1 2 dioleoyl sn glycero 3 phosphocholine dopc  (Avanti Polar)

 
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    Structured Review

    Avanti Polar 1 2 dioleoyl sn glycero 3 phosphocholine dopc
    Hydrolysis of one medium-chain ox-PC by LPLA2 under neutral conditions. The reaction mixture contained 49 mM HEPES (pH 7.4), 10 μg/ml BSA, liposomes (130 μM PL), and 80 ng/ml of recombinant mouse LPLA2 in 500 μl of total volume. The liposomes consisted of <t>DODPC/DOPC</t> or one medium-chain ox-PC (PAzPC) (2.4:1, molar ratio). The reaction was initiated by the addition of recombinant LPLA2 and kept for 30 to 120 min at 37°C. The reaction products were extracted and separated with a HPTLC plate using a solvent system consisting of chloroform/methanol/pyridine (98:2:0.5, v/v) (A, B) or chloroform/methanol/water (60:35:8, v/v) (C), as described in the Materials and Methods. The reaction products produced by LPLA2 in (A–C) were quantified by scanning the plate, as described in the Materials and Methods, and were plotted against the incubation time (D). 1-Pal-2-LysoPC, 1-palmitoyl- sn <t>-glycero-3-phosphocholine.</t>
    1 2 Dioleoyl Sn Glycero 3 Phosphocholine Dopc, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 99/100, based on 47 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Preferential hydrolysis of truncated oxidized glycerophospholipids by lysosomal phospholipase A2"

    Article Title: Preferential hydrolysis of truncated oxidized glycerophospholipids by lysosomal phospholipase A2

    Journal: Journal of Lipid Research

    doi: 10.1194/jlr.M070730

    Hydrolysis of one medium-chain ox-PC by LPLA2 under neutral conditions. The reaction mixture contained 49 mM HEPES (pH 7.4), 10 μg/ml BSA, liposomes (130 μM PL), and 80 ng/ml of recombinant mouse LPLA2 in 500 μl of total volume. The liposomes consisted of DODPC/DOPC or one medium-chain ox-PC (PAzPC) (2.4:1, molar ratio). The reaction was initiated by the addition of recombinant LPLA2 and kept for 30 to 120 min at 37°C. The reaction products were extracted and separated with a HPTLC plate using a solvent system consisting of chloroform/methanol/pyridine (98:2:0.5, v/v) (A, B) or chloroform/methanol/water (60:35:8, v/v) (C), as described in the Materials and Methods. The reaction products produced by LPLA2 in (A–C) were quantified by scanning the plate, as described in the Materials and Methods, and were plotted against the incubation time (D). 1-Pal-2-LysoPC, 1-palmitoyl- sn -glycero-3-phosphocholine.
    Figure Legend Snippet: Hydrolysis of one medium-chain ox-PC by LPLA2 under neutral conditions. The reaction mixture contained 49 mM HEPES (pH 7.4), 10 μg/ml BSA, liposomes (130 μM PL), and 80 ng/ml of recombinant mouse LPLA2 in 500 μl of total volume. The liposomes consisted of DODPC/DOPC or one medium-chain ox-PC (PAzPC) (2.4:1, molar ratio). The reaction was initiated by the addition of recombinant LPLA2 and kept for 30 to 120 min at 37°C. The reaction products were extracted and separated with a HPTLC plate using a solvent system consisting of chloroform/methanol/pyridine (98:2:0.5, v/v) (A, B) or chloroform/methanol/water (60:35:8, v/v) (C), as described in the Materials and Methods. The reaction products produced by LPLA2 in (A–C) were quantified by scanning the plate, as described in the Materials and Methods, and were plotted against the incubation time (D). 1-Pal-2-LysoPC, 1-palmitoyl- sn -glycero-3-phosphocholine.

    Techniques Used: Recombinant, High Performance Thin Layer Chromatography, Produced, Incubation

    2) Product Images from "Ganglioside embedded in reconstituted lipoprotein binds cholera toxin with elevated affinity [S]"

    Article Title: Ganglioside embedded in reconstituted lipoprotein binds cholera toxin with elevated affinity [S]

    Journal: Journal of Lipid Research

    doi: 10.1194/jlr.M007401

    CTB-GM1 binding in surface-supported membranes. A: UV patterning enables a side-by-side comparison of Texas Red-labeled cholera toxin binding to 1 mol% GM1 supported in a fluid DMPC bilayer (outside squares) versus rHDL supports (inside squares). B: A plot of the fluorescence intensity along the line shown, indicates a 2-to 3-fold increase between the region inside and outside of the squares. CTB, cholera toxin subunit B; DMPC, 1,2-dimyristoyl-sn-glycero-3-phosphocholine; GM1, monosialotetrahexosylganglioside.
    Figure Legend Snippet: CTB-GM1 binding in surface-supported membranes. A: UV patterning enables a side-by-side comparison of Texas Red-labeled cholera toxin binding to 1 mol% GM1 supported in a fluid DMPC bilayer (outside squares) versus rHDL supports (inside squares). B: A plot of the fluorescence intensity along the line shown, indicates a 2-to 3-fold increase between the region inside and outside of the squares. CTB, cholera toxin subunit B; DMPC, 1,2-dimyristoyl-sn-glycero-3-phosphocholine; GM1, monosialotetrahexosylganglioside.

    Techniques Used: CtB Assay, Binding Assay, Labeling, Fluorescence

    Interaction of cells with vesicles and rHDL separately. Equal concentrations of fluorescently-labeled lipid particles are incubated for 4 h with RPE cells. POPC 100 nm diameter unilamellar vesicles with 2 mol% Texas Red-DHPE (A) and reconstituted HDL composed of apoA-I, DMPC, and 2 mol% Texas Red-DHPE (B) both show some association with cells. All images obtained at 10× magnification. ApoA-I, apolipoprotein A-I; DHPE, 1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine, triethyl-ammonium salt; DMPC, 1,2-dimyristoyl-sn-glycero-3-phosphocholine.
    Figure Legend Snippet: Interaction of cells with vesicles and rHDL separately. Equal concentrations of fluorescently-labeled lipid particles are incubated for 4 h with RPE cells. POPC 100 nm diameter unilamellar vesicles with 2 mol% Texas Red-DHPE (A) and reconstituted HDL composed of apoA-I, DMPC, and 2 mol% Texas Red-DHPE (B) both show some association with cells. All images obtained at 10× magnification. ApoA-I, apolipoprotein A-I; DHPE, 1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine, triethyl-ammonium salt; DMPC, 1,2-dimyristoyl-sn-glycero-3-phosphocholine.

    Techniques Used: Labeling, Incubation

    Characterization of FRET pair and toxin-quencher titration. A: Excitation and emission spectra of DPH and FITC-CTB. Intensity of each spectrum is not to scale. Inset: schematic representation of DPH (green) embedded in the hydrophobic core of the lipoprotein (yellow) and its proximity to a receptor (purple) and fluorescently-labeled pentavalent ligand (red). B: Stern-Volmer plot of GM1-CTB binding for DMPC vesicles containing 1.0 mol% GM1. The independent axis is molarity of CTB (nM) and the dependent axis is the inverse normalized donor fluorescence ( I o / I) . Error bars are derived from instrument error. The entire collection of S-V plots are available in the supplementary data. CTB, cholera toxin subunit B; DMPC, 1,2-dimyristoyl-sn-glycero-3-phosphocholine; DPH, diphenylhexatriene; FITC, fluorescein-isothiocyanate; FRET, Foerster Resonant Energy Transfer; GM1, monosialotetrahexosylganglioside.
    Figure Legend Snippet: Characterization of FRET pair and toxin-quencher titration. A: Excitation and emission spectra of DPH and FITC-CTB. Intensity of each spectrum is not to scale. Inset: schematic representation of DPH (green) embedded in the hydrophobic core of the lipoprotein (yellow) and its proximity to a receptor (purple) and fluorescently-labeled pentavalent ligand (red). B: Stern-Volmer plot of GM1-CTB binding for DMPC vesicles containing 1.0 mol% GM1. The independent axis is molarity of CTB (nM) and the dependent axis is the inverse normalized donor fluorescence ( I o / I) . Error bars are derived from instrument error. The entire collection of S-V plots are available in the supplementary data. CTB, cholera toxin subunit B; DMPC, 1,2-dimyristoyl-sn-glycero-3-phosphocholine; DPH, diphenylhexatriene; FITC, fluorescein-isothiocyanate; FRET, Foerster Resonant Energy Transfer; GM1, monosialotetrahexosylganglioside.

