Search results for "LIPOSOMES"

showing 10 items of 221 documents

Fluidity of liposome membranes doped with metalloporphyrins: An ESR study

2008

Changes in membrane fluidity of porphyrin-doped liposomes have been investigated to assess the kinetics of the fluidization process. Metal complexes of tert-butylphenyl mesosubstituted porphyrin, containing ions of Mg, Mn, Fe, Co, Ni and Cu, were used as dopants. Liposomes were obtained by sonication of hen egg yolk lecithin (EYL). Electron paramagnetic resonance (ESR) was applied using two spin probes, TEMPO (2,2,6,6-tetramethylpiperidine- 1-oxyl) and 16-DOXYL-stearic acid [2-ethyl-2-(15-methoxy-15-oxopentadecyl)-4,4- dimethyl-3-oxazolidinyloxyl], localized at different sites within the membrane to determine the spectroscopic parameters: partition (F) and rotation correlation time (τ), rel…

Models MolecularMembrane FluidityMetalloporphyrinsSonicationInorganic chemistryKineticsMolecular ConformationGeneral Biochemistry Genetics and Molecular Biologylaw.inventionEYL LiposomesMetalCyclic N-Oxideschemistry.chemical_compoundlawMembrane fluidityElectron paramagnetic resonanceESRLiposomeChemistryElectron Spin Resonance SpectroscopyPorphyrinKineticsMembranevisual_artLiposomesvisual_art.visual_art_mediumSpin Labels
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Pore Formation by a Bax-Derived Peptide: Effect on the Line Tension of the Membrane Probed by AFM

2007

AbstractBax is a critical regulator of physiological cell death that increases the permeability of the outer mitochondrial membrane and facilitates the release of the so-called apoptotic factors during apoptosis. The molecular mechanism of action is unknown, but it probably involves the formation of partially lipidic pores induced by Bax. To investigate the interaction of Bax with lipid membranes and the physical changes underlying the formation of Bax pores, we used an active peptide derived from helix 5 of this protein (Bax-α5) that is able to induce Bax-like pores in lipid bilayers. We report the decrease of line tension due to peptide binding both at the domain interface in phase-separa…

Models MolecularMembrane FluidityProtein ConformationLipid BilayersBiophysicsPeptide bindingPeptideMicroscopy Atomic ForceProtein structureBcl-2-associated X proteinMembrane fluiditySurface TensionComputer SimulationLipid bilayerbcl-2-Associated X Proteinchemistry.chemical_classificationLiposomeMembranesbiologyChemistryCell biologyMembraneModels ChemicalLiposomesbiology.proteinPorosityBiophysical Journal
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Peptides Derived from Apoptotic Bax and Bid Reproduce the Poration Activity of the Parent Full-Length Proteins

2005

Bax and Bid are proapoptotic proteins of the Bcl-2 family that regulate the release of apoptogenic factors from mitochondria. Although they localize constitutively in the cytoplasm, their apoptotic function is exerted at the mitochondrial outer membrane, and is related to their ability to form transbilayer pores. Here we report the poration activity of fragments from these two proteins, containing the first alpha-helix of a colicinlike hydrophobic hairpin (alpha-helix 5 of Bax and alpha-helix 6 of Bid). Both peptides readily bind to synthetic lipid vesicles, where they adopt predominantly alpha-helical structures and induce the release of entrapped calcein. In planar lipid membranes they fo…

Models MolecularMolecular Sequence DataBiophysicsApoptosisPeptideIn Vitro TechniquesBiophysical PhenomenaIon ChannelsPermeabilityProtein Structure Secondarychemistry.chemical_compoundBcl-2-associated X proteinSpectroscopy Fourier Transform InfraredHumansChannels Receptors and Electrical SignalingAmino Acid SequencePeptide sequenceIon channelbcl-2-Associated X Proteinchemistry.chemical_classificationbiologyChemistryCircular DichroismPeptide FragmentsCell biologyCalceinMembraneProto-Oncogene Proteins c-bcl-2CytoplasmMultiprotein ComplexesLiposomesbiology.proteinPèptidsCarrier ProteinsBacterial outer membraneProteïnesBH3 Interacting Domain Death Agonist ProteinBiophysical Journal
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Metalloporphyrin intercalation in liposome membranes: ESR study

2010

Liposomes characterized by membranes featuring diverse fluidity (liquid-crystalline and/or gel phase), prepared from egg yolk lecithin (EYL) and dipalmitoylphosphatidylcholine (DPPC), were doped with selected metalloporphyrins and the time-related structural and dynamic changes within the lipid double layer were investigated. Porphyrin complexes of Mg(II), Mn(III), Fe(III), Co(II), Ni(II), Cu(II), Zn(II), and the metal-free base were embedded into the particular liposome systems and tested for 350 h at 24°C using the electron spin resonance (ESR) spin probe technique. 5-DOXYL, 12-DOXYL, and 16-DOXYL stearic acid methyl ester spin labels were applied to explore the interior of the lipid bila…

