Search results for "LIPOSOMES"

showing 10 items of 221 documents

Vibrio cholerae cytolysin: assembly and membrane insertion of the oligomeric pore are tightly linked and are not detectably restricted by membrane fl…

2000

AbstractHemolytic strains of Vibrio cholerae secrete a cytolysin that, upon binding as a monomer, forms pentameric pores in animal cell membranes. Pore formation is inhibited at low temperature and in the absence of cholesterol. We here posed the following questions: firstly, can oligomerization be observed in the absence of pore formation? Secondly, is membrane fluidity responsible for the effect of temperature or of cholesterol upon pore formation? The first issue was approached by chemical cross-linking, by electrophoretic heteromer analysis, and by electron microscopy. None of these methods yielded any evidence of a non-lytic pre-pore oligomer. The second question was addressed by the u…

DiphenylhexatrieneCell Membrane PermeabilityMembrane permeabilityMembrane FluidityBacterial ToxinsBiophysicsPorinsFluorescence PolarizationBiologymedicine.disease_causePore forming toxinBiochemistrychemistry.chemical_compoundProtein oligomerizationBacterial ProteinsBacteriocinsmedicineMembrane fluidityProtein oligomerizationVibrio choleraePhospholipidsFluorescent DyesLiposomeCytotoxinsCell MembraneCell BiologyFluoresceinsCholesterolMembranechemistryBiochemistryVibrio choleraeLiposomesPhosphatidylcholinesCytolysinDiphenylhexatrieneBiochimica et Biophysica Acta (BBA) - Biomembranes
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Time-resolved fluorescence and fourier transform infrared spectroscopic investigations of lateral packing defects and superlattice domains in composi…

2003

Time-resolved fluorescence and Fourier transform infrared spectroscopies were used to investigate the lateral organization of lipids in compositionally uniform and fully equilibrated 1-palmitoyl-2-oleoyl-phosphatidylcholine/cholesterol (POPC/CHOL) liposomes prepared by a recently devised low-temperature trapping method. Independent fluorescence decay lifetime and rotational dynamics parameters of diphenylhexatriene (DPH) chain-labeled phosphatidylcholine (DPH-PC) in these liposomes were recovered from the time-resolved fluorescence measurements as a function of cholesterol molar fraction (X(CHOL)) at 23 degrees C. The results indicate significantly greater lifetime heterogeneity, shorter av…

DiphenylhexatrieneModels MolecularMacromolecular SubstancesMembrane FluidityLipid BilayersBiophysicsAnalytical chemistry010402 general chemistryMole fraction01 natural sciences03 medical and health scienceschemistry.chemical_compoundPhosphatidylcholineSpectroscopy Fourier Transform InfraredMembrane fluiditypolycyclic compoundsComputer SimulationLipid bilayerPOPCRotational correlation time030304 developmental biology0303 health sciencesLiposomeMembranestechnology industry and agricultureSignal Processing Computer-Assisted0104 chemical sciencesCrystallographyCholesterolSpectrometry FluorescencechemistryLiposomesPhosphatidylcholinesAnisotropylipids (amino acids peptides and proteins)AlgorithmsBiophysical journal
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Recombinant cDNA encapsulation in small liposomes with hepatocyte access ability.

1993

Liposomal encapsulation efficiency of a recombinant cDNA was studied by several procedures. We observed that supernatant fraction of ultracentrifuged liposomes prepared by extrusion through polycarbonate filters of 400 nm pore size yielded a very homogeneous suspension of small (50 nm diameter) unilamellar liposomes with highest DNA/lipid ratio and great ability to access to hepatocytes.

Drug CompoundingDNA RecombinantPharmaceutical ScienceBioengineeringBiologyIn Vitro Techniqueslaw.inventionchemistry.chemical_compoundMiceColloid and Surface ChemistrylawComplementary DNAmedicineAnimalsHumansPhysical and Theoretical ChemistryFluoresceinParticle SizeLiposomeDrug CarriersChromatographyParaffin EmbeddingStaining and LabelingOrganic ChemistryFluoresceinsMice Inbred C57BLMicroscopy Electronmedicine.anatomical_structureBiochemistrychemistryLiverHepatocytealpha 1-AntitrypsinLiposomesRecombinant DNAExtrusionParticle sizeDrug carrierFiltrationPlasmidsJournal of microencapsulation
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Pharmacokinetics of oligodeoxynucleotides encapsulated in liposomes: effect of lipid composition and preparation method