    Techniques Used: Titration, CtB Assay, Labeling, Binding Assay, Fluorescence, Derivative Assay

    3) Product Images from "Topical delivery of anti-TNFα siRNA and capsaicin via novel lipid-polymer hybrid nanoparticles efficiently inhibits skin inflammation in vivo"

    Article Title: Topical delivery of anti-TNFα siRNA and capsaicin via novel lipid-polymer hybrid nanoparticles efficiently inhibits skin inflammation in vivo

    Journal: Journal of controlled release : official journal of the Controlled Release Society

    doi: 10.1016/j.jconrel.2013.04.021

    Schematic illustration shows the formulation of CyLiPn. The CyLiPn comprises a hydrophobic PLGA core, a hydrophilic PEG shell and a lipid monolayer consisting of 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) and a new cationic cyclic-head lipid at the
    Figure Legend Snippet: Schematic illustration shows the formulation of CyLiPn. The CyLiPn comprises a hydrophobic PLGA core, a hydrophilic PEG shell and a lipid monolayer consisting of 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) and a new cationic cyclic-head lipid at the

    Techniques Used:

    4) Product Images from "A non-mitotic role for Aurora kinase A as a direct activator of cell migration upon interaction with PLD, FAK and Src"

    Article Title: A non-mitotic role for Aurora kinase A as a direct activator of cell migration upon interaction with PLD, FAK and Src

    Journal: Journal of Cell Science

    doi: 10.1242/jcs.157339

    Phosphatidic acid binds to and activates AURA and positively affects tubulin polymerization. (A) Protein–lipid overlay assays using 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPA) and lysates from cells overexpressing AURA. DOPC was used as a negative control. (B) Positive effect of increasing concentrations of phosphatidic acid (PA) on catalytic activity of recombinant purified AURA. Experiments were performed in triplicate and are expressed as the mean±s.e.m. percentage of control. * P
    Figure Legend Snippet: Phosphatidic acid binds to and activates AURA and positively affects tubulin polymerization. (A) Protein–lipid overlay assays using 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPA) and lysates from cells overexpressing AURA. DOPC was used as a negative control. (B) Positive effect of increasing concentrations of phosphatidic acid (PA) on catalytic activity of recombinant purified AURA. Experiments were performed in triplicate and are expressed as the mean±s.e.m. percentage of control. * P

    Techniques Used: Negative Control, Activity Assay, Recombinant, Purification

    5) Product Images from "Phosphatidic Acid (PA) can Displace PPARα/LXRα Binding to The EGFR Promoter Causing its Transrepression in Luminal Cancer Cells"

    Article Title: Phosphatidic Acid (PA) can Displace PPARα/LXRα Binding to The EGFR Promoter Causing its Transrepression in Luminal Cancer Cells

    Journal: Scientific Reports

    doi: 10.1038/srep15379

    Binding and circular dichroism of PPARα in the presence of PA. ( A ) Phospholipase assay was performed using recombinant PLD2 and cells overexpressing PLD2 in the presence of several phospholipids: potential PLD substrates, 1,2-dioctanoyl-sn-glycero-3-phosphocholine (DOPC); 1,2-dimirystoyl-sn-glycero-3-phosphocholine (DMPC); 1,2-diarachidonoyl-sn-glycero-3-phosphocholine (AraPC); 1-oleoyl-2 -hydroxy-sn-glycero-3-phosphatidic acid (lyso-PC) and oxidized 1-palimitoyl, 2-arachidonoyl—sn-glycero-3-phosphocholine (OxPAPC). DOPC is considered the best substrate (positive control). ( B ) Protein-lipid overlay assays to PVDF membranes were performed with recombinant PPARα. PIP 2 was used as a positive control for biding to PPARα and cholesterol was used as a negative control. ( C–E ) Protein-lipid binding by quenching of intrinsic aromatic amino acid fluorescence using the lipids: PC ( C ), DOPA ( D ) or AraPA ( E ) with recombinant PPARα in vitro . ( F,G ) Circular dichroism of PPARα upon binding to ( F ) AraPA (yellow circles) or lysoPA (blue circles), or ( G ) DOPA (red circles) or DMPA (green circles). ( H ) Positive control for Circular Dichroism; PPAR bound to C18:0-CoA, its strongest lignad. ( I ) Secondary structure analysis to ascertain the percentage of alpha helices, beta sheets, turns and undetermined structures in PPAR in the presence of PC or PA. C18:0-CoA was used as a positive control.
    Figure Legend Snippet: Binding and circular dichroism of PPARα in the presence of PA. ( A ) Phospholipase assay was performed using recombinant PLD2 and cells overexpressing PLD2 in the presence of several phospholipids: potential PLD substrates, 1,2-dioctanoyl-sn-glycero-3-phosphocholine (DOPC); 1,2-dimirystoyl-sn-glycero-3-phosphocholine (DMPC); 1,2-diarachidonoyl-sn-glycero-3-phosphocholine (AraPC); 1-oleoyl-2 -hydroxy-sn-glycero-3-phosphatidic acid (lyso-PC) and oxidized 1-palimitoyl, 2-arachidonoyl—sn-glycero-3-phosphocholine (OxPAPC). DOPC is considered the best substrate (positive control). ( B ) Protein-lipid overlay assays to PVDF membranes were performed with recombinant PPARα. PIP 2 was used as a positive control for biding to PPARα and cholesterol was used as a negative control. ( C–E ) Protein-lipid binding by quenching of intrinsic aromatic amino acid fluorescence using the lipids: PC ( C ), DOPA ( D ) or AraPA ( E ) with recombinant PPARα in vitro . ( F,G ) Circular dichroism of PPARα upon binding to ( F ) AraPA (yellow circles) or lysoPA (blue circles), or ( G ) DOPA (red circles) or DMPA (green circles). ( H ) Positive control for Circular Dichroism; PPAR bound to C18:0-CoA, its strongest lignad. ( I ) Secondary structure analysis to ascertain the percentage of alpha helices, beta sheets, turns and undetermined structures in PPAR in the presence of PC or PA. C18:0-CoA was used as a positive control.

    Techniques Used: Binding Assay, Recombinant, Positive Control, Negative Control, Fluorescence, In Vitro

    Related Articles

    Clone Assay:

    Article Title: CHIP as a membrane-shuttling proteostasis sensor
    Article Snippet: 1,2-dioleoyl-sn -glycero-3-phosphocholine (DOPC) and 1,2-dipalmitoyl-sn -glycero-3-phosphate (phosphatidic acid, PA) were from Avanti Polar Lipids (Alabaster, AL), 1,2-dipalmitoyl-sn -glycero-3-phosphoinositol-4-phosphate (phosphadtidylinositol-4-phosphate, PI4P) was from Echelon Bioscience (Salt Lake City, UT). .. N-terminal EGFP-CHIP fusion protein was constructed by cloning human CHIP coding sequence in pEGFP-C2 vector (Clontech) using HindIII and BamHI restriction sites.

    Synthesized:

    Article Title: Reversible glycosidic switch for secure delivery of molecular nanocargos
    Article Snippet: DSPC, 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), 1,2-distearoyl-sn-glycero-3-phosphoethanolamine-N-[methoxy(polyethylene glycol)-2000] (DSPE-PEG-2000), 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[methoxy(polyethylene glycol)-2000] (DOPE-PEG), and cholesterol were purchased from Avanti Polar Lipids, Inc. (Alabaster, AL). .. 9AC , 9-aminocamptothecin-β-D-glucuronide (9AC-GW ), and 5,6-dihydro-4H-benzo[de]quinoline-camptothecin-β-D-glucuronide (BQC-GW ) were chemically synthesized.

    Construct:

    Article Title: CHIP as a membrane-shuttling proteostasis sensor
    Article Snippet: 1,2-dioleoyl-sn -glycero-3-phosphocholine (DOPC) and 1,2-dipalmitoyl-sn -glycero-3-phosphate (phosphatidic acid, PA) were from Avanti Polar Lipids (Alabaster, AL), 1,2-dipalmitoyl-sn -glycero-3-phosphoinositol-4-phosphate (phosphadtidylinositol-4-phosphate, PI4P) was from Echelon Bioscience (Salt Lake City, UT). .. N-terminal EGFP-CHIP fusion protein was constructed by cloning human CHIP coding sequence in pEGFP-C2 vector (Clontech) using HindIII and BamHI restriction sites.