Models MolecularOriginal PaperLiposomeMolecular StructureMetalloporphyrinsIntercalation (chemistry)Electron Spin Resonance SpectroscopyPorphyrinBiochemistryLipid bilayerSpin probeInorganic Chemistrychemistry.chemical_compoundCrystallographyMembranechemistryElectron spin resonanceDipalmitoylphosphatidylcholineLiposomesDensity functional theory calculationsOrganic chemistrylipids (amino acids peptides and proteins)Lipid bilayer phase behaviorLipid bilayerJBIC Journal of Biological Inorganic Chemistry
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Dynamics of surface of lipid membranes: theoretical considerations and the ESR experiment.

2016

The effect of the surface layer of model membranes on their physical properties was discussed in this paper. The research involved a physical ESR experiment with the use of spin probes and computer simulation based on the Monte Carlo technique. Liposomes formed during the process of sonication of lecithin were scanned in an ESR spectrometer. The membrane surface layer model, represented by the system of electric dipoles arranged in rectangular or hexagonal matrices, was studied. The final states of computer simulations were presented as textures. It was found that in the gel phase some ordered domain structures are formed, while in the liquid–crystal phase we got complex textures comprising…

Models MolecularPhase transition12-DipalmitoylphosphatidylcholineSurface PropertiesMonte Carlo methodBiophysicsAnalytical chemistryMolecular Conformation02 engineering and technologyPhase Transition03 medical and health sciencesSonication0302 clinical medicinePhase (matter)Lipid membraneSurface layerMembrane fluidityLipid bilayerMonte Carlo simulationChemistryCell MembraneElectron Spin Resonance SpectroscopyTemperatureGeneral MedicineHydrogen-Ion ConcentrationESR probe021001 nanoscience & nanotechnologyElectric dipole momentDipoleKineticsMembraneChemical physics030220 oncology & carcinogenesisLiposomesOriginal Article0210 nano-technologyMonte Carlo MethodEuropean biophysics journal : EBJ
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2NH and 3OH are crucial structural requirements in sphingomyelin for sticholysin II binding and pore formation in bilayer membranes.

2013

AbstractSticholysin II (StnII) is a pore-forming toxin from the sea anemone Stichodactyla heliantus which belongs to the large actinoporin family. The toxin binds to sphingomyelin (SM) containing membranes, and shows high binding specificity for this lipid. In this study, we have examined the role of the hydrogen bonding groups of the SM long-chain base (i.e., the 2NH and the 3OH) for StnII recognition. We prepared methylated SM-analogs which had reduced hydrogen bonding capability from 2NH and 3OH. Both surface plasmon resonance experiments, and isothermal titration calorimetry measurements indicated that StnII failed to bind to bilayers containing methylated SM-analogs, whereas clear bind…

Models MolecularPore Forming Cytotoxic ProteinsMembrane permeabilizationLipid BilayersBiophysicsCalorimetryta3111Biochemistrychemistry.chemical_compoundCnidarian VenomsAnimalsComputer SimulationLipid bilayerta116Binding selectivityUnilamellar LiposomesPhosphocholineBinding SitesMolecular StructureChemistryHydrogen bondVesicleta1182Isothermal titration calorimetryHydrogen BondingCell BiologySurface Plasmon ResonanceProtein Structure TertiarySphingomyelinsKineticsMembraneSea AnemonesBiochemistryMolecular dockingIsothermal titration calorimetryBiophysicsPhosphatidylcholinesSphingomyelinProtein BindingBiochimica et biophysica acta
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Interaction of Heparins and Dextran Sulfates with a Mesoscopic Protein Nanopore

2009

A mechanism of how polyanions influence the channel formed by Staphylococcus aureus alpha-hemolysin is described. We demonstrate that the probability of several types of polyanions to block the ion channel depends on the presence of divalent cations and the polyanion molecular weight and concentration. For heparins, a 10-fold increase in molecular weight decreases the half-maximal inhibitory concentration, IC(50), nearly 10(4)-fold. Dextran sulfates were less effective at blocking the channel. The polyanions are significantly more effective at reducing the conductance when added to the trans side of this channel. Lastly, the effectiveness of heparins on the channel conductance correlated wi…