2000

1. The effect of the method employed to prepare liposomes and their lipid composition were evaluated in terms of the encapsulation efficiency and pharmacokinetic features of two oligodeoxynucleotides of a 21 mer: the normal (N-Odn) and the phosphorothioate (S-Odn) oligodeoxynucleotide. 2. Liposomes were prepared by the classical method of multilamellar vesicles (MV) and by the dehydration-rehydration method (DR). Two lipid mixtures were used to prepare liposomes--the predominant lipid being phosphatidylcholine (PC) and sphingomyelin (SM) respectively. 3. The DR method for liposome preparation provided the highest encapsulation efficiency, regardless of liposome lipid composition and the typ…

Drug CompoundingHealth Toxicology and MutagenesisLipid compositionMultilamellar vesiclesToxicologyBiochemistryPreparation methodMicechemistry.chemical_compoundPharmacokineticsPhosphatidylcholineAnimalsPharmacologyPlasma clearanceLiposomeChromatographyChemistryhemic and immune systemsGeneral MedicineThionucleotidesrespiratory systemLipidsOligodeoxyribonucleotidesBiochemistryInjections IntravenousLiposomesSphingomyelinXenobiotica
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Cyanocobalamin Ultraflexible Lipid Vesicles: Characterization and In Vitro Evaluation of Drug-Skin Depth Profiles

2021

Atopic dermatitis (AD) and psoriasis are the most common chronic inflammatory skin disorders, which importantly affect the quality of life of patients who suffer them. Among other causes, nitric oxide has been reported as part of the triggering factors in the pathogenesis of both conditions. Cyanocobalamin (vitamin B12) has shown efficacy as a nitric oxide scavenger and some clinical trials have given positive outcomes in its use for treating skin pathologies. Passive skin diffusion is possible only for drugs with low molecular weights and intermediate lipophilicity. Unfortunately, the molecular weight and hydrophilicity of vitamin B12 do not predict its effective diffusion through the skin…

Drugliposomesmedia_common.quotation_subjectPharmaceutical Sciencelcsh:RS1-441Dermatitis02 engineering and technologyPharmacology030226 pharmacology & pharmacyArticleNitric oxidelcsh:Pharmacy and materia medica03 medical and health scienceschemistry.chemical_compound0302 clinical medicinePsoriasismedicineCyanocobalaminVitamin B12cyanocobalaminskin topical deliverymedia_commonLiposomeatopic dermatitisVesiclePellAtopic dermatitisvitamin B12psoriasis021001 nanoscience & nanotechnologymedicine.diseaselipid vesicleschemistrytransferosomes0210 nano-technologyTecnologia farmacèuticaPharmaceutics
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Activation of bee venom phospholipase A2 through a peptide-enzyme complex

1995

AbstractPhospholipase A2 activation by membrane-bound peptides was investigated in order to understand the role of the membrane-induced conformation on activation, and to examine the occurrence of a peptide-enzyme complex at the lipid/water interface. For the peptides studies, bee venom phospholipase A2 was stimulated regardless of the membrane-bound conformation (α-helix, β-sheet or random coil). Using antisera raised against melittin, we were able to demonstrate the occurrence of a calcium-dependent complex involving the enzyme, phospholipid substrate, and peptide.

Enzyme complexProtein ConformationMolecular Sequence DataBiophysicsPhospholipidPeptidePhospholipaseBiochemistrycomplex mixturesAbellesMelittinAntibodiesPhospholipases AProtein Structure Secondarychemistry.chemical_compoundEnzyme activatorPhospholipase A2Structural BiologyGeneticsAnimalsAmino Acid SequencePhospholipaseMolecular BiologyPeptide sequencePeptide-enzyme complexchemistry.chemical_classificationbiologyCircular DichroismMembrane ProteinsMelittinCell BiologyMelittenEnzyme ActivationBee VenomsPhospholipases A2chemistryBiochemistryLiposomesbiology.proteinPèptidsPeptides
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Expression of Active Streptolysin O in Escherichia coli as a Maltose-Binding-Protein-Streptolysin-O Fusion Protein. The N-Terminal 70 Amino Acids are…

1996

Streptolysin 0 (SLO) is the prototype of a family of cytolysins that consists of proteins which bind to cholesterol and form very large transmembrane pores. Structure/function studies on the pore-forming cytolysin SLO have been complicated by the proteolytic inactivation of a substantial portion of recombinant SLO (rSLO) expressed in Escherichia coli. To overcome this problem, translational fusions between the E. coli maltose-binding protein (MBP) gene and SLO were constructed, using the vectors pMAL-p2 and pMAL-c2. MBP-SLO fusion proteins were degraded if secreted into the E. coli periplasm, but intact, soluble MBP-SLO fusion proteins were produced at high levels in the cytoplasm. Active S…