    Incubation:

    Article Title: A non-mitotic role for Aurora kinase A as a direct activator of cell migration upon interaction with PLD, FAK and Src
    Article Snippet: Briefly, increasing concentrations (0, 3, 10 or 30 µg) of either 1,2-dioleoyl-sn-glycero-3-phosphate (DOPA) or 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) from Avanti Polar Lipids (Alabaster, AL) were spotted onto a PVDF membrane. .. The membrane was blocked overnight with a 3% fatty-acid-free BSA solution, then incubated with the cell lysate at 4°C, then was washed extensively with TBS-T and incubated with anti-AURA antibody for 1–2 h at room temperature.

    Activity Assay:

    Article Title: Interaction of Melittin with Membrane Cholesterol: A Fluorescence Approach
    Article Snippet: 1,2-Dioleoyl- sn -glycero-3-phosphocholine (DOPC), 1-palmitoyl-2-(5-doxyl)stearoyl- sn -glycero-3-phosphocholine (5-PC), and 1-palmitoyl-2-(12-doxyl)stearoyl- sn -glycero-3-phosphocholine (12-PC) were purchased from Avanti Polar Lipids (Alabaster, AL). .. To check for any residual phospholipase A2 contamination in melittin, phospholipase activity was assayed using 14 C-labeled (DOPC) (Amersham International, Buckinghamshire, UK) as described earlier ( ).

    Cell Culture:

    Article Title: ESeroS-GS Protects Neuronal Cells from Oxidative Stress by Stabilizing Lysosomes
    Article Snippet: 1,2-Dioleoyl-sn-glycero-3-phosphate (DOPA), 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) and 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE) were from Avanti Polar Lipids (Alabaster, AL, USA). .. Acridine orange (AO), N -(1-pyrenyl)maleimide (PM), 4’,6-diamidino-2-phenylindole (DAPI), cell culture medium, cell culture supplements and fetal bovine serum were from Life Technologies (Eugene, OR, USA).

    Expressing:

    Article Title: CHIP as a membrane-shuttling proteostasis sensor
    Article Snippet: 1,2-dioleoyl-sn -glycero-3-phosphocholine (DOPC) and 1,2-dipalmitoyl-sn -glycero-3-phosphate (phosphatidic acid, PA) were from Avanti Polar Lipids (Alabaster, AL), 1,2-dipalmitoyl-sn -glycero-3-phosphoinositol-4-phosphate (phosphadtidylinositol-4-phosphate, PI4P) was from Echelon Bioscience (Salt Lake City, UT). .. For mammalian expression of EGFP, the expression vector pEGFP-N1 from Clontech (Mountain View, CA) was used.

    High Performance Liquid Chromatography:

    Article Title: Insertion of perilipin 3 into a glycero(phospho)lipid monolayer depends on lipid headgroup and acyl chain species [S]
    Article Snippet: The 1-palmitoyl-2-oleoyl- sn -glycerol (POG), 1-palmitoyl-2-oleoyl- sn -glycero-3-phosphocholine (POPC), 1,2-dioleoyl- sn -glycero-3-phosphocholine (DOPC), 1-palmitoyl-2-oleoyl- sn -glycero-3-phosphoethanolamine (POPE), 1,2-dioleoyl- sn -glycero-3-phosphoethanolamine (DOPE), 1-palmitoyl-2-oleoyl- sn -glycero-3-phospho-(1′-rac-glycerol) (POPG), 1-palmitoyl-2-oleoyl- sn -glycero-3-phosphate (sodium salt) (POPA), and 1,2-dioleoyl- sn -glycero-3-phosphate (sodium salt) (DOPA) were purchased from Avanti Polar Lipids (Alabaster, AL). .. HPLC grade water was purchased from Fisher Scientific.

    Article Title: Aggregation of Aß(25-35) on DOPC and DOPC/DHA Bilayers: An Atomic Force Microscopy Study
    Article Snippet: Materials Dichloromethane and methanol, HPLC-grade solvents, were purchased from Merck (Darmstadt, Germany), while 1,1,1,3,3,3-hexafluoroisopropanol (HFIP) was supplied by Sigma-Aldrich (St. Louis, MO, USA). .. 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) and 1,2-didocosahexaenoyl-sn-glycero-3 phosphocholine (22∶6(cis)PC) were obtained from Avanti Polar Lipids (Birmingham, AL, USA).

    Article Title: Topical delivery of anti-TNFα siRNA and capsaicin via novel lipid-polymer hybrid nanoparticles efficiently inhibits skin inflammation in vivo
    Article Snippet: HPLC grade of acetonitrile, water and ethanol were purchased from Sigma-Aldrich Co (St. Louis, MO, USA). .. 1,2-dioleoyl- sn -glycero-3-phosphocholine (DOPC), 1,2-distearoyl- sn -glycero-3-phosphoethanolamine-N-[amino(poly-ethylene glycol)-2000] (ammonium salt) (DSPE-PEG2000 ) were purchased from Avanti Polar lipids (Alabaster, AL, USA).

    Flow Cytometry:

    Article Title: Hybrid cell reactor system from Escherichia coli protoplast cells and arrayed lipid bilayer chamber device
    Article Snippet: Paragraph title: Preparation of flow channel and hybrid cells ... Next, 20 μL of lipid solution containing 1.0 mg/mL 1,2-dioleoyl- sn -glycero-3-phosphocholine (DOPC) (Avanti Polar Lipids, Alabaster, AL, USA) and 0.2 mg/mL 1,2-dioleoyl- sn -glycero-3-phosphoethanolamine (DOPE) (Avanti Polar Lipids) in hexadecane (Sigma-Aldrich, St. Louis, MO, USA) was injected to flush away the first SP buffer.

    Protein-lipid Overlay Assay (PLOA):

    Article Title: A non-mitotic role for Aurora kinase A as a direct activator of cell migration upon interaction with PLD, FAK and Src
    Article Snippet: Paragraph title: Protein–lipid overlay assay ... Briefly, increasing concentrations (0, 3, 10 or 30 µg) of either 1,2-dioleoyl-sn-glycero-3-phosphate (DOPA) or 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) from Avanti Polar Lipids (Alabaster, AL) were spotted onto a PVDF membrane.

    CtB Assay:

    Article Title: Ganglioside embedded in reconstituted lipoprotein binds cholera toxin with elevated affinity [S]
    Article Snippet: 1,2-Dimyristoyl-sn-glycero-3-phosphocholine (DMPC), 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), sphingomyelin, cholesterol (ovine wool)( > 98%), and GM1 ganglioside (brain, ovine, ammonium salt) were obtained from Avanti Polar Lipids (Alabaster, AL). .. 1,6-Diphenyl-1,3,5-hexatriene (DPH), Texas Red 1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine, triethyl-ammonium salt (TR-DHPE), N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)-1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine, triethyl-ammonium salt (NBD-PE), along with Alexa594-labeled cholera toxin subunit (CTB) were purchased from Invitrogen (Carlsbad, CA).

    Sequencing:

    Article Title: CHIP as a membrane-shuttling proteostasis sensor
    Article Snippet: 1,2-dioleoyl-sn -glycero-3-phosphocholine (DOPC) and 1,2-dipalmitoyl-sn -glycero-3-phosphate (phosphatidic acid, PA) were from Avanti Polar Lipids (Alabaster, AL), 1,2-dipalmitoyl-sn -glycero-3-phosphoinositol-4-phosphate (phosphadtidylinositol-4-phosphate, PI4P) was from Echelon Bioscience (Salt Lake City, UT). .. N-terminal EGFP-CHIP fusion protein was constructed by cloning human CHIP coding sequence in pEGFP-C2 vector (Clontech) using HindIII and BamHI restriction sites.

    Sonication:

    Article Title: Bacterial Secretins Form Constitutively Open Pores Akin to General Porins
    Article Snippet: 1,2-Dioleoyl- sn -glycero-3-phosphocholine (DOPC) (Avanti Polar Lipids) dissolved in chloroform was dried under a stream of nitrogen. .. Multilamellar liposomes were probe sonicated three times for 2 min (with 1-min intervals on ice) at 50% duty cycle and at an output of 3 using a Sonics Vibracell sonicator.

    Injection:

    Article Title: Hybrid cell reactor system from Escherichia coli protoplast cells and arrayed lipid bilayer chamber device
    Article Snippet: .. Next, 20 μL of lipid solution containing 1.0 mg/mL 1,2-dioleoyl- sn -glycero-3-phosphocholine (DOPC) (Avanti Polar Lipids, Alabaster, AL, USA) and 0.2 mg/mL 1,2-dioleoyl- sn -glycero-3-phosphoethanolamine (DOPE) (Avanti Polar Lipids) in hexadecane (Sigma-Aldrich, St. Louis, MO, USA) was injected to flush away the first SP buffer. ..

