Search results for "Dimyristoylphosphatidylcholine"

showing 10 items of 21 documents

Evaluation of the interaction and drug release from alpha,beta-polyaspartamide derivatives to a biomembrane model

2005

This article reports on a comparative study on the ability of various polymers, containing hydrophilic and/or hydrophobic groups, to interact with a biomembrane model using the differential scanning calorimetry (DSC) technique. Multilamellar vesicles of mixed dimyristoylphosphatidylcholine (DMPC) and dimyristoylphosphatidic acid (DMPA) were chosen as a model of cell membranes. The investigated samples were a water soluble polymer, the alpha,beta-poly(N-2-hydroxyethyl)-DL-aspartamide (PHEA) and its derivatives partially functionalized with polyethylene glycol (PEG2000) to obtain PHEA-PEG2000, with hexadecylamine (C16) to obtain PHEA-C16, and with both compounds to obtain PHEA-PEG2000-C16. Th…

Materials sciencePolymersPharmaceutical SciencePolyethylene glycolGlycerophospholipidsMicellePolyethylene Glycolschemistry.chemical_compoundDifferential scanning calorimetryOrganic chemistryAminesMicelleschemistry.chemical_classificationDrug CarriersAniline CompoundsCalorimetry Differential ScanningPOLYASTARTAMIDE DRUG RELEASE BIOMEMBRANE MODELVesicleAnti-Inflammatory Agents Non-Steroidaltechnology industry and agricultureTemperatureBiological membraneMembranes ArtificialGeneral MedicinePolymerCombinatorial chemistryHydrocarbonsMembranechemistrySolubilityKetoprofenDrug deliverylipids (amino acids peptides and proteins)DimyristoylphosphatidylcholinePeptides
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Temperature and pressure dependence of quercetin-3-O-palmitate interaction with a model phospholipid membrane: film balance and scanning probe micros…

2004

The molecular interaction of quercetin-3-O-palmitate (QP) with dimyristoylphosphatidylcholine (DMPC) has been studied. Film balance measurements of the average molecular area vs QP molar fraction in DMPC/QP mixed monolayers showed that relevant positive deviations from ideality, i.e., a less dense monolayer packing, occurred for a temperature of 10 degrees C, below the critical melting transition temperature of DMPC monolayers T c m approximately equal 20 degrees C), while ideal behavior was observed at 37 degrees C, above this phase transition temperature. The positive deviation observed at low temperatures in the average molecular area increased with the surface pressure. Scanning probe m…

Membrane FluiditySurface PropertiesLipid BilayersAnalytical chemistryPhospholipidPalmitic AcidPhase separationPalmitic AcidsSurface pressureMole fractionMicroscopy Atomic ForcePhase TransitionBiomaterialsScanning probe microscopychemistry.chemical_compoundMembrane LipidsColloid and Surface ChemistryMonolayerLangmuir-Blodgett monolayersMolecular StructureTransition temperatureTemperatureQuercetin palmitateSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsLangmuir–Blodgett monolayerMembranechemistryAluminum SilicatesQuercetinMicaStress MechanicalDimyristoylphosphatidylcholineAlgorithmsScanning force microscopy
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Influence of Whole-Body Dynamics on 15N PISEMA NMR Spectra of Membrane Proteins: A Theoretical Analysis

2009

AbstractMembrane proteins and peptides exhibit a preferred orientation in the lipid bilayer while fluctuating in an anisotropic manner. Both the orientation and the dynamics have direct functional implications, but motions are usually not accessible, and structural descriptions are generally static. Using simulated data, we analyze systematically the impact of whole-body motions on the peptide orientations calculated from two-dimensional polarization inversion spin exchange at the magic angle (PISEMA) NMR. Fluctuations are found to have a significant effect on the observed spectra. Nevertheless, wheel-like patterns are still preserved, and it is possible to determine the average peptide til…

Models MolecularMagic angleRotationGaussianLipid BilayersNormal DistributionBiophysicsMolecular physicsProtein Structure SecondarySpectral lineQuantitative Biology::Subcellular ProcessesMolecular dynamicssymbols.namesakeNuclear magnetic resonanceOrientationComputer SimulationLipid bilayerAnisotropyNuclear Magnetic Resonance BiomolecularQuantitative Biology::BiomoleculesChemistryMembranePolarization (waves)AmplitudesymbolsDimyristoylphosphatidylcholinePeptidesBiophysical Journal
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Hydrolytic action of phospholipase A2 in monolayers in the phase transition region: direct observation of enzyme domain formation using fluorescence …

