Search results for "Phosphatidylcholines"

showing 10 items of 90 documents

Microscale synthesis of phosphatidyl-[3H]choline from 1,2-diacylglycerol. Assessment of isomerization by reversed-phase high-performance liquid chrom…

1995

The synthesis of rac-1-palmitoyl-2-oleoylglycero-3-phospho-[3H]choline of high specific activity was carried out on a microscale by making 7 mumol of rac-1-palmitoyl-2-oleoylglycerol react first with an equimolar amount of POCl3 and then of [3H]choline. After purification by thin-layer chromatography and normal-phase high-performance liquid chromatography and normal-phase high-performance liquid chromatography (HPLC), the yield of the synthesis of [3H]phosphatidylcholine (120 microCi/mumol) was 22%. rac-1-Palmitoyl-2-oleoylglycerol was purified before use by reversed-phase HPLC under conditions which were nonisomerizing and allowed the separation of 1,2- and 1,3-isomers of diacylglycerol. E…

Chromatography GasChromatographyOrganic ChemistryStereoisomerismCell BiologyReference StandardsBiochemistryHigh-performance liquid chromatographyDiglycerideschemistry.chemical_compoundchemistryPhosphatidylcholinePhosphatidylcholinesCholineChromatography Thin LayerMethanolAcetonitrileIsomerizationChromatography High Pressure LiquidCholine chlorideDiacylglycerol kinaseLipids
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HPLC study on the ‘history’ dependence of gramicidin A conformation in phospholipid model membranes

1989

AbstractA novel HPLC methodology for the study of gramicidin A reconstituted in model membranes has been tested in comparison with circular dichroism data. It is shown that this chromatographic technique not only corroborates most of the recent spectroscopic results but allows one to explain them in terms of mass fractions of different actual conformational species of GA in the phospholipid assemblies. In particular, the dependence of the inserted peptide configuration on the organic solvent and other parameters involved in the ‘history’ of the sample preparation and handling has been analyzed by HPLC in two phospholipid model systems: small unilamellar vesicles and micelles. Moreover, a sl…

Circular dichroismProtein ConformationMolecular ConformationBiophysicsPhospholipidPeptideBiochemistryHigh-performance liquid chromatographyMicellechemistry.chemical_compoundStructural BiologyGramicidin A conformationGeneticsGramicidin ASample preparationMolecular BiologyChromatography High Pressure Liquidchemistry.chemical_classificationChromatographyChemistryCircular DichroismGramicidinMembranes ArtificialCell BiologyModels TheoreticalCDMembraneLiposomesPhospholipid vesiclePhosphatidylcholinesHPLCFEBS Letters
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Environment- and sequence-dependent modulation of the double-stranded to single-stranded conformational transition of gramicidin A in membranes.

1998

The role of the membrane lipid composition and the individual Trp residues in the conformational rearrangement of gramicidin A along the folding pathway to its channel conformation has been examined in phospholipid bilayers by means of previously described size-exclusion high-performance liquid chromatography HPLC-based strategy (Bano et al. (1991) Biochemistry 30, 886). It has been demonstrated that the chemical composition of the membrane influences the transition rate of the peptide rearrangement from double-stranded dimers to beta-helical monomers. The chemical modification of Trp residues, or its substitution by the more hydrophobic residues phenylalanine or naphthylalanine, stabilized…

Circular dichroismStereochemistryProtein ConformationDimerPhenylalanineEnterococcus faeciumLipid BilayersMolecular Sequence DataPeptideMicrobial Sensitivity TestsBiochemistrychemistry.chemical_compoundProtein structureAmino Acid SequencePeptide sequenceChromatography High Pressure Liquidchemistry.chemical_classificationChemistryCholestenesCircular DichroismGramicidinTryptophanFolding (chemistry)MembraneSpectrometry FluorescenceAmino Acid SubstitutionGramicidinFatty Acids UnsaturatedPhosphatidylcholinesDimerizationBiochemistry
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Inverse Conformational Selection in Lipid–Protein Binding

2021

International audience; Interest in lipid interactions with proteins and other biomolecules is emerging not only in fundamental biochemistry but also in the field of nanobiotechnology where lipids are commonly used, for example, in carriers of mRNA vaccines. The outward-facing components of cellular membranes and lipid nanoparticles, the lipid headgroups, regulate membrane interactions with approaching substances, such as proteins, drugs, RNA, or viruses. Because lipid headgroup conformational ensembles have not been experimentally determined in physiologically relevant conditions, an essential question about their interactions with other biomolecules remains unanswered: Do headgroups excha…

DYNAMICSELECTRIC CHARGEBILAYERSPHOSPHATIDYLCHOLINE HEADGROUPMembrane lipidsDEUTERIUMPlasma protein bindingMolecular Dynamics Simulationlipidit010402 general chemistry01 natural sciencesBiochemistrybiomolekyylitCatalysis03 medical and health sciencesMolecular dynamicskemialliset sidoksetColloid and Surface ChemistryProtein structurePHOSPHOLIPID-BINDINGMAGNETIC-RESONANCE[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologySEGMENTAL ORDER[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyConformational ensemblesNuclear Magnetic Resonance Biomolecular030304 developmental biologychemistry.chemical_classification0303 health sciencesChemistryBiomoleculeMEMBRANE-LIPIDSProteinsPhosphatidylglycerolsGeneral Chemistrycomputer.file_formatProtein Data BankLipids0104 chemical sciencesBiophysicsPhospholipid BindingPhosphatidylcholinesMAS NMR1182 Biochemistry cell and molecular biologylipids (amino acids peptides and proteins)proteiinitcomputerProtein Binding
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Detergent Properties Influence the Stability of the Glycophorin A Transmembrane Helix Dimer in Lysophosphatidylcholine Micelles

2012

AbstractDetergents might affect membrane protein structures by promoting intramolecular interactions that are different from those found in native membrane bilayers, and fine-tuning detergent properties can be crucial for obtaining structural information of intact and functional transmembrane proteins. To systematically investigate the influence of the detergent concentration and acyl-chain length on the stability of a transmembrane protein structure, the stability of the human glycophorin A transmembrane helix dimer has been analyzed in lyso-phosphatidylcholine micelles of different acyl-chain length. While our results indicate that the transmembrane protein is destabilized in detergents w…

DetergentsMolecular Sequence DataBiophysicsMicelleProtein Structure SecondaryCell membraneHydrophobic mismatchmedicineHumansGlycophorinAmino Acid SequenceGlycophorinsLipid bilayerMicellesAggregation numberDose-Response Relationship DrugbiologyChemistryCell MembraneMembraneLysophosphatidylcholinesTransmembrane proteinTransmembrane domainmedicine.anatomical_structureBiochemistrybiology.proteinBiophysicslipids (amino acids peptides and proteins)Protein MultimerizationHydrophobic and Hydrophilic InteractionsBiophysical Journal
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Acyl-Chain Mismatch Driven Superlattice Arrangements in DPPC/DLPC/Cholesterol Bilayers

2010

Fluorescence and infrared spectroscopy and cholesterol oxidase activity were employed to investigate the effect of phosphatidylcholine (PC) acyl chain length mismatch on the lateral organizations of lipids in liquid-ordered dipalmitoyl-PC/dilauroyl-PC/cholesterol (DPPC/DLPC/CHOL) bilayers. Plots of steady-state fluorescence emission anisotropy of diphenylhexatriene (DPH) labeled PC (DPH-PC) embedded in the DPPC/DLPC/CHOL bilayers revealed significant peaks at several DPPC mole fractions (Y(DPPC)) when the cholesterol mole fraction (X(CHOL)) was fixed to particular values. Analogously, the DPH-PC anisotropy peaked at several critical X(CHOL)'s when Y(DPPC) was fixed. Acyl chain C-H and C hor…

Diphenylhexatriene12-DipalmitoylphosphatidylcholineCholesterol oxidaseSuperlatticeLipid BilayersAnalytical chemistryInfrared spectroscopyFluorescence Polarization010402 general chemistryMole fraction01 natural sciencesArticle03 medical and health scienceschemistry.chemical_compoundPhosphatidylcholineSpectroscopy Fourier Transform Infraredpolycyclic compoundsMaterials ChemistryPhysical and Theoretical ChemistryLipid bilayer030304 developmental biology0303 health sciencesCholesterol OxidaseCholesteroltechnology industry and agriculture0104 chemical sciencesSurfaces Coatings and FilmsCrystallographyCholesterolchemistryCholesterol oxidase activity13. Climate actionAcyl chainPhosphatidylcholineslipids (amino acids peptides and proteins)Fluorescence anisotropyThe Journal of Physical Chemistry B
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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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Acute renal failure and liver dysfunction after subcutaneous injection of 3-sn-phosphatidylcholine (Lipostabil®)-case report.

2011

INTRODUCTION Drug-induced tubulointerstitial nephritis and acute tubular necrosis are common, and are often caused by drugs especially antibiotics or non-steroidal anti-inflammatory drugs. Drug-induced liver dysfunction and renal failure after subcutaneous injection of phosphatidylcholine was not reported so far. 3-sn-Phosphatidylcholine has been described as a cell lysis reaction-inducing drug. Its in vitro data indicated a relevant toxicity potential. In particular human cell types such as fibroblast-like preadipocytes, vascular and skeletal muscle cells, or renal epithelial cells react more sensitive than other human cell types. CASE REPORT We present a 28-year-old woman who received 3.5…

DrugAdultmedicine.medical_specialtymedicine.drug_classNauseamedia_common.quotation_subjectInjections SubcutaneousAntibioticsUrologyRenal functionSubcutaneous injectionmedicineHumansFat embolismAcute tubular necrosismedia_commonNephritisbusiness.industryGastroenterologyAcute Kidney Injurymedicine.diseaseSurgeryToxicityPhosphatidylcholinesFemalemedicine.symptombusinessZeitschrift fur Gastroenterologie
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Cholesterol binds to synaptophysin and is required for biogenesis of synaptic vesicles.

1999

Here, to study lipid-protein interactions that contribute to the biogenesis of regulated secretory vesicles, we have developed new approaches by which to label proteins in vivo, using photoactivatable cholesterol and glycerophospholipids. We identify synaptophysin as a major specifically cholesterol-binding protein in PC12 cells and brain synaptic vesicles. Limited cholesterol depletion, which has little effect on total endocytic activity, blocks the biogenesis of synaptic-like microvesicles (SLMVs) from the plasma membrane. We propose that specific interactions between cholesterol and SLMV membrane proteins, such as synaptophysin, contribute to both the segregation of SLMV membrane constit…

Endocytic cycleSynaptophysinKidneyTritiumSynaptic vesiclePC12 CellsExocytosisR-SNARE ProteinsAnimalsHumansNeuronsVAMP2biologyCell MembraneMembrane ProteinsCell BiologySecretory VesicleMicrovesiclesEndocytosisCell biologyRatsCholesterolMembrane proteinSynaptophysinbiology.proteinPhosphatidylcholinesSynaptic VesiclesBiogenesisSynaptosomesNature cell biology
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