    Recombinant:

    Article Title: Preferential hydrolysis of truncated oxidized glycerophospholipids by lysosomal phospholipase A2
    Article Snippet: .. The 1,2-dioleoyl- sn -glycero-3-phosphocholine (DOPC), 1,2- O -octadecenyl- sn -glycero-3-phosphocholine (DODPC), N -acetylsphingosine (NAS), N -oleoyl-sphingosine, POVPC, PGPC, PONPC, PAzPC, 1-palmitoyl-2-acetyl- sn -glycero-3-phosphocholine (PAcPC), and 1-nonanoyl- sn -glycero-3-phosphocholine were obtained from Avanti Polar Lipids Corp. (Alabaster, AL); recombinant mouse LPLA2 was from Proteos (Kalamazoo, MI); high-performance TLC (HPTLC) silica gel plates (10 × 20 cm) were from Merck (Darmstadt, Germany). .. A HPTLC plate was immersed into 100 mM AgNO3 in acetonitrile and incubated for 10 min.

    MTT Assay:

    Article Title: ESeroS-GS Protects Neuronal Cells from Oxidative Stress by Stabilizing Lysosomes
    Article Snippet: 6-Hydroxy-2,5,7,8-tetramethychroman-2-carboxylic acid (Trolox), 2,2’-azinobis (3-ethylbenzothiozoline-6-sulphonic acid) diammonium salt (ABTS), 1,1-dipheny-2-picrylhydrazyl (DPPH), 5-carboxyfluorescein (CF), N -p-tosyl-l -phenylalanine chloromethyl ketone (TPCK), (2S ,3S )-trans-epoxysuccinyl-l -leucylamido-3-methylbutane ethyl ester (E-64d), pepstatin A, 2-[4-(2-Hydroxyethyl)-1-piperazinyl]ethanesulfonic acid (HEPES), 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2-H-tetrazolium bromide (MTT) and ethylenediaminetetraacetic acid disodium salt (EDTA) were from Sigma-Aldrich (St Louis, MO, USA). .. 1,2-Dioleoyl-sn-glycero-3-phosphate (DOPA), 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) and 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE) were from Avanti Polar Lipids (Alabaster, AL, USA).

    Isolation:

    Article Title: Oxidative Stress Can Affect the Gene Silencing Effect of DOTAP Liposome in an In Vitro Translation System
    Article Snippet: Experimental Materials 1,2-Dioleoyl-3-trimethyl-ammonium-propane (DOTAP) and 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) were purchased from Avanti Polar Lipids (Alabaster, AL). .. The SV Total RNA Isolation System was purchased from Promega (Madison, WI).

    Transfection:

    Article Title: Topical delivery of anti-TNFα siRNA and capsaicin via novel lipid-polymer hybrid nanoparticles efficiently inhibits skin inflammation in vivo
    Article Snippet: 1,2-dioleoyl- sn -glycero-3-phosphocholine (DOPC), 1,2-distearoyl- sn -glycero-3-phosphoethanolamine-N-[amino(poly-ethylene glycol)-2000] (ammonium salt) (DSPE-PEG2000 ) were purchased from Avanti Polar lipids (Alabaster, AL, USA). .. Lipofectamine™ RNAiMAX transfection reagent was purchased from Life Technologies (Grand Island, NY, USA).

    Protein Purification:

    Article Title: Insertion of perilipin 3 into a glycero(phospho)lipid monolayer depends on lipid headgroup and acyl chain species [S]
    Article Snippet: The 1-palmitoyl-2-oleoyl- sn -glycerol (POG), 1-palmitoyl-2-oleoyl- sn -glycero-3-phosphocholine (POPC), 1,2-dioleoyl- sn -glycero-3-phosphocholine (DOPC), 1-palmitoyl-2-oleoyl- sn -glycero-3-phosphoethanolamine (POPE), 1,2-dioleoyl- sn -glycero-3-phosphoethanolamine (DOPE), 1-palmitoyl-2-oleoyl- sn -glycero-3-phospho-(1′-rac-glycerol) (POPG), 1-palmitoyl-2-oleoyl- sn -glycero-3-phosphate (sodium salt) (POPA), and 1,2-dioleoyl- sn -glycero-3-phosphate (sodium salt) (DOPA) were purchased from Avanti Polar Lipids (Alabaster, AL). .. The 1-palmitoyl-2-oleoyl- sn -glycerol (POG), 1-palmitoyl-2-oleoyl- sn -glycero-3-phosphocholine (POPC), 1,2-dioleoyl- sn -glycero-3-phosphocholine (DOPC), 1-palmitoyl-2-oleoyl- sn -glycero-3-phosphoethanolamine (POPE), 1,2-dioleoyl- sn -glycero-3-phosphoethanolamine (DOPE), 1-palmitoyl-2-oleoyl- sn -glycero-3-phospho-(1′-rac-glycerol) (POPG), 1-palmitoyl-2-oleoyl- sn -glycero-3-phosphate (sodium salt) (POPA), and 1,2-dioleoyl- sn -glycero-3-phosphate (sodium salt) (DOPA) were purchased from Avanti Polar Lipids (Alabaster, AL).

    Chromatin Immunoprecipitation:

    Article Title: CHIP as a membrane-shuttling proteostasis sensor
    Article Snippet: 1,2-dioleoyl-sn -glycero-3-phosphocholine (DOPC) and 1,2-dipalmitoyl-sn -glycero-3-phosphate (phosphatidic acid, PA) were from Avanti Polar Lipids (Alabaster, AL), 1,2-dipalmitoyl-sn -glycero-3-phosphoinositol-4-phosphate (phosphadtidylinositol-4-phosphate, PI4P) was from Echelon Bioscience (Salt Lake City, UT). .. N-terminal EGFP-CHIP fusion protein was constructed by cloning human CHIP coding sequence in pEGFP-C2 vector (Clontech) using HindIII and BamHI restriction sites.

    Plasmid Preparation:

    Article Title: CHIP as a membrane-shuttling proteostasis sensor
    Article Snippet: 1,2-dioleoyl-sn -glycero-3-phosphocholine (DOPC) and 1,2-dipalmitoyl-sn -glycero-3-phosphate (phosphatidic acid, PA) were from Avanti Polar Lipids (Alabaster, AL), 1,2-dipalmitoyl-sn -glycero-3-phosphoinositol-4-phosphate (phosphadtidylinositol-4-phosphate, PI4P) was from Echelon Bioscience (Salt Lake City, UT). .. For mammalian expression of EGFP, the expression vector pEGFP-N1 from Clontech (Mountain View, CA) was used.

    Binding Assay:

    Article Title: A non-mitotic role for Aurora kinase A as a direct activator of cell migration upon interaction with PLD, FAK and Src
    Article Snippet: Protein–lipid overlay assay The method for preparing and detecting protein–lipid binding was as previously described ( ). .. Briefly, increasing concentrations (0, 3, 10 or 30 µg) of either 1,2-dioleoyl-sn-glycero-3-phosphate (DOPA) or 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) from Avanti Polar Lipids (Alabaster, AL) were spotted onto a PVDF membrane.

    Article Title: Phosphatidic Acid (PA) can Displace PPARα/LXRα Binding to The EGFR Promoter Causing its Transrepression in Luminal Cancer Cells
    Article Snippet: Paragraph title: (a) Protein-lipid binding to PVDF membranes ... Briefly, the following list lipids were spotted on to the PVDF membrane: 1,2-dioleoyl-sn-glycero-3-phosphate (DOPA), 1,2-diarachidinooyl-sn-glycero-3-phosphate (AraPA), 1,2-diMirystoyl-sn-glycero-3-phosphate (DMPA), 1-oleoyl, 2-hydroxy-sn-glycero-3-phosphate (LysoPA), 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) and 1,2-diarachidonoyl-sn-glycero-3-phosphocholine (AraPC) lipids from Avanti Polar Lipids (Alabaster, AL) were spotted onto a PVDF membrane.

    High Performance Thin Layer Chromatography:

    Article Title: Preferential hydrolysis of truncated oxidized glycerophospholipids by lysosomal phospholipase A2
    Article Snippet: .. The 1,2-dioleoyl- sn -glycero-3-phosphocholine (DOPC), 1,2- O -octadecenyl- sn -glycero-3-phosphocholine (DODPC), N -acetylsphingosine (NAS), N -oleoyl-sphingosine, POVPC, PGPC, PONPC, PAzPC, 1-palmitoyl-2-acetyl- sn -glycero-3-phosphocholine (PAcPC), and 1-nonanoyl- sn -glycero-3-phosphocholine were obtained from Avanti Polar Lipids Corp. (Alabaster, AL); recombinant mouse LPLA2 was from Proteos (Kalamazoo, MI); high-performance TLC (HPTLC) silica gel plates (10 × 20 cm) were from Merck (Darmstadt, Germany). .. A HPTLC plate was immersed into 100 mM AgNO3 in acetonitrile and incubated for 10 min.