1990

Phospholipase A2, a ubiquitous lipolytic enzyme highly active in the hydrolysis of organized phospholipid substrates, has been characterized optically in its action against a variety of phospholipid monolayers using fluorescence microscopy. By labeling the enzyme with a fluorescent marker and introducing it into the subphase of a Langmuir film balance, the hydrolysis of lipid monolayers in their liquid-solid phase transition region could be directly observed with the assistance of an epifluorescence microscope. Visual observation of hydrolysis of different phospholipid monolayers in the phase transition region in real-time could differentiate various mechanisms of hydrolytic action against …

Phase transition12-DipalmitoylphosphatidylcholineStereochemistryBiophysicsPhospholipidBiochemistryPhospholipases Achemistry.chemical_compoundPhospholipase A2Phase (matter)MonolayerEnzyme StabilityFluorescence microscopeLipid bilayer phase behaviorParticle SizePhospholipidsFluorescent DyesElapid VenomsPhospholipase ABinding SitesbiologyHydrolysisPhosphatidylethanolaminesCell BiologyImage EnhancementPhospholipases A2chemistryMicroscopy FluorescencePhospholipasesBiophysicsbiology.proteinlipids (amino acids peptides and proteins)DimyristoylphosphatidylcholineBiochimica et biophysica acta
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Thermal Expansion of Microstructured DMPC Bilayers Quantified by Temperature-Controlled Atomic Force Microscopy

2006

Phase transitionMembrane FluiditySurface PropertiesLipid BilayersBiophysicsAnalytical chemistryPhospholipidMicroscopy Atomic ForcePhase TransitionThermal expansionchemistry.chemical_compoundAdsorptionMembrane fluidityPhysical and Theoretical ChemistryLipid bilayerAtomic force microscopyBilayerTemperatureProteinsLipidsAtomic and Molecular Physics and OpticsModels ChemicalchemistryChemical physicsAdsorptionDimyristoylphosphatidylcholinePeptidesChemPhysChem
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Influence of surface chemistry on the structural organization of monomolecular protein layers adsorbed to functionalized aqueous interfaces.

1993

The molecular organization of streptavidin (SA) bound to aqueous surface monolayers of biotin-functionalized lipids and binary lipid mixtures has been investigated with neutron reflectivity and electron and fluorescence microscopy. The substitution of deuterons (2H) for protons (1H), both in subphase water molecules and in the alkyl chains of the lipid surface monolayer, was utilized to determine the interface structure on the molecular length scale. In all cases studied, the protein forms monomolecular layers underneath the interface with thickness values of approximately 40 A. A systematic dependence of the structural properties of such self-assembled SA monolayers on the surface chemistr…

StreptavidinSurface PropertiesAnalytical chemistrySynthetic membraneBiophysicsBiophysical Phenomenachemistry.chemical_compoundAdsorptionBacterial ProteinsMonolayerMoietyMoleculeAlkylchemistry.chemical_classificationNeutronsAqueous solutionChemistryPhosphatidylethanolaminesProteinsWaterMembranes ArtificialLipidsCrystallographyMicroscopy ElectronCholesterolMicroscopy FluorescenceModels ChemicalAdsorptionStreptavidinDimyristoylphosphatidylcholineResearch ArticleBiophysical journal
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Anomalous surface diffusion of protons on lipid membranes.

2014

AbstractThe cellular energy machinery depends on the presence and properties of protons at or in the vicinity of lipid membranes. To asses the energetics and mobility of a proton near a membrane, we simulated an excess proton near a solvated DMPC bilayer at 323 K, using a recently developed method to include the Grotthuss proton shuttling mechanism in classical molecular dynamics simulations. We obtained a proton surface affinity of −13.0 ± 0.5 kJ mol−1. The proton interacted strongly with both lipid headgroup and linker carbonyl oxygens. Furthermore, the surface diffusion of the proton was anomalous, with a subdiffusive regime over the first few nanoseconds, followed by a superdiffusive re…

Surface diffusionPhysics::Biological PhysicsProtonChemistryBilayerLipid BilayersBiophysicsDiffusionQuantitative Biology::Subcellular ProcessesMolecular dynamicsCrystallographymolecular-dynamics simulationsMembraneDiffusion processChemical physicsphosphatidylcholine bilayersRestricted DiffusionChannels and TransportersProtonsDiffusion (business)Dimyristoylphosphatidylcholineta116
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Interaction of an odorant lactone with model phospholipid bilayers and its strong fluidizing action in yeast membrane