ErythrocytesMonosaccharide Transport Proteinsgenetic structuresProtein ConformationStreptococcus pyogenesRecombinant Fusion ProteinsMolecular Sequence Datamedicine.disease_causeHemolysisBiochemistryMaltose-Binding ProteinsStructure-Activity RelationshipMaltose-binding proteinProtein structureBacterial ProteinsEscherichia colimedicineHumansCloning MolecularEscherichia coliSequence DeletionPore-forming toxinBase SequencebiologyEscherichia coli ProteinsFluoresceinsFusion proteineye diseasesTransmembrane proteinBiochemistryLiposomesStreptolysinsbiology.proteinATP-Binding Cassette TransportersStreptolysinsense organsCytolysinCarrier ProteinsSequence AnalysisEuropean Journal of Biochemistry
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Evidence that clustered phosphocholine head groups serve as sites for binding and assembly of an oligomeric protein pore.

2006

High susceptibility of rabbit erythrocytes toward the pore-forming action of staphylococcal alpha-toxin correlates with the presence of saturable, high affinity binding sites. All efforts to identify a protein or glycolipid receptor have failed, and the fact that liposomes composed solely of phosphatidylcholine are efficiently permeabilized adds to the enigma. A novel concept is advanced here to explain the puzzle. We propose that low affinity binding moieties can assume the role of high affinity binding sites due to their spatial arrangement in the membrane. Evidence is presented that phosphocholine head groups of sphingomyelin, clustered in sphingomyelin-cholesterol microdomains, serve th…

ErythrocytesPhosphorylcholineBacterial ToxinsBiologyBiochemistryCell Linechemistry.chemical_compoundHemolysin ProteinsGlycolipidMembrane MicrodomainsPhosphatidylcholineAnimalsHumansReceptorProtein Structure QuaternaryMolecular BiologyPhosphocholineLiposomeBinding SitesCell BiologySphingomyelinsMembraneCholesterolSphingomyelin PhosphodiesteraseBiochemistrychemistryLiposomesRabbitsSphingomyelinFunction (biology)Protein BindingThe Journal of biological chemistry
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Relationship between the structure of amphiphilic copolymers and their ability to disturb lipid bilayers.

2005

Nonionic amphiphiles and particularly block copolymers of ethylene oxide and propylene oxide (Pluronics) cause pronounced chemosensitization of tumor cells that exhibit multiple resistance to antineoplastic drugs. This effect is due to inhibition of P-glycoprotein (P-gp) responsible for drug efflux. It was suggested that the inhibition of P-gp might be due to changes in its lipid surrounding. Indeed, high dependence of P-gp activity on the membrane microviscosity was demonstrated [Regev et al. (1999) Eur. J. Biochem. 259, 18-24], suggesting that the ability of Pluronics to affect the P-gp activity is mediated by their effect on the membrane structure. We have found recently that adsorption …

Ethylene OxideGlycerolFree RadicalsPolymersLipid BilayersPoloxamerBiochemistryPermeabilityPolyethylene GlycolsMicroviscositychemistry.chemical_compoundStructure-Activity RelationshipAmphiphilePolymer chemistryCopolymerAnimalsHexanesLipid bilayerLiposomeEthylene oxideWaterMembranes ArtificialPoloxamerMembranechemistryDoxorubicinLiposomesBiophysicsPhosphatidylcholinesEpoxy CompoundsCattleAdsorptionBiochemistry
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Shape transitions of giant liposomes induced by an anisotropic spontaneous curvature

2000

International audience; We explore how a magnetic field breaks the symmetry of an initially spherical giant liposome filled with a magnetic colloid. The condition of rotational symmetry along the field axis leads either to a prolate or to an oblate ellipsoid. We demonstrate that an electrostatic interaction between the nanoparticles and the membrane triggers the shape transition. PACS numbers: 75.

Field (physics)Static ElectricityRotational symmetryFOS: Physical sciencesNanoparticle02 engineering and technologyCondensed Matter - Soft Condensed Matter[CHIM.INOR]Chemical Sciences/Inorganic chemistryCurvatureFerric Compounds01 natural sciencesMagneticsColloid0103 physical sciencesColloids010306 general physicsAnisotropyDebye lengthPhysicsCondensed matter physicsOsmolar Concentration[CHIM.MATE]Chemical Sciences/Material chemistryModels Theoretical021001 nanoscience & nanotechnologyGiant liposomesSymmetry (physics)Magnetic field[CHIM.POLY]Chemical Sciences/PolymersClassical mechanicsLiposomesMagnetic nanoparticlesPhosphatidylcholinesSoft Condensed Matter (cond-mat.soft)AnisotropySpontaneous curvature0210 nano-technology[PHYS.COND.CM-SCM]Physics [physics]/Condensed Matter [cond-mat]/Soft Condensed Matter [cond-mat.soft]Physical Review E
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