    Thin Layer Chromatography:

    Article Title: Interaction of Melittin with Membrane Cholesterol: A Fluorescence Approach
    Article Snippet: 1,2-Dioleoyl- sn -glycero-3-phosphocholine (DOPC), 1-palmitoyl-2-(5-doxyl)stearoyl- sn -glycero-3-phosphocholine (5-PC), and 1-palmitoyl-2-(12-doxyl)stearoyl- sn -glycero-3-phosphocholine (12-PC) were purchased from Avanti Polar Lipids (Alabaster, AL). .. Lipids were checked for purity by thin layer chromatography on silica gel precoated plates (Sigma) in chloroform/methanol/water (65:35:5, v/v/v) and were found to give only one spot in all cases with a phosphate-sensitive spray and on subsequent charring ( ).

    Article Title: Preferential hydrolysis of truncated oxidized glycerophospholipids by lysosomal phospholipase A2
    Article Snippet: .. The 1,2-dioleoyl- sn -glycero-3-phosphocholine (DOPC), 1,2- O -octadecenyl- sn -glycero-3-phosphocholine (DODPC), N -acetylsphingosine (NAS), N -oleoyl-sphingosine, POVPC, PGPC, PONPC, PAzPC, 1-palmitoyl-2-acetyl- sn -glycero-3-phosphocholine (PAcPC), and 1-nonanoyl- sn -glycero-3-phosphocholine were obtained from Avanti Polar Lipids Corp. (Alabaster, AL); recombinant mouse LPLA2 was from Proteos (Kalamazoo, MI); high-performance TLC (HPTLC) silica gel plates (10 × 20 cm) were from Merck (Darmstadt, Germany). .. A HPTLC plate was immersed into 100 mM AgNO3 in acetonitrile and incubated for 10 min.

    Fractionation:

    Article Title: Using Breast Cancer Cell CXCR4 Surface Expression to Predict Liposome Binding and Cytotoxicity
    Article Snippet: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-dodecanoyl (N-dod-PE) and 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) were purchased from Avanti Polar Lipids (Alabaster, AL). .. Doxorubicin hydrochloride (Dox), 1-Ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride (EDC), N-hydroxysuccinimide (NHS), Triton X-100, bovine serum albumin (BSA), rhodamine-B isothio-cyanate-conjugated dextran (rhodamine-dextran, 10 kDa MW), ammonium molybdate, ammonium sulfate, ascorbic acid, anhydrous dimethyl sulfoxide (DMSO), Sepharose CL-4B column (fractionation range: 60-20,000 kDa), dialysis tubing cellulose membrane (MWCO 12.4 kDa), and ethanol (EtOH) were purchased from Sigma-Aldrich (St. Louis, MO).

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  • 99
    Avanti Polar dopc
    Characterization of <t>SthK</t> channel activity. (A) Normalized 86 Rb + flux through SthK (reconstituted in 5:3:2 <t>DOPC:POPG:cardiolipin)</t> in the presence of 200 µM cAMP (red squares), cGMP (blue circles), both cAMP and cGMP (black triangles), and without cyclic nucleotides (open triangles). Flux through empty liposomes (open circles) is shown as a reference. All flux values are normalized to the maximum uptake recorded in the presence of valinomycin. Bars represent means ± SEM for three separate experiments. (B) SthK channel activity represented by the maximum achieved 86 Rb + uptake through SthK reconstituted in liposomes made from 3:1 POPE:POPG (PE:PG) or 5:3:2 DOPC:POPG:cardiolipin (PC:PG:CA), as indicated, in the presence of 200 µM cAMP. Bars represent means ± SEM for three separate experiments. (C) Representative single-channel recordings of SthK in 0.1 mM intracellular cAMP. (D) I-V relationship of SthK single-channel current amplitude at 100 µM cAMP. (E) Open probability of SthK at 100 mV as a function of the cAMP concentration. Fitting the data with Eq. 10 yields an apparent activation constant of EC 50 = 17 µM and a Hill coefficient of n H = 3. The number of repeats is indicated beside each data point. (F) Open probability of SthK in the presence of 500 µM cAMP as function of the membrane potential. The line indicates the fit according to Eq. 13 , leading to z = 0.8 and V half = 87 mV, Po max = 0.65, and Po min = 0.05. Symbols and error bars in D–F represent means ± SEM from at least three separate bilayers.
    Dopc, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 99/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Characterization of SthK channel activity. (A) Normalized 86 Rb + flux through SthK (reconstituted in 5:3:2 DOPC:POPG:cardiolipin) in the presence of 200 µM cAMP (red squares), cGMP (blue circles), both cAMP and cGMP (black triangles), and without cyclic nucleotides (open triangles). Flux through empty liposomes (open circles) is shown as a reference. All flux values are normalized to the maximum uptake recorded in the presence of valinomycin. Bars represent means ± SEM for three separate experiments. (B) SthK channel activity represented by the maximum achieved 86 Rb + uptake through SthK reconstituted in liposomes made from 3:1 POPE:POPG (PE:PG) or 5:3:2 DOPC:POPG:cardiolipin (PC:PG:CA), as indicated, in the presence of 200 µM cAMP. Bars represent means ± SEM for three separate experiments. (C) Representative single-channel recordings of SthK in 0.1 mM intracellular cAMP. (D) I-V relationship of SthK single-channel current amplitude at 100 µM cAMP. (E) Open probability of SthK at 100 mV as a function of the cAMP concentration. Fitting the data with Eq. 10 yields an apparent activation constant of EC 50 = 17 µM and a Hill coefficient of n H = 3. The number of repeats is indicated beside each data point. (F) Open probability of SthK in the presence of 500 µM cAMP as function of the membrane potential. The line indicates the fit according to Eq. 13 , leading to z = 0.8 and V half = 87 mV, Po max = 0.65, and Po min = 0.05. Symbols and error bars in D–F represent means ± SEM from at least three separate bilayers.

    Journal: The Journal of General Physiology

    Article Title: Ligand binding and activation properties of the purified bacterial cyclic nucleotide–gated channel SthK

    doi: 10.1085/jgp.201812023

    Figure Lengend Snippet: Characterization of SthK channel activity. (A) Normalized 86 Rb + flux through SthK (reconstituted in 5:3:2 DOPC:POPG:cardiolipin) in the presence of 200 µM cAMP (red squares), cGMP (blue circles), both cAMP and cGMP (black triangles), and without cyclic nucleotides (open triangles). Flux through empty liposomes (open circles) is shown as a reference. All flux values are normalized to the maximum uptake recorded in the presence of valinomycin. Bars represent means ± SEM for three separate experiments. (B) SthK channel activity represented by the maximum achieved 86 Rb + uptake through SthK reconstituted in liposomes made from 3:1 POPE:POPG (PE:PG) or 5:3:2 DOPC:POPG:cardiolipin (PC:PG:CA), as indicated, in the presence of 200 µM cAMP. Bars represent means ± SEM for three separate experiments. (C) Representative single-channel recordings of SthK in 0.1 mM intracellular cAMP. (D) I-V relationship of SthK single-channel current amplitude at 100 µM cAMP. (E) Open probability of SthK at 100 mV as a function of the cAMP concentration. Fitting the data with Eq. 10 yields an apparent activation constant of EC 50 = 17 µM and a Hill coefficient of n H = 3. The number of repeats is indicated beside each data point. (F) Open probability of SthK in the presence of 500 µM cAMP as function of the membrane potential. The line indicates the fit according to Eq. 13 , leading to z = 0.8 and V half = 87 mV, Po max = 0.65, and Po min = 0.05. Symbols and error bars in D–F represent means ± SEM from at least three separate bilayers.

    Article Snippet: To reconstitute SthK into liposomes, DOPC, POPG, and cardiolipin (Avanti Polar Lipids), dissolved in chloroform, were mixed in a 5:3:2 (wt/wt/wt) ratio and dried under constant N2 flow in disposable glass tubes to a thin layer.

    Techniques: Activity Assay, Concentration Assay, Activation Assay

    Raman spectra in the region of 1620–1700 cm −1 for CerPE ( red ) and three mixtures of CerPE/DOPC (1:1) ( blue ), CerPE /DPPC (1:1) ( green ), and CerPE/Chol (1:1) ( black ). The Raman spectrum was collected 25 h after sample deposition at 23°C.

