Search results for "Bilayer"

showing 10 items of 391 documents

Solid State NMR Structure Analysis of the Antimicrobial Peptide Gramicidin S in Lipid Membranes: Concentration-Dependent Re-alignment and Self-Assemb…

2008

Antimicrobial peptides can kill bacteria by permeabilizing their cell membrane, as these amphiphilicmolecules interact favourably with lipid bilayers. This mechanism of action is attributed eitherto the formation of a peptide “carpet” on the membrane surface, or to a transmembranepore. However, the structure of such a pore has not yet been resolved under relevant conditions.Gramicidin S is a symmetrical cyclic β-sheet decapeptide, which has been previouslyshown by solid state NMR to lie flat on the membrane surface at low peptide:lipid ratios (≤ 1:80).Using highly sensitive 19F-NMR, supported by 15N-labelling,we found that gramicidin S can flip into an upright transmembrane alignment at hig…

chemistry.chemical_classificationchemistry.chemical_compoundMembranechemistryPeripheral membrane proteinMembrane fluidityBiophysicsOrganic chemistryPeptideLipid bilayer phase behaviorGramicidin SModel lipid bilayerLipid bilayer
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Cationic Au Nanoparticle Binding with Plasma Membrane-like Lipid Bilayers: Potential Mechanism for Spontaneous Permeation to Cells Revealed by Atomis…

2014

Despite being chemically inert as a bulk material, nanoscale gold can pose harmful side effects to living organisms. In particular, cationic Au nanoparticles (AuNP+) of 2 nm diameter or less permeate readily through plasma membranes and induce cell death. We report atomistic simulations of cationic Au nanoparticles interacting with realistic membranes and explicit solvent using a model system that comprises two cellular compartments, extracellular and cytosolic, divided by two asymmetric lipid bilayers. The membrane-AuNP+ binding and membrane reorganization processes are discovered to be governed by cooperative effects where AuNP+, counterions, water, and the two membrane leaflets all contr…

chemistry.chemical_classificationta114ta221Cationic polymerizationNanoparticlePermeationSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsGeneral EnergyMembranechemistryExtracellularBiophysicsOrganic chemistryPhysical and Theoretical ChemistryCounterionLipid bilayerta116Cellular compartment
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Block copolymers in giant unilamellar vesicles with proteins or with phospholipids

2013

Biocompatible, highly water-soluble, nonionic, amphiphilic block copolymers having different hydrophobic blocks and architectures, but similar molecular size and chemical nature of the hydrophilic blocks, were investigated to check for their ability to form hybrid giant unilamellar vesicles with proteins, and for their interactions with giant unilamellar phospholipid vesicles (GUV). PGM14-b-PPO34-b-PGM14 (PGM-PPO-PGM) consists of a poly(propylene oxide) middle block and outer poly(glycerol monomethacrylate) blocks. Ch-PEG32-b-lPG18 (Ch-PEG-lPG) and Ch-PEG30-b-hbPG17 (Ch-PEG-hbPG) have a linear poly(ethylene glycol) block, linked to a cholesterol end group and to a linear (lPG) or hyperbranc…

chemistry.chemical_compoundEnd-groupchemistryChemical engineeringVesicleAmphiphilePolymer chemistryPolymersomePhospholipidCopolymerPhysical and Theoretical ChemistryLipid bilayerEthylene glycolFaraday Discussions
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Atomic Force Microscopy: Interaction Forces Measured in Phospholipid Monolayers, Bilayers, and Cell Membranes

2009

Atomic force microscopy (AFM) is a powerful technique which is commonly used to image surfaces at the nanoscale and single-molecule level, as well as to investigate physical properties of the sample surface using a technique known as force spectroscopy. In this chapter, we review our recent research where we used AFM to investigate physical properties of phospholipid monolayers, bilayers, and cell membranes. We describe the experimental procedures for AFM imaging, force measurements, and theoretical models to analyze force spectroscopy data. The data obtained allowed correlations between AFM topography and local adhesion and mechanoelastic properties of supported lipid bilayers in water, su…

chemistry.chemical_compoundMembraneMaterials sciencePulmonary surfactantchemistryMonolayertechnology industry and agricultureForce spectroscopyBiophysicsPhospholipidAdhesionLipid bilayerNanoscopic scale
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Studies on the interaction of C1q,a subcomponent of the first component of complement, with porins fromSalmonella minnesotaincorporated into artifici…

