( π )– mean molecular area ( A ) isotherm with a visual representation of the molecular alignment of the lipid molecules at different phases of the isotherm. b) π - A isotherm for the different membrane conditions that include myelin membrane with and without Aβ-40 (blue and light blue), DOPC/BSM/Chol/PIP2 (2:4:3:1) membrane with and without Aβ-40 (green and light green), DOPC/BSM/Chol (4:4:2) membrane with and without Aβ-40 (pink and light pink) DOPC/BSM/Chol (3:3:4) membrane with and without Aβ-40 (orange and beige) at 25°C. c) Compressibility modulus ( C s -1 ) – surface pressure ( π ) curves for each control monolayer model as well as in the presence of Aβ-40 are shown in the graph following the same labelling order and color scheme for the membrane conditions as above. d) Compressibility moduli ( C s -1 ) at surface pressure of 30 mN/m (at the bilayer equivalence pressure) is shown in the graph with the same labelling order and color scheme for the membrane conditions as above. e) Surface pressure ( π )- Time plot for different membrane conditions that include myelin membrane (black line), DOPC/BSM/Chol/PIP2 (2:4:3:1) (red line), DOPC/BSM/Chol (5:5:0) (blue line), DOPC/BSM/Chol (4:4:2) (green line), DOPC/BSM/Chol (3:3:4) (purple line) at 25°C for 12 hours. f) Bending force (ΔF b ), a measure of deformability, of different membrane conditions is shown in the histogram.

    Journal: bioRxiv

    Article Title: In vitro reconstitution demonstrates the amyloid-beta mediated myelin membrane deformation

    doi: 10.1101/2021.08.13.456302

    Figure Lengend Snippet: a) Illustration of a typical surface pressure ( π )– mean molecular area ( A ) isotherm with a visual representation of the molecular alignment of the lipid molecules at different phases of the isotherm. b) π - A isotherm for the different membrane conditions that include myelin membrane with and without Aβ-40 (blue and light blue), DOPC/BSM/Chol/PIP2 (2:4:3:1) membrane with and without Aβ-40 (green and light green), DOPC/BSM/Chol (4:4:2) membrane with and without Aβ-40 (pink and light pink) DOPC/BSM/Chol (3:3:4) membrane with and without Aβ-40 (orange and beige) at 25°C. c) Compressibility modulus ( C s -1 ) – surface pressure ( π ) curves for each control monolayer model as well as in the presence of Aβ-40 are shown in the graph following the same labelling order and color scheme for the membrane conditions as above. d) Compressibility moduli ( C s -1 ) at surface pressure of 30 mN/m (at the bilayer equivalence pressure) is shown in the graph with the same labelling order and color scheme for the membrane conditions as above. e) Surface pressure ( π )- Time plot for different membrane conditions that include myelin membrane (black line), DOPC/BSM/Chol/PIP2 (2:4:3:1) (red line), DOPC/BSM/Chol (5:5:0) (blue line), DOPC/BSM/Chol (4:4:2) (green line), DOPC/BSM/Chol (3:3:4) (purple line) at 25°C for 12 hours. f) Bending force (ΔF b ), a measure of deformability, of different membrane conditions is shown in the histogram.

    Article Snippet: 1,2-Dioleoyl-sn-glycero-3-phosphocholine (DOPC), 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE), L-α-phosphatidylinositol (liver PI), 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), 1,2-dioleoyl-sn-glycero-3-phospho-Lserine (DOPS) 1,2-dioleoyl-sn-glycero-3-phospho-(1′-rac-glycerol) (DOPG), L-α-phosphatidylinositol-4,5-bisphosphate (PIP2), sphingomyelin (Brain, Porcine) (BSM), L-α-phosphatidylinositol-4,5-bisphosphate (Brain, Porcine), 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-(lissamine rhodamine B sulfonyl) (Rhod PE) and cholesterol were purchased from (Avanti Polar Lipids, Alabaster, Alabama, U.S.A.) Composition of myelin membrane - DOPC/BSM/DOPE/PI/DOPS/Cholesterol (4:3:1:1:0.4:0.6).

