Search results for "ion channels"

showing 10 items of 137 documents

Ion transport and selectivity in nanopores with spatially inhomogeneous fixed charge distributions

2007

Polymeric nanopores with fixed charges show ionic selectivity when immersed in aqueous electrolyte solutions. The understanding of the electrical interaction between these charges and the mobile ions confined in the inside nanopore solution is the key issue in the design of potential applications. The authors have theoretically described the effects that spatially inhomogeneous fixed charge distributions exert on the ionic transport and selectivity properties of the nanopore. A comprehensive set of one-dimensional distributions including the skin, core, cluster, and asymmetric cases are analyzed on the basis of the Nernst-Planck equations. Current-voltage curves, nanopore potentials, and tr…

Models MolecularMaterials scienceStatic ElectricityGeneral Physics and AstronomyIonic bondingNanotechnologyElectrolyteIon ChannelsNanoporous materialsIonQuantitative Biology::Subcellular ProcessesElectrolytesBiopolymersIonic conductivityStatic electricityCluster (physics)Ionic conductivityComputer SimulationPhysical and Theoretical Chemistry:FÍSICA::Química física [UNESCO]AnisotropyIon TransportUNESCO::FÍSICA::Química físicaNanostructuresNanoporeModels ChemicalPolymer solutionsChemical physicsNanoporous materials ; Polymer solutions ; Electrolytes ; Ionic conductivityAnisotropyIon Channel GatingPorosityThe Journal of Chemical Physics
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Peptides Derived from Apoptotic Bax and Bid Reproduce the Poration Activity of the Parent Full-Length Proteins

2005

Bax and Bid are proapoptotic proteins of the Bcl-2 family that regulate the release of apoptogenic factors from mitochondria. Although they localize constitutively in the cytoplasm, their apoptotic function is exerted at the mitochondrial outer membrane, and is related to their ability to form transbilayer pores. Here we report the poration activity of fragments from these two proteins, containing the first alpha-helix of a colicinlike hydrophobic hairpin (alpha-helix 5 of Bax and alpha-helix 6 of Bid). Both peptides readily bind to synthetic lipid vesicles, where they adopt predominantly alpha-helical structures and induce the release of entrapped calcein. In planar lipid membranes they fo…

Models MolecularMolecular Sequence DataBiophysicsApoptosisPeptideIn Vitro TechniquesBiophysical PhenomenaIon ChannelsPermeabilityProtein Structure Secondarychemistry.chemical_compoundBcl-2-associated X proteinSpectroscopy Fourier Transform InfraredHumansChannels Receptors and Electrical SignalingAmino Acid SequencePeptide sequenceIon channelbcl-2-Associated X Proteinchemistry.chemical_classificationbiologyChemistryCircular DichroismPeptide FragmentsCell biologyCalceinMembraneProto-Oncogene Proteins c-bcl-2CytoplasmMultiprotein ComplexesLiposomesbiology.proteinPèptidsCarrier ProteinsBacterial outer membraneProteïnesBH3 Interacting Domain Death Agonist ProteinBiophysical Journal
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Molecular and topological membrane folding determinants of transient receptor potential vanilloid 2 channel.

2015

Transient Receptor Potential (TRP) channels are related to adaptation to the environment and somatosensation. The transient receptor potential vanilloid (TRPV) subfamily includes six closely evolutionary related ion channels sharing the same domain organization and tetrameric arrangement in the membrane. In this study we have characterized biochemically TRPV2 channel membrane protein folding and transmembrane (TM) architecture. Deleting the first N-terminal 74 residues preceding the ankyrin repeat domain (ARD) show a key role for this region in targeting the protein to the membrane. We have demonstrated the co-translational insertion of the membrane-embedded region of the TRPV2 and its disp…

Models MolecularVesicle-associated membrane protein 8Protein FoldingTRPV5Protein ConformationBiophysicsTRPV Cation ChannelsBiochemistryTRPVTransient receptor potential channelAnimalsHumansProtein Structure QuaternaryMolecular BiologyIon channelTransmembrane channelsChemistryCell MembraneCell BiologyTransmembrane proteinRecombinant ProteinsAnkyrin RepeatProtein Structure TertiaryRatsHEK293 CellsBiochemistryBiophysicsAnkyrin repeatBiochemical and biophysical research communications
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Cluster organization and pore structure of ion channels formed by beticolin 3, a nonpeptidic fungal toxin