1990

AbstractPurified outer membrane proteins (OMP) of Salmonella minnesota, Re-form, were incorporated into liposomes. These induced in macrophages a chemiluminescence signal identical to that of the intact Re-form. This signal was abolished by preincubation of porin-containing liposomes with purified C1q. Incorporation of isolated OMP into black lipid membranes (BLM) resulted in channel-formation which could not be inhibited by isolated C1q. Additionally, incubation of OMP-containing liposomes with BLM resulted in pore-formation within the BLM. This was amplified when lipid A was present within the liposomes. Preincubation of OMP-containing liposomes with purified C1q abolished pore-formation …

congenital hereditary and neonatal diseases and abnormalitiesLuminescenceMacrophageLipid BilayersBiophysicsSynthetic membranePorinschemical and pharmacologic phenomenaBiochemistryIon ChannelsMembrane PotentialsLipid AMiceSalmonellaStructural BiologyGeneticsAnimalsHumansBlack lipid membraneLipid bilayerMolecular BiologyC1qCells CulturedMice Inbred BALB CLiposomeurogenital systemChemistryComplement C1qMacrophagesElectric Conductivitynutritional and metabolic diseasesMembranes ArtificialCell BiologyLiposomeKineticsCholesterolMembraneMembrane proteinBiochemistryOuter membrane proteinPorinPhosphatidylcholinesbacteriaBacterial outer membraneBacterial Outer Membrane ProteinsFEBS Letters
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Liposomes modified by mono- and bis-phthalocyanines: A comprehensive EPR study.

2016

The impact of selected metallophthalocyanines, featuring diverse molecular structure, upon the fluidity of liposome membranes was studied using the spin label EPR technique. The “mono”-type MPc’s (M = Zn, Sn; Pc = C32H16N8 is the phthalocyanine ligand) and sandwich LnPc2 complexes (Ln = Nd, Sm, Gd) were explored. Liposomes were obtained in a sonication process, from egg yolk lecithin (EYL) in water. TEMPO and 16-DOXYL spin labels were used to monitor the peripheral and central part of the lipid double layer, respectively, which allowed to localize the phthalocyanine additive within the bilayer, as well as to perform independent measurements of changes in fluidity upon addition thereof. All …

food.ingredientBiophysics02 engineering and technologyLecithinlaw.inventionCyclic N-Oxides03 medical and health scienceschemistry.chemical_compoundSonication0302 clinical medicineNuclear magnetic resonancefoodlawLecithinsOrganometallic CompoundsGeneral Materials ScienceLipid bilayerElectron paramagnetic resonanceSpin labelLiposomeChemistryLiquid crystalsBilayerElectron Spin Resonance SpectroscopySurfaces and InterfacesGeneral Chemistry021001 nanoscience & nanotechnologyCrystallographyMembraneSoft Matter030220 oncology & carcinogenesisLiposomesPhthalocyanine0210 nano-technologyBiotechnologyThe European physical journal. E, Soft matter
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Cooperativity of Protein Binding to Vesicles

2011

Electrostatics role is studied in protein adsorption to phosphatidylcholine (PC) and PC/phosphatidylglycerol (PG) small unilamellar vesicles (SUVs). Protein interaction is monitored vs. PG content at low ionic strength. Adsorption of lysozyme, myoglobin and bovine serum albumin (BSA) isoelectric point (pI) is investigated in SUVs, along with changes in protein fluorescence emission spectra. Partition coefficients and cooperativity parameters are calculated. At pI, binding is maximum while at lower/higher pHs binding drops. In Gouy–Chapman model activity coefficient goes with square charge number, which deviations indicate asymmetric location of anionic lipid in the bilayer inner leaflet, in…

genetic structuresbiologyBilayerVesicleBinding proteinCooperativitychemistry.chemical_compoundIsoelectric pointMyoglobinchemistrybiology.proteinBiophysicsBovine serum albuminProtein adsorption
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Viroporins, Examples of the Two-Stage Membrane Protein Folding Model