    Journal: Biophysical Journal

    Article Title: Detection of Sphingomyelin Clusters by Raman Spectroscopy

    doi: 10.1016/j.bpj.2016.07.035

    Figure Lengend Snippet: Raman spectra in the region of 1620–1700 cm −1 for CerPE ( red ) and three mixtures of CerPE/DOPC (1:1) ( blue ), CerPE /DPPC (1:1) ( green ), and CerPE/Chol (1:1) ( black ). The Raman spectrum was collected 25 h after sample deposition at 23°C.

    Article Snippet: We purchased SM (egg, chicken; egg SM; > 80% of the amide-linked fatty acid of egg SM is palmitic acid according to the manufacturer), DPPC, DOPC, N -lauroyl-D- erythro -sphingosylphosphorylcholine (lauroyl SM), N -stearoyl-D- erythro -sphingosylphosphorylcholine (stearoyl SM), and N -palmitoyl-d31-D- erythro -sphingosylphosphorylcholine (d31 SM) from Avanti Polar Lipids (Alabaster, AL); Chol from Sigma (St. Louis, MO); and N -Acyl-sphingosylphosphorylethanolamine (CerPE) from Matreya LLC (Pleasant Gap, PA).

    Techniques:

    Raman spectra of various lipid suspensions. ( A ) Raman spectra of egg SM, egg SM/DOPC (1:1), egg SM/DPPC (1:1), DOPC, and DPPC. ( B ) Raman spectra of the 1620–1720 cm −1 region for egg SM ( red ), egg SM/DOPC (1:1) ( blue ), and egg SM/DPPC (1:1) ( black ). ( C ) Concentration dependence of the relative intensities of the trans C=C stretching band ( circle ) and the amide I band ( square ) for a 1:1 mixture of egg SM and DOPC. ( D ) Concentration dependence of the relative intensities of the trans C=C stretching band ( circle ) and the amide I band ( square ) for a 1:1 mixture of egg SM and DPPC. The Raman spectrum was collected 25 h after sample deposition at 23°C.

    Journal: Biophysical Journal

    Article Title: Detection of Sphingomyelin Clusters by Raman Spectroscopy

    doi: 10.1016/j.bpj.2016.07.035

    Figure Lengend Snippet: Raman spectra of various lipid suspensions. ( A ) Raman spectra of egg SM, egg SM/DOPC (1:1), egg SM/DPPC (1:1), DOPC, and DPPC. ( B ) Raman spectra of the 1620–1720 cm −1 region for egg SM ( red ), egg SM/DOPC (1:1) ( blue ), and egg SM/DPPC (1:1) ( black ). ( C ) Concentration dependence of the relative intensities of the trans C=C stretching band ( circle ) and the amide I band ( square ) for a 1:1 mixture of egg SM and DOPC. ( D ) Concentration dependence of the relative intensities of the trans C=C stretching band ( circle ) and the amide I band ( square ) for a 1:1 mixture of egg SM and DPPC. The Raman spectrum was collected 25 h after sample deposition at 23°C.

    Article Snippet: We purchased SM (egg, chicken; egg SM; > 80% of the amide-linked fatty acid of egg SM is palmitic acid according to the manufacturer), DPPC, DOPC, N -lauroyl-D- erythro -sphingosylphosphorylcholine (lauroyl SM), N -stearoyl-D- erythro -sphingosylphosphorylcholine (stearoyl SM), and N -palmitoyl-d31-D- erythro -sphingosylphosphorylcholine (d31 SM) from Avanti Polar Lipids (Alabaster, AL); Chol from Sigma (St. Louis, MO); and N -Acyl-sphingosylphosphorylethanolamine (CerPE) from Matreya LLC (Pleasant Gap, PA).

    Techniques: Concentration Assay

    Pre-proccesing of spectra and selection of appropriate wavelengths . A) Raw fluorescence emission spectra of various AChR-free liposomes with varying molar ratios of DOPA/DOPC (ranging from 0 to 60%) and two AChR-containing liposomes with DOPA/DOPC (20:40). Two replicas from independent experiments are shown. In all samples, NBD-Chol and PyPC concentrations were kept at 40 and 5%, respectively. The final lipid concentration and the lipid to protein molar ratio in the AChR-containing liposomes were 40 μM and 500:1, respectively. Excitation wavelength = 340 nm. Temperature = 25°C. B) Pre-processed spectra obtained by smoothing throughout the Savitsky-Golay procedure (with a window width of 8 points and a second order polynomial fit) and normalizing to the highest value of each spectrum (corresponding to the first PyPC emission band at 374 nm). The wavelengths further employed for the multivariate analysis are outlined in the dotted rectangle. It is clear that the sixteen spectra in each panel are difficult to identify due to their high degree of overlap; this is precisely what multivariate analysis dissects so effectively. Where possible, spectra have been identified with the sample numbers appearing in Table 1 .

    Journal: PMC Biophysics

    Article Title: Resolution of complex fluorescence spectra of lipids and nicotinic acetylcholine receptor by multivariate analysis reveals protein-mediated effects on the receptor's immediate lipid microenvironment

    doi: 10.1186/1757-5036-1-6

    Figure Lengend Snippet: Pre-proccesing of spectra and selection of appropriate wavelengths . A) Raw fluorescence emission spectra of various AChR-free liposomes with varying molar ratios of DOPA/DOPC (ranging from 0 to 60%) and two AChR-containing liposomes with DOPA/DOPC (20:40). Two replicas from independent experiments are shown. In all samples, NBD-Chol and PyPC concentrations were kept at 40 and 5%, respectively. The final lipid concentration and the lipid to protein molar ratio in the AChR-containing liposomes were 40 μM and 500:1, respectively. Excitation wavelength = 340 nm. Temperature = 25°C. B) Pre-processed spectra obtained by smoothing throughout the Savitsky-Golay procedure (with a window width of 8 points and a second order polynomial fit) and normalizing to the highest value of each spectrum (corresponding to the first PyPC emission band at 374 nm). The wavelengths further employed for the multivariate analysis are outlined in the dotted rectangle. It is clear that the sixteen spectra in each panel are difficult to identify due to their high degree of overlap; this is precisely what multivariate analysis dissects so effectively. Where possible, spectra have been identified with the sample numbers appearing in Table 1 .

    Article Snippet: DOPA, DOPC and Chol were obtained from Avanti Polar Lipids, Inc (Alabaster, AL).

    Techniques: Selection, Fluorescence, Concentration Assay

    Förster resonance energy transfer (FRET) from the AChR . Smoothened fluorescence emission spectrum of an AChR PyPC-containing sample at 25°C showing the areas (A1 and A2) used to evaluate FRET. The dotted line indicates the average boundary wavelength at which the absolute value of the first derivative of the spectrum passed through a minimum. Excitation wavelength = 290 nm. Inset: FRET from AChR to PyPC as a function of temperature. FRET was calculated according to [1-(A 1 /A 2 )]. Liposomes contained DOPA/DOPC/NBD-Chol at a molar fraction 20/40/40 and a lipid to protein molar ratio of 500:1. PyPC concentration was 5 mol%. Error bars represent the S.D. of two independent samples.

    Journal: PMC Biophysics

    Article Title: Resolution of complex fluorescence spectra of lipids and nicotinic acetylcholine receptor by multivariate analysis reveals protein-mediated effects on the receptor's immediate lipid microenvironment

    doi: 10.1186/1757-5036-1-6

    Figure Lengend Snippet: Förster resonance energy transfer (FRET) from the AChR . Smoothened fluorescence emission spectrum of an AChR PyPC-containing sample at 25°C showing the areas (A1 and A2) used to evaluate FRET. The dotted line indicates the average boundary wavelength at which the absolute value of the first derivative of the spectrum passed through a minimum. Excitation wavelength = 290 nm. Inset: FRET from AChR to PyPC as a function of temperature. FRET was calculated according to [1-(A 1 /A 2 )]. Liposomes contained DOPA/DOPC/NBD-Chol at a molar fraction 20/40/40 and a lipid to protein molar ratio of 500:1. PyPC concentration was 5 mol%. Error bars represent the S.D. of two independent samples.

    Article Snippet: DOPA, DOPC and Chol were obtained from Avanti Polar Lipids, Inc (Alabaster, AL).