Models MolecularStereochemistryBacterial ToxinsLipid BilayersMolecular ConformationBiophysicsmacromolecular substancesDivalentIonchemistry.chemical_compoundHemolysin ProteinsCysteineChannels and TransportersLipid bilayerIon channelchemistry.chemical_classificationMesoscopic physicsHeparinCell MembraneElectric Conductivitytechnology industry and agricultureConductanceDextransNanostructuresNanoporeDextranchemistryLiposomesMutationBiophysicsPorosityProtein BindingBiophysical Journal
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Quenching of fluorescein-conjugated lipids by antibodies. Quantitative recognition and binding of lipid-bound haptens in biomembrane models, formatio…

1992

Three model biomembrane systems, monolayers, micelles, and vesicles, have been used to study the influence of chemical and physical variables of hapten presentation at membrane interfaces on antibody binding. Hapten recognition and binding were monitored for the anti-fluorescein monoclonal antibody 4–4-20 generated against the hapten, fluorescein, in these membrane models as a function of fluorescein-conjugated lipid architecture. Specific recognition and binding in this system are conveniently monitored by quenching of fluorescein emission upon penetration of fluorescein into the antibody's active site. Lipid structure was shown to play a large role in affecting antibody quenching. Interes…

Models MolecularTime FactorsProtein ConformationStereochemistry030303 biophysicsMolecular ConformationBiophysicsModels BiologicalMice03 medical and health scienceschemistry.chemical_compoundAnimalsFluoresceinBinding siteLipid bilayerMicellesPhospholipids030304 developmental biologyPhosphatidylethanolamine0303 health sciencesLiposomeVesicleCell MembraneAntibodies MonoclonalMembranes ArtificialBiological membraneFluoresceinsKineticsSpectrometry FluorescencechemistryLiposomeslipids (amino acids peptides and proteins)Binding Sites AntibodyHaptensHaptenResearch ArticleBiophysical Journal
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The impact of model peptides on structural and dynamic properties of egg yolk lecithin liposomes - experimental and DFT studies.

2015

Electron spin resonance (ESR), 1H-NMR, voltage and resistance experiments were performed to explore structural and dynamic changes of Egg Yolk Lecithin (EYL) bilayer upon addition of model peptides. Two of them are phenylalanine (Phe) derivatives, Ac-Phe-NHMe (1) and Ac-Phe-NMe2 (2), and the third one, Ac-(Z)-ΔPhe-NMe2 (3), is a derivative of (Z)-α,β-dehydrophenylalanine. The ESR results revealed that all compounds reduced the fluidity of liposome's membrane, and the highest activity was observed for compound 2 with N-methylated C-terminal amide bond (Ac-Phe-NMe2). This compound, being the most hydrophobic, penetrates easily through biological membranes. This was also observed in voltage an…

Models Molecularfood.ingredientBioengineeringBiochemistryLecithinlaw.inventionfoodlawLecithinsOrganic chemistryPeptide bondElectron paramagnetic resonanceMolecular BiologyLiposomeMolecular StructureChemistryBilayerBiological membraneGeneral ChemistryGeneral MedicineNuclear magnetic resonance spectroscopyEgg YolkCrystallographyMembraneLiposomesMolecular MedicineQuantum TheoryThermodynamicsPeptidesChemistrybiodiversity
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Effect of tin and lead chlorotriphenyl analogues on selected living cells.

2010

Three kinds of living cells, human embryonic kidney cells, Saccharomyces cerevisiae, and Escherichia coli, were tested for their sensitivity to chlorotriphenyltin and chlorotriphenyllead. The tin compound proved definitely more toxic than the lead derivative, particularly in the case of the human embryonic kidney cells devoid of any protective cell wall. Electron paramagnetic resonance (EPR) comparative studies carried out by using a natural model liposome system (egg yolk lecithin) confirmed considerable changes within the lipid bilayer upon doping by the aforementioned additives, which may be crucial to the mechanism of the observed cell cleavage. The individual dopants revealed diverse i…

Models Molecularfood.ingredientCell SurvivalHealth Toxicology and MutagenesisCellMolecular Conformationchemistry.chemical_elementSaccharomyces cerevisiaeToxicologyCleavage (embryo)BiochemistryLecithinCell wallfoodLecithinsmedicineEscherichia coliOrganometallic CompoundsOrganotin CompoundsHumansChlorotriphenyltinLipid bilayerMolecular BiologyLiposomeElectron Spin Resonance SpectroscopyGeneral MedicineYeastChlorotriphenylleadElectron Paramagnetic Resonancemedicine.anatomical_structureMembraneHEK293 CellsBiochemistrychemistryLeadHuman Embryonic Kidney CellsLiposomesMolecular MedicineTinJournal of biochemical and molecular toxicology
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