2015

Viroporins are small, α-helical, hydrophobic virus encoded proteins, engineered to form homo-oligomeric hydrophilic pores in the host membrane. Viroporins participate in multiple steps of the viral life cycle, from entry to budding. As any other membrane protein, viroporins have to find the way to bury their hydrophobic regions into the lipid bilayer. Once within the membrane, the hydrophobic helices of viroporins interact with each other to form higher ordered structures required to correctly perform their porating activities. This two-step process resembles the two-stage model proposed for membrane protein folding by Engelman and Poppot. In this review we use the membrane protein folding …

influenza A virus M2Protein Foldingviroporinslcsh:QR1-502ReviewBiologyhelix-helix packinglcsh:MicrobiologyCell membraneViral ProteinsVirologymedicinetransmembrane protein foldingAnimalsHumansmembrane insertionLipid bilayerCell MembraneVirologyTransmembrane proteinVirusFolding (chemistry)Transmembrane domainGenòmicaInfectious DiseasesMembranemedicine.anatomical_structureMembrane proteinVirus DiseasesVirusesBiophysicsProtein foldingProteïnesGenètica
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Nitrated Fatty Acids Modulate the Physical Properties of Model Membranes and the Structure of Transmembrane Proteins

2017

Nitrated fatty acids (NO2 -FAs) act as anti-inflammatory signal mediators, albeit the molecular mechanisms behind NO2 -FAs' influence on diverse metabolic and signaling pathways in inflamed tissues are essentially elusive. Here, we combine fluorescence measurements with surface-specific sum frequency generation vibrational spectroscopy and coarse-grained computer simulations to demonstrate that NO2 -FAs alter lipid organization by accumulation at the membrane-water interface. As the function of membrane proteins strongly depends on both, protein structure as well as membrane properties, we consecutively follow the structural dynamics of an integral membrane protein in presence of NO2 -FAs. …

inorganic chemicals0301 basic medicineProtein Conformationcomplex mixturesPhase TransitionCatalysisPhysical Phenomena03 medical and health sciences0302 clinical medicineProtein structureJournal ArticleFluorescence Resonance Energy TransferMembrane fluidityComputer SimulationLipid bilayerIntegral membrane proteinNitratesChemistryCircular DichroismCell MembraneFatty AcidsOrganic ChemistryPeripheral membrane proteinMembrane ProteinsGeneral Chemistryrespiratory systemLipidsTransmembrane protein030104 developmental biologyMembraneMembrane proteinBiochemistryBiophysics030217 neurology & neurosurgerySignal TransductionChemistry – A European Journal
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Investigation of the dynamics of bacteriorhodopsin

1990

Bacteriorhodopsin (bR) converted to the blue form by deionization has been reconstituted to the active purple membrane by addition of57Fe ions. Mossbauer spectra measured in a wide temperature range reveal Fe3+ binding places with oxygen atoms in the neighbourhood. No evidence for a well defined functional binding place of the iron has been found. On a timescale faster 100 ns the purple membrane shows increasing flexibility above 200 K. In order to analyse the influence of the lipids, a bacteriorhodopsin sample where the lipid content has been increased artificially by the incorporation of DMPC as well as a sample consisting of lipid bilayer have been investigated.

inorganic chemicalsNuclear and High Energy PhysicsbiologyChemistryBacteriorhodopsinAtmospheric temperature rangeCondensed Matter PhysicsAtomic and Molecular Physics and OpticsIonCrystallographyMembraneOxygen atomLipid contentbiology.proteinMossbauer spectraPhysical and Theoretical ChemistryLipid bilayerHyperfine Interactions
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