    Techniques: Förster Resonance Energy Transfer, Fluorescence, Concentration Assay

    Build-up of Lateral Compression in Snf7 Spirals by Polymerization (A) HS-AFM images of Snf7 spirals acquiring polygonal shapes with time. (B) AFM Topography and nanomechanical mapping of polygonal Snf7 spirals. A significant proportion of spirals (dashed outlines) have a lower center with increased mechanical stiffness. (C) Snf7 polymerization on GUVs made of DOPC 60% / DOPS 40% + Rhodamine-PE 0.1% (red), 0.003% DOPE-Peg2000-Biotin. GUVs are incubated with 500 nM Snf7-Alexa488 (green). Top: SDC images of a GUV equatorial plane during Snf7 polymerization. Bottom: fluorescence intensity (equatorial plane) of 4 GUVs with time. (D) GUVs before (top) and after (bottom) several hours of incubation with Snf7-Alexa488. (E) Snf7 coated GUVs keep the aspirated shape after release from the micropipette. (F) Sketch of membrane stretching by Snf7 spiral compression. (G) Schematic of the membrane tension measurement setup combining holding pipette, injection pipette, bead within an optical trap, giant vesicle (red) and Snf7 (green). (H) Top image: SDC image of a membrane tension measurement experiment (red = membrane, green = Snf7-Alexa488). Note that Snf7-Alexa488 did not polymerize on the membrane nanotube. Bottom: brightfield image of the same vesicle. The yellow cross indicates the resting position of the bead held by the optical trap. (I) Top: Normalized Snf7 fluorescence intensity versus time (measured from equatorial plane); bottom: force exerted by the membrane nanotube on the bead versus time. See also Figure S5 .

    Journal: Cell

    Article Title: Relaxation of Loaded ESCRT-III Spiral Springs Drives Membrane Deformation

    doi: 10.1016/j.cell.2015.10.017

    Figure Lengend Snippet: Build-up of Lateral Compression in Snf7 Spirals by Polymerization (A) HS-AFM images of Snf7 spirals acquiring polygonal shapes with time. (B) AFM Topography and nanomechanical mapping of polygonal Snf7 spirals. A significant proportion of spirals (dashed outlines) have a lower center with increased mechanical stiffness. (C) Snf7 polymerization on GUVs made of DOPC 60% / DOPS 40% + Rhodamine-PE 0.1% (red), 0.003% DOPE-Peg2000-Biotin. GUVs are incubated with 500 nM Snf7-Alexa488 (green). Top: SDC images of a GUV equatorial plane during Snf7 polymerization. Bottom: fluorescence intensity (equatorial plane) of 4 GUVs with time. (D) GUVs before (top) and after (bottom) several hours of incubation with Snf7-Alexa488. (E) Snf7 coated GUVs keep the aspirated shape after release from the micropipette. (F) Sketch of membrane stretching by Snf7 spiral compression. (G) Schematic of the membrane tension measurement setup combining holding pipette, injection pipette, bead within an optical trap, giant vesicle (red) and Snf7 (green). (H) Top image: SDC image of a membrane tension measurement experiment (red = membrane, green = Snf7-Alexa488). Note that Snf7-Alexa488 did not polymerize on the membrane nanotube. Bottom: brightfield image of the same vesicle. The yellow cross indicates the resting position of the bead held by the optical trap. (I) Top: Normalized Snf7 fluorescence intensity versus time (measured from equatorial plane); bottom: force exerted by the membrane nanotube on the bead versus time. See also Figure S5 .

    Article Snippet: Giant Unilamellar Vesicles and Large Unilamellar Vesicles Preparation GUVs were prepared by electroformation using DOPC and DOPS mixtures, purchased from Avanti Polar Lipids (Alabaster, USA).

    Techniques: Incubation, Fluorescence, Transferring, Injection

    Nucleation and Disruption of Snf7, Related to Figure 4 All images are acquired with TIRF Microcopy. (A) Control of Snf7 polymerization induced by ESCRT-II and Vps20 proteins. Kymograph of a membrane slice over time. Fluorescents dots appear as lines when Snf7 nuclei are polymerized. Lines appear only when both Vps20 and ESCRT-II are present (both kymograph, lower panel). Snf7 and Vps20 without ESCRT-II (left kymograph middle panel) as well as Snf7 and ESCRT-II without Vps20 (right kymograph middle panel) do not nucleate Snf7 filaments. (B) Photobleaching induces breaks in Snf7 dotted structures. Snf7 dots are formed by incubation of Snf7 at 300 nM for 1 hr on DOPC 60% /DOPS 40% membrane. Snf7 is then washed out. Snf7 dots are subsequently imaged at a high frequency (1 fps) and under long exposure time and high laser power. When an antibleaching solution (AB) is present in the chamber, the dots remain intact (first and second image). However 5 min and 15 min after the antibleaching solution is washed out (third and fourth image), dots are disrupted into wider structures showing multiple maxima (see 2 × 2 μm insets for details). Structures located outside the imaged field of view are not affected by the removal of the antibleaching solution. (C) Photobleaching triggers patch formation from Snf7 dots. Compared to (B), Snf7 is maintained in the chamber at 300 nM throughout the experiment. In this case, the removal of the antibleaching solution (Snf7 - AB point of the kymograph) synchronously triggers the transition from Snf7 dots to patches. (D) Histogram of the Snf7 filament radius distribution after nanodissection (total of three experiments, see Figure 4 D).

    Journal: Cell

    Article Title: Relaxation of Loaded ESCRT-III Spiral Springs Drives Membrane Deformation

    doi: 10.1016/j.cell.2015.10.017

    Figure Lengend Snippet: Nucleation and Disruption of Snf7, Related to Figure 4 All images are acquired with TIRF Microcopy. (A) Control of Snf7 polymerization induced by ESCRT-II and Vps20 proteins. Kymograph of a membrane slice over time. Fluorescents dots appear as lines when Snf7 nuclei are polymerized. Lines appear only when both Vps20 and ESCRT-II are present (both kymograph, lower panel). Snf7 and Vps20 without ESCRT-II (left kymograph middle panel) as well as Snf7 and ESCRT-II without Vps20 (right kymograph middle panel) do not nucleate Snf7 filaments. (B) Photobleaching induces breaks in Snf7 dotted structures. Snf7 dots are formed by incubation of Snf7 at 300 nM for 1 hr on DOPC 60% /DOPS 40% membrane. Snf7 is then washed out. Snf7 dots are subsequently imaged at a high frequency (1 fps) and under long exposure time and high laser power. When an antibleaching solution (AB) is present in the chamber, the dots remain intact (first and second image). However 5 min and 15 min after the antibleaching solution is washed out (third and fourth image), dots are disrupted into wider structures showing multiple maxima (see 2 × 2 μm insets for details). Structures located outside the imaged field of view are not affected by the removal of the antibleaching solution. (C) Photobleaching triggers patch formation from Snf7 dots. Compared to (B), Snf7 is maintained in the chamber at 300 nM throughout the experiment. In this case, the removal of the antibleaching solution (Snf7 - AB point of the kymograph) synchronously triggers the transition from Snf7 dots to patches. (D) Histogram of the Snf7 filament radius distribution after nanodissection (total of three experiments, see Figure 4 D).

    Article Snippet: Giant Unilamellar Vesicles and Large Unilamellar Vesicles Preparation GUVs were prepared by electroformation using DOPC and DOPS mixtures, purchased from Avanti Polar Lipids (Alabaster, USA).

    Techniques: Incubation

    Using GUVs to Study Snf7 Mechanics, Related to Figure 5 (A) Partially adhered GUVs within a flow chamber. Top left: experimental setup to follow partially adhered vesicles within a flow chamber. A coverslip (blue-gray) is coated with avidin (orange) by adsorption. GUVs (red) containing peg-biotin lipids (black arrows) are flowed within the chamber and attach to the glass surface. Passivation of the surface is then made by flowing biotinylated bsa, allowing to keep for long time partially adhered vesicles. Bottom left: GUVs images taken at the coverslip surface showing the adhesion patch of vesicles. Bottom middle: equatorial section of GUVs. Side images: Y-Z and X-Z sections (dashed line) reconstructed from Z optical sections. (B) Comparison between patch coverage dynamics and GUV coverage dynamics. Gray: dynamics equals to the average of 4 GUVs shown Figure 5 C. Orange: equivalent to graphs shown Figure S1 E for [Snf7] = 500 nM. The initial dynamics is steeper for Snf7 patches but the saturation dynamics is similar. (C) Comparison of the dynamics of surface coverage between GUVs experiments and the mathematical modeling. Orange: dynamics equals to the average of 4 GUVs shown Figure 5 C. Gray: result of the mathematical modeling for [Snf7] = 500 nM ( w = 40 nm 2 .s −1 and λ = 8.2 × 10 −3 spiral.μm −1 .s −1 ). (D) Plastic behavior of strongly coated vesicle, another example of Figure 5 E. A round shaped vesicle is being held gently by a pipette (left), then a suction pressure is exerted (middle) to deform the vesicle. Upon pressure release (right), the vesicle keeps the shape of the pipette. (E) Membrane bending rigidity (κ) measurement of a DOPC 60% / DOPS 40% vesicle. Plot of the tether force squared as a function of experimentally imposed membrane tension for the vesicle shown in Figure 5 H and 5I. The variation is linear with an expected slope of 8π 2 κ. The linear fit yields the bending rigidity κ = 12 k b T = 4.8 × 10 − 20 J.