1999

Beticolin 3 (B3) belongs to a family of nonpeptidic phytotoxins produced by the fungus Cercospora beticola, which present a broad spectrum of cytotoxic effects. We report here that, at cytotoxic concentration (10 microM), B3 formed voltage-independent, weakly selective ion channels with multiple conductance levels in planar lipid bilayers. In symmetrical standard solutions, conductance values of the first levels were, respectively, 16 +/- 1 pS, 32 +/- 2 pS, and 57 +/- 2 pS (n = 4) and so on, any conductance level being roughly twice the lower one. Whether a cluster organization of elementary channels or different channel structures underlies this particular property was addressed by investi…

Models Molecular[SDV]Life Sciences [q-bio]Lipid BilayersMolecular ConformationBiophysicsIn Vitro Techniques010402 general chemistryHeterocyclic Compounds 4 or More Rings01 natural sciencesBiophysical PhenomenaIon ChannelsMembrane Potentials03 medical and health sciencesElectrical resistivity and conductivityCluster (physics)Lipid bilayerIon channelComputingMilieux_MISCELLANEOUS030304 developmental biologyMembrane potential0303 health sciencesChemistryElectric ConductivityConductanceBiological activityMycotoxins0104 chemical sciencesCrystallographySelectivityResearch Article
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Complement lysis: a hole is a hole.

1991

recent experimental advances 21, it is now possible to produce MACs with a precise molecular composition 7 for better designed experiments. In my judgement, however, it will always be problematic to propose a single unifying mechanism for MAC action simply because MAC effects are not uniform. The reason for attempting to classify MACs as leaky patch or channel formers is a desire to wield Occam's razor and carve out the simplest unifying theory. But this razor often cuts one's throat, especially when it comes to immunological processes. A system that degranulates platelets, 'kills' such widely diverse targets as artificial liposomes, 'dead' viruses and erythrocytes, metabolically active cel…

Molecular compositionCell Membrane PermeabilityComputer scienceNuclear EnvelopeCarve outImmunologyoccamComplement System ProteinsTopologyHemolysisModels BiologicalIon ChannelsComplement (complexity)Patch formationAction (philosophy)Channel (programming)Humanscomputercomputer.programming_languageSimple (philosophy)Immunology today
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Killer-toxin-resistant kre12 mutants of Saccharomyces cerevisiae: genetic and biochemical evidence for a secondary K1 membrane receptor.

1995

The Saccharomyces cerevisiae killer toxin K1 is a secreted alpha/beta-heterodimeric protein toxin that kills sensitive yeast cells in a receptor-mediated two-stage process. The first step involves toxin binding to beta-1,6-D-glucan-components of the outer yeast cell surface; this step is blocked in yeast mutants bearing nuclear mutations in any of the KRE genes whose products are involved in synthesis and/or assembly of cell wall beta-D-glucans. After binding to the yeast cell wall, the killer toxin is transferred to the cytoplasmic membrane, subsequently leading to cell death by forming lethal ion channels. In an attempt to identify a secondary K1 toxin receptor at the plasma membrane leve…

MutantSaccharomyces cerevisiaeGenes FungalReceptors Cell SurfaceSaccharomyces cerevisiaeSpheroplastsBiologymedicine.disease_causeBiochemistryMicrobiologyModels BiologicalIon ChannelsFungal ProteinsCell surface receptorCell WallGeneticsmedicineMolecular BiologyDiphtheria toxinToxinMembrane ProteinsDrug Resistance MicrobialGeneral MedicineSpheroplastMycotoxinsbiology.organism_classificationYeastKiller Factors YeastBiochemistryMembrane proteinMutationArchives of microbiology
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Current rectification by nanoparticle blocking in single cylindrical nanopores.

2014

Blocking of a charged pore by an oppositely charged nanoparticle can support rectifying properties in a cylindrical nanopore, as opposed to the usual case of a fixed asymmetry in the pore geometry and charge distribution. We present here experimental data and model calculations to confirm this fundamental effect. The nanostructure imaging and the effects of nanoparticle concentration, pore radius, and salt concentration on the electrical conductance–voltage (G–V) curves are discussed. Logic responses based on chemical and electrical inputs/outputs could also be implemented with a single pore acting as an effective nanofluidic diode. To better show the generality of the results, different ch…

NanostructureMaterials scienceNanoparticleIonic bondingTransportNanotechnologyElectronQuantitative Biology::Subcellular ProcessesNanoporesRectificationElectrical resistivity and conductivityGeneral Materials ScienceQuantitative Biology::BiomoleculesMembranesPolyethylene TerephthalatesElectric ConductivityCharge densityAntibiotic moleculesNanoporePoresChemical physicsIon channelsFISICA APLICADAMicroscopy Electron ScanningNanoparticlesGradientNanoscale
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Co-expression of heat sensitive vanilloid receptor subtypