Search results for "Lipid bilayer fusion"

showing 10 items of 30 documents

Stability of Asymmetric Lipid Bilayers Assessed by Molecular Dynamics Simulations

2009

The asymmetric insertion of amphiphiles into biological membranes compromises the balance between the inner and outer monolayers. As a result, area expansion of the receiving leaflet and curvature strain may lead to membrane permeation, shape changes, or membrane fusion events. We have conducted both atomistic and coarse-grained molecular dynamics simulations of dipalmitoyl-phosphatidylcholine (DPPC) bilayers to study the effect of an asymmetric distribution of lipids between the two monolayers on membrane stability. Highly asymmetric lipid bilayers were found to be surprisingly stable within the submicrosecond time span of the simulations. Even the limiting case of a monolayer immersed in …

12-DipalmitoylphosphatidylcholineLipid BilayersBiochemistryCatalysisColloid and Surface ChemistryCOARSE-GRAINED MODELSHAPE TRANSFORMATIONSMonolayerComputer SimulationLipid bilayer phase behaviorLipid bilayerChemistryBilayerLipid bilayer fusionBiological membraneGeneral ChemistryLipid bilayer mechanicsANTIMICROBIAL PEPTIDESCrystallographyMembraneTRANSMEMBRANE DISTRIBUTIONEGG PHOSPHATIDYLCHOLINEPhosphatidylcholinesPORE FORMATIONBiophysicsPRESSURE PROFILESMECHANOSENSITIVE CHANNELlipids (amino acids peptides and proteins)OCTYL GLUCOSIDEPHOSPHOLIPID-BILAYERSJournal of the American Chemical Society
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The Alignment of Membrane-Active Peptides Depends on the Lipid Phase State as Viewed by solid state 19F-NMR

2009

Amphipathic membrane-active peptides (antimicrobial, hemolytic, cell-penetrating, fusogenic, etc.) achieve their functions by distinct interaction with lipid bilayers. Some typical structural modes are described in terms of models like the “barrel stave”, “toroidal pore”, “carpet” etc. These models are related to the alignment states of the peptides in the lipid bilayers (surface bound “S-state”, inserted “I-state” or tilted “T-state”), which can be readily characterized by solid state NMR. When determining such alignment, factors like peptide/lipid ratio, charge of the bilayer surface, thickness of the bilayer core, presence of cholesterol, and humidity are typically investigated. Yet, the…

AlamethicinBilayerBiophysicsMagaininLipid bilayer fusionBiological membranechemistry.chemical_compoundCrystallographychemistryBiophysicsGramicidinlipids (amino acids peptides and proteins)Lipid bilayer phase behaviorLipid bilayerBiophysical Journal
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Characterization of fusion from without induced by herpes simplex virus

1991

The process of fusion from without (FFWO) induced by herpes simplex virus (HSV) was analyzed by using various inhibitors and compared to fusion from within (FFWI). The fate of certain elements of the cytoskeleton after FFWO was also investigated. Our experiments demonstrate FFWO as a very suitable system for study of early virus-cell interactions. Zn++ ions proved inhibitory for penetration whilst pretreatment of cells with Ca++ ions before infection enhanced FFWO activity. Dissociation of penetration from the fusion process itself was possible by use of Zn++ ions, low pH-treatment and antiserum on the one hand and N-ethylmaleimide and cytochalasin D on the other. Penetration itself needs o…

Cations DivalentCycloheximideBiologyVirusCell FusionCell membranechemistry.chemical_compoundSpecies SpecificityLectinsVirologymedicineAnimalsSimplexvirusProtease InhibitorsVero CellsCytoskeletonPolysaccharide-LyasesCytochalasin DCell fusionCell MembraneLipid bilayer fusionGeneral MedicineTunicamycinLipidsVirologymedicine.anatomical_structurechemistryEthylmaleimideVero cellReceptors VirusGlycoconjugatesArchives of Virology
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Hexapeptides that interfere with HIV-1 fusion peptide activity in liposomes block GP41-mediated membrane fusion

2006

AbstractUpon receptor-mediated activation, the gp41 hydrophobic, conserved fusion peptide inserts into the target membrane and promotes the kind of perturbations required for the progression of the HIV-cell fusion reaction. Using a synthetic combinatorial library we have identified all d-amino acid hexapeptide sequences that inhibited the fusion peptide capacity of perturbing model membranes. Two hexapeptides that effectively inhibited the fusion peptide in these systems were subsequently shown to inhibit cell–cell fusion promoted by gp41 expressed at cell surfaces. These observations might be of importance for understanding the mechanisms underlying fusion peptide activity and suggest new …

CellBiophysicsMembrane fusionCHO CellsGp41BiochemistryFusion peptideMembranes (Biologia)Structural BiologyCricetinaeGeneticsmedicineNuclear fusionAnimalsMolecular BiologyFusion inhibitorFusionLiposomeChemistryLipid bilayer fusionViral fusionCell Biologygp41HIV Envelope Protein gp41Cell biologyMembranemedicine.anatomical_structureBiochemistryLiposomesHIV-1PèptidsPeptidesFusion peptide
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Comprehensive analysis of expression, subcellular localization, and cognate pairing of SNARE proteins in oligodendrocytes

2009

Oligodendrocytes form the central nervous system myelin sheath by spiral wrapping of their plasma membrane around axons, necessitating a high rate of exocytic membrane addition to the growing myelin membrane. Membrane fusion is mediated by soluble N-ethylmaleimide-sensitive factor attachment protein receptor proteins (SNAREs), which act by specific pairing of vesicle (R)- and target (Q)-SNAREs. To characterize oligodendroglial SNAREs and their trafficking pathways, we performed a detailed expression analysis of SNAREs in differentiating cultured oligodendrocytes and myelin and determined their subcellular localization. Expression of the plasma membrane Q-SNAREs syntaxin 3, syntaxin 4, SNAP2…

Central Nervous SystemMaleVesicle-Associated Membrane Protein 3SynaptobrevinGolgi ApparatusBiologyMembrane FusionR-SNARE ProteinsMiceCellular and Molecular NeuroscienceSNAP23AnimalsSyntaxinQc-SNARE ProteinsTransport VesiclesCells CulturedMyelin SheathR-SNARE ProteinsQa-SNARE ProteinsVesicleCell MembraneLipid bilayer fusionQb-SNARE ProteinsSyntaxin 3Cell CompartmentationTransport proteinCell biologyOligodendrogliaProtein Transportnervous systemFemalebiological phenomena cell phenomena and immunitySNARE ProteinsDimerizationJournal of Neuroscience Research
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Role of hydrophobic forces in bilayer adhesion and fusion.

1992

With the aim of gaining more insight into the forces and molecular mechanisms associated with bilayer adhesion and fusion, the surface forces apparatus (SFA) was used for measuring the forces and deformations of interacting supported lipid bilayers. Concerning adhesion, we find that the adhesion between two bilayers can be progressively increased by up to two orders of magnitude if they are stressed to expose more hydrophobic groups. Concerning fusion, we find that the most important force leading to direct fusion is the hydrophobic attraction acting between the (exposed) hydrophobic interiors of bilayers; however, the occurrence of fusion is not simply related to the strength of the attrac…

Chemical PhenomenaChemistryCetrimoniumChemistry PhysicalMembrane FluidityBilayerLipid BilayersLipid bilayer fusionAdhesivenessSurface forces apparatusNanotechnologyAdhesionInterbilayer forces in membrane fusionBiochemistryMembrane FusionBiomechanical PhenomenaHydrophobic effectDiffusionChemical physicsCetrimonium CompoundsStress MechanicalLipid bilayerDimyristoylphosphatidylcholineFusion mechanismPhospholipidsBiochemistry
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Role of calcium in the adhesion and fusion of bilayers.

1993

The interaction forces and fusion mechanisms of mixed zwitterionic-anionic phospholipid bilayers were measured with the surface forces apparatus. The bilayers were 3:1 mixtures of either dimyristoylphosphatidylcholine and dimyristoylphosphatidylglycerol (DMPC/DMPG) or dilauroylphosphatidylcholine and dilauroylphosphatidylglycerol (DLPC/DLPG), and experiments were carried out in NaCl solutions with and without CaCl2. In NaCl solutions, the forces between either mixed bilayer system were consistent with the DLVO (Derjaguin-Landau-Verwey-Overbeek) theory of repulsive electrostatic and attractive van der Waals forces, and fusion did not occur. At high pH (> 6) and in high (20 mM) NaCl concentra…

ChemistryBilayerLipid BilayersAnalytical chemistryLipid bilayer fusionSurface forces apparatusPhosphatidylglycerolsAdhesionInterbilayer forces in membrane fusionSodium ChlorideBiochemistryMembrane FusionSolutionssymbols.namesakeCalcium ChlorideChemical physicsPhase (matter)symbolsPhosphatidylcholinesDLVO theoryCalciumvan der Waals forceMathematicsBiochemistry
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Mg2+-binding shifts the IM30 activity from membrane protection to membrane destabilization

2020

ABSTRACTThe inner membrane-associated protein of 30 kDa (IM30) is essential in chloroplasts and cyanobacteria. The spatio-temporal cellular localization of the protein appears to be highly dynamic and triggered by internal as well as external stimuli, mainly light intensity. A soluble fraction of the protein is localized in the cyanobacterial cytoplasm or the chloroplast stroma, respectively. Additionally, the protein attaches to the thylakoid membrane as well as to the chloroplast inner envelope or the cyanobacterial cytoplasmic membrane, respectively, especially under conditions of membrane stress. IM30 is involved in thylakoid membrane biogenesis and/or maintenance, where it either stabi…

ChloroplastLight intensityChloroplast stromaMembraneCytoplasmChemistryThylakoidBiophysicsLipid bilayer fusionCellular localization
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IM30 triggers membrane fusion in cyanobacteria and chloroplasts

2015

The thylakoid membrane of chloroplasts and cyanobacteria is a unique internal membrane system harbouring the complexes of the photosynthetic electron transfer chain. Despite their apparent importance, little is known about the biogenesis and maintenance of thylakoid membranes. Although membrane fusion events are essential for the formation of thylakoid membranes, proteins involved in membrane fusion have yet to be identified in photosynthetic cells or organelles. Here we show that IM30, a conserved chloroplast and cyanobacterial protein of approximately 30 kDa binds as an oligomeric ring in a well-defined geometry specifically to membranes containing anionic lipids. Triggered by Mg2+, membr…

ChloroplastsGeneral Physics and AstronomyBiologyMembrane FusionThylakoidsGeneral Biochemistry Genetics and Molecular BiologyBacterial ProteinsCentrifugation Density GradientIntegral membrane proteinMultidisciplinaryGalactolipidsPeripheral membrane proteinSynechocystisLipid bilayer fusionfood and beveragesPhosphatidylglycerolsGeneral ChemistryTransmembrane proteinCell biologyChloroplastMembraneThylakoidLiposomesQuantasomeGlycolipidsProtein BindingNature Communications
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Protein/lipid coaggregates are formed during α-synuclein-induced disruption of lipid bilayers.

2014

Amyloid formation is associated with neurodegenerative diseases such as Parkinson's disease (PD). Significant α-synuclein (αSN) deposition in lipid-rich Lewy bodies is a hallmark of PD. Nonetheless, an unraveling of the connection between neurodegeneration and amyloid fibrils, including the molecular mechanisms behind potential amyloid-mediated toxic effects, is still missing. Interaction between amyloid aggregates and the lipid cell membrane is expected to play a key role in the disease progress. Here, we present experimental data based on hybrid analysis of two-photon-microscopy, solution small-angle X-ray scattering and circular dichroism data. Data show in real time changes in liposome …

Circular dichroismAmyloidPolymers and PlasticsAmyloidLipid BilayersBioengineeringProtein Structure SecondaryBiomaterialsCell membraneMaterials ChemistrymedicineScattering RadiationLipid bilayerSpectroscopyLiposomeLaurdanAdvanced MicroscopyChemistryCircular DichroismX-RaysNeurodegenerationCell MembraneLipid bilayer fusionProteinsmedicine.diseaseamyloid-membrane interactionco-aggregatemedicine.anatomical_structureMembraneBiophysicsalpha-SynucleinLewy BodiesBiomacromolecules
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