    Techniques:

    Useful antibodies to characterize human Schwann cells (hSCs) and non-glial cells established in cell culture. These antibodies were validated using traditional adult nerve-derived hSC monocultures. Staining with NGFR, Sox10, and S100B antibodies, alone or together with fibronectin, SMA (α-smooth muscle actin), and FAP (fibroblast activation protein/seprase) antibodies, is recommended for the initial characterization of hSCs and non-glial cells. We have not found a ubiquitous non-glial cell marker. Protocol 1C is suitable for staining with all antibodies except for anti-O1 and anti-O4, which can be accomplished only in live cells (Protocol 1B). A 1:200–1:500 starting dilution is suitable for most antibodies; the optimal concentration should be determined by the end user in the target cells. (*) Indicates that the antibodies are produced from hybridoma cell lines. MBP: myelin basic protein; MAG: myelin-associated glycoprotein; MPZ: myelin protein zero; GFAP: glial fibrillary acidic protein.

    Journal: Bio-protocol

    Article Title: Human Schwann Cells in vitro III. Analytical Methods and a Practical Approach for Quality Control

    doi: 10.21769/BioProtoc.4840

    Figure Lengend Snippet: Useful antibodies to characterize human Schwann cells (hSCs) and non-glial cells established in cell culture. These antibodies were validated using traditional adult nerve-derived hSC monocultures. Staining with NGFR, Sox10, and S100B antibodies, alone or together with fibronectin, SMA (α-smooth muscle actin), and FAP (fibroblast activation protein/seprase) antibodies, is recommended for the initial characterization of hSCs and non-glial cells. We have not found a ubiquitous non-glial cell marker. Protocol 1C is suitable for staining with all antibodies except for anti-O1 and anti-O4, which can be accomplished only in live cells (Protocol 1B). A 1:200–1:500 starting dilution is suitable for most antibodies; the optimal concentration should be determined by the end user in the target cells. (*) Indicates that the antibodies are produced from hybridoma cell lines. MBP: myelin basic protein; MAG: myelin-associated glycoprotein; MPZ: myelin protein zero; GFAP: glial fibrillary acidic protein.

    Article Snippet: MPZ/P0 Cell membrane and myelin , Chicken polyclonal. AB9352 (Millipore, former Chemicon) , Mostly in myelin debris. Non-myelin-associated MPZ is rarely detectable in expanded hSC cultures..

    Techniques: Cell Culture, Staining, Activation Assay, Marker, Concentration Assay, Produced, Membrane, Isolation, Immunostaining

    Quick staining protocols for human Schwann cell (hSC) validation in culture. Table 2 presents simple strategies for verifying both the human and the SC background of cultured cells. Different antibody combinations using human-selective and multispecies-selective NGFR antibodies in combination with other stains are proposed. NGFR-8737 (mouse monoclonal), S100B (rabbit polyclonal), and GFAP (rabbit polyclonal) antibodies are described in <xref ref-type= Table 1 . HNA monoclonal antibodies are described in Materials and Reagents." width="100%" height="100%">

    Journal: Bio-protocol

    Article Title: Human Schwann Cells in vitro III. Analytical Methods and a Practical Approach for Quality Control

    doi: 10.21769/BioProtoc.4840

    Figure Lengend Snippet: Quick staining protocols for human Schwann cell (hSC) validation in culture. Table 2 presents simple strategies for verifying both the human and the SC background of cultured cells. Different antibody combinations using human-selective and multispecies-selective NGFR antibodies in combination with other stains are proposed. NGFR-8737 (mouse monoclonal), S100B (rabbit polyclonal), and GFAP (rabbit polyclonal) antibodies are described in Table 1 . HNA monoclonal antibodies are described in Materials and Reagents.

    Article Snippet: MPZ/P0 Cell membrane and myelin , Chicken polyclonal. AB9352 (Millipore, former Chemicon) , Mostly in myelin debris. Non-myelin-associated MPZ is rarely detectable in expanded hSC cultures..

    Techniques: Staining, Cell Culture, Derivative Assay