2003

International audience; Some odorant lactones are naturally present in fruits or in fermented products; they can also be used as food additives and can be produced by microorganisms at the industrial scale by biotechnological processes. Gamma-decalactone was previously shown to have antimicrobial properties. We determined by infrared spectroscopy measurements that this compound rapidly diffused into model phospholipid bilayers (within 2 min), modifying the general physical state of a dimyristoyl-L-alpha-phosphatidylcholine (DMPC) film. In vivo, the lactone strongly increased membrane fluidity in the model yeast Yarrowia lipolytica, as evaluated by fluorescence anisotropy measurements. This …

Time Factors[SDV.BIO]Life Sciences [q-bio]/BiotechnologyLipid BilayersYarrowiaMESH : Models BiologicalLactonesMESH : Spectroscopy Fourier Transform InfraredMESH: Dimyristoylphosphatidylcholinechemistry.chemical_compoundMESH : DimyristoylphosphatidylcholineSpectroscopy Fourier Transform InfraredMembrane fluidityOrganic chemistryMESH : Anti-Bacterial Agents[INFO.INFO-BT]Computer Science [cs]/BiotechnologyAntibacterial agentMESH : Spectrometry FluorescencebiologyMESH: Lipid BilayersMESH: Indicators and Reagentsfood and beveragesGeneral MedicineAnti-Bacterial AgentsMESH : LactonesMembraneBenzyl alcoholDimyristoylphosphatidylcholine[ INFO.INFO-BT ] Computer Science [cs]/BiotechnologyMESH: LactonesMESH: Spectrometry FluorescenceMESH : Time FactorsMESH : YarrowiaPhospholipid[SDV.BC]Life Sciences [q-bio]/Cellular BiologyModels BiologicalMicrobiologyMESH: Spectroscopy Fourier Transform InfraredMESH : Indicators and ReagentsMESH: Anti-Bacterial Agents[ SDV.BC ] Life Sciences [q-bio]/Cellular BiologyMESH: Time FactorsMESH: Models Biological[ SDV.BIO ] Life Sciences [q-bio]/BiotechnologyYarrowiaBiological membranebiology.organism_classificationYeastSpectrometry FluorescencechemistryIndicators and ReagentsMESH: YarrowiaMESH : Lipid BilayersFood ScienceInternational Journal of Food Microbiology
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Influence of functionalization on interaction and drug release from α,β-polyaspartylhydrazide derivatives to a biomembrane model: evaluation by diffe…

2004

Abstract A comparative study on the ability of various polymers to interact with a biomembrane model was carried out by differential scanning calorimetry (DSC). The investigated samples were a water soluble polymer, the α,β-polyaspartylhydrazide (PAHy) and its derivatives containing polyethylene glycol (PEG2000) (sample PAHy–PEG2000), or hexadecylamine (C16) (sample PAHy–C16) or both compounds (sample PAHy–PEG2000–C16). Some samples are able to arrange themselves as micellar structures and to interact potentially with the membrane surface so as to favor the release of the drug near the target membrane and consequently to improve drug adsorption processes. First, the interaction of all polym…

chemistry.chemical_classificationChemistryDimyristoylphosphatidic acidtechnology industry and agricultureBiological membraneDrug releasePolymerPolyethylene glycolPolyaspartylhydrazideCondensed Matter PhysicsMicelleThermotropic crystalchemistry.chemical_compoundDifferential scanning calorimetryMembraneChemical engineeringDifferential scanning calorimetrySettore CHIM/09 - Farmaceutico Tecnologico ApplicativoPolymeric micelleOrganic chemistrylipids (amino acids peptides and proteins)Physical and Theoretical ChemistryDimyristoylphosphatidylcholineDrug carrierInstrumentationThermochimica Acta
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The dynamic orientation of membrane-bound peptides: bridging simulations and experiments.

2007

AbstractThe structural organization in a peptide/membrane supramolecular complex is best described by knowledge of the peptide orientation plus its time-dependent and spatial fluctuations. The static orientation, defined by the peptide tilt and a rotation about its molecular axis, is accessible through a number of spectroscopic methods. However, peptide dynamics, although relevant to understand the functionality of these systems, remains largely unexplored. Here, we describe the orientation and dynamics of Trp-flanked and Lys-flanked hydrophobic peptides in a lipid bilayer from molecular dynamics simulations. A novel view is revealed, where collective nontrivial distributions of time-evolvi…

chemistry.chemical_classificationModels MolecularMembranesProtein ConformationLipid BilayersBiophysicsSupramolecular chemistryAnchoringMembrane ProteinsPeptideOrientation (graph theory)CrystallographyMolecular dynamicsMembraneProtein structurechemistryModels ChemicalChemical physicsComputer SimulationLipid bilayerDimyristoylphosphatidylcholinePeptidesBiophysical journal
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