    Journal: Cell

    Article Title: Relaxation of Loaded ESCRT-III Spiral Springs Drives Membrane Deformation

    doi: 10.1016/j.cell.2015.10.017

    Figure Lengend Snippet: Using GUVs to Study Snf7 Mechanics, Related to Figure 5 (A) Partially adhered GUVs within a flow chamber. Top left: experimental setup to follow partially adhered vesicles within a flow chamber. A coverslip (blue-gray) is coated with avidin (orange) by adsorption. GUVs (red) containing peg-biotin lipids (black arrows) are flowed within the chamber and attach to the glass surface. Passivation of the surface is then made by flowing biotinylated bsa, allowing to keep for long time partially adhered vesicles. Bottom left: GUVs images taken at the coverslip surface showing the adhesion patch of vesicles. Bottom middle: equatorial section of GUVs. Side images: Y-Z and X-Z sections (dashed line) reconstructed from Z optical sections. (B) Comparison between patch coverage dynamics and GUV coverage dynamics. Gray: dynamics equals to the average of 4 GUVs shown Figure 5 C. Orange: equivalent to graphs shown Figure S1 E for [Snf7] = 500 nM. The initial dynamics is steeper for Snf7 patches but the saturation dynamics is similar. (C) Comparison of the dynamics of surface coverage between GUVs experiments and the mathematical modeling. Orange: dynamics equals to the average of 4 GUVs shown Figure 5 C. Gray: result of the mathematical modeling for [Snf7] = 500 nM ( w = 40 nm 2 .s −1 and λ = 8.2 × 10 −3 spiral.μm −1 .s −1 ). (D) Plastic behavior of strongly coated vesicle, another example of Figure 5 E. A round shaped vesicle is being held gently by a pipette (left), then a suction pressure is exerted (middle) to deform the vesicle. Upon pressure release (right), the vesicle keeps the shape of the pipette. (E) Membrane bending rigidity (κ) measurement of a DOPC 60% / DOPS 40% vesicle. Plot of the tether force squared as a function of experimentally imposed membrane tension for the vesicle shown in Figure 5 H and 5I. The variation is linear with an expected slope of 8π 2 κ. The linear fit yields the bending rigidity κ = 12 k b T = 4.8 × 10 − 20 J.

    Article Snippet: Giant Unilamellar Vesicles and Large Unilamellar Vesicles Preparation GUVs were prepared by electroformation using DOPC and DOPS mixtures, purchased from Avanti Polar Lipids (Alabaster, USA).

    Techniques: Flow Cytometry, Avidin-Biotin Assay, Adsorption, Transferring

    Dynamics of Snf7 Patches on Supported Membranes, Related to Figure 1 (A) GUV bursting on glass coverslip. Left: GUV before bursting. A strongly adhered GUV, labeled with Rhodamine-PE, is visualized by spinning-disk confocal microscopy. The focus is made on the bottom of the vesicle, showing the circular patch of adhesion. Below is the 3D sketch showing the strongly adhered vesicle. Right: Same vesicle shortly after bursting occurred and corresponding sketch. See also Movie S1 . (B) Spontaneous Snf7 patch depolymerization after Snf7 washout in solution. The curves represent different locations where depolymerization is measured. See also Movie S3 . (C) Patch nucleation rate as a function of [Snf7] for a DOPC 60% / DOPS 40% membrane (blue curve) and for a DOPC 80% / DOPS 20% membrane (orange curve). (D) Patch radial growth speed as a function of [Snf7] for a DOPC 60% / DOPS 40% membrane (blue curve) and for a DOPC 80% / DOPS 20% membrane (orange curve). Lines are linear fit with the slope equals to 760 nm.min −1 .μM −1 (blue) and 150 nm.min −1 .μM −1 (orange). (E) Fluorescence intensity curve (average of 5 patches) with time at a given point on the membrane upon coverage by a Snf7 patch, for [Snf7] = 100 nM (thin gray line), 200 nM (orange line), 400 nM (thick gray line). (F) Same curves as (E) plotted as a function of time multiplied by Snf7 concentration in μM. All graphs merge on one single master curve, revealing that the coverage dynamics is proportional to Snf7 bulk concentration.

    Journal: Cell

    Article Title: Relaxation of Loaded ESCRT-III Spiral Springs Drives Membrane Deformation

    doi: 10.1016/j.cell.2015.10.017

    Figure Lengend Snippet: Dynamics of Snf7 Patches on Supported Membranes, Related to Figure 1 (A) GUV bursting on glass coverslip. Left: GUV before bursting. A strongly adhered GUV, labeled with Rhodamine-PE, is visualized by spinning-disk confocal microscopy. The focus is made on the bottom of the vesicle, showing the circular patch of adhesion. Below is the 3D sketch showing the strongly adhered vesicle. Right: Same vesicle shortly after bursting occurred and corresponding sketch. See also Movie S1 . (B) Spontaneous Snf7 patch depolymerization after Snf7 washout in solution. The curves represent different locations where depolymerization is measured. See also Movie S3 . (C) Patch nucleation rate as a function of [Snf7] for a DOPC 60% / DOPS 40% membrane (blue curve) and for a DOPC 80% / DOPS 20% membrane (orange curve). (D) Patch radial growth speed as a function of [Snf7] for a DOPC 60% / DOPS 40% membrane (blue curve) and for a DOPC 80% / DOPS 20% membrane (orange curve). Lines are linear fit with the slope equals to 760 nm.min −1 .μM −1 (blue) and 150 nm.min −1 .μM −1 (orange). (E) Fluorescence intensity curve (average of 5 patches) with time at a given point on the membrane upon coverage by a Snf7 patch, for [Snf7] = 100 nM (thin gray line), 200 nM (orange line), 400 nM (thick gray line). (F) Same curves as (E) plotted as a function of time multiplied by Snf7 concentration in μM. All graphs merge on one single master curve, revealing that the coverage dynamics is proportional to Snf7 bulk concentration.

    Article Snippet: Giant Unilamellar Vesicles and Large Unilamellar Vesicles Preparation GUVs were prepared by electroformation using DOPC and DOPS mixtures, purchased from Avanti Polar Lipids (Alabaster, USA).

    Techniques: Labeling, Confocal Microscopy, Fluorescence, Concentration Assay

    Nucleation and Growth of Snf7 Patches on Supported Membranes Lipid composition is DOPC 60% / DOPS 40%+ Rhodamine PE 0.1%. (A) Time-lapse images of Snf7-Alexa488 patches growth (green) at [Snf7] = 400 nM on supported membrane (gray). (B) Time-lapse images (every 10 min) of a single Snf7-Alexa488 patch (green) growing at [Snf7] = 200 nM. (C) Patch nucleation rate as a function of [Snf7]. (D) Successive (from bright to dark green, every 10 min) Snf7 patch fluorescence profiles (circularly averaged) at [Snf7] = 200 nM. (E) Snf7 patch edge fluorescence profile (average of 3 patches) as a function of [Snf7] (data for [Snf7]

    Journal: Cell

    Article Title: Relaxation of Loaded ESCRT-III Spiral Springs Drives Membrane Deformation

    doi: 10.1016/j.cell.2015.10.017

    Figure Lengend Snippet: Nucleation and Growth of Snf7 Patches on Supported Membranes Lipid composition is DOPC 60% / DOPS 40%+ Rhodamine PE 0.1%. (A) Time-lapse images of Snf7-Alexa488 patches growth (green) at [Snf7] = 400 nM on supported membrane (gray). (B) Time-lapse images (every 10 min) of a single Snf7-Alexa488 patch (green) growing at [Snf7] = 200 nM. (C) Patch nucleation rate as a function of [Snf7]. (D) Successive (from bright to dark green, every 10 min) Snf7 patch fluorescence profiles (circularly averaged) at [Snf7] = 200 nM. (E) Snf7 patch edge fluorescence profile (average of 3 patches) as a function of [Snf7] (data for [Snf7]

    Article Snippet: Giant Unilamellar Vesicles and Large Unilamellar Vesicles Preparation GUVs were prepared by electroformation using DOPC and DOPS mixtures, purchased from Avanti Polar Lipids (Alabaster, USA).

    Techniques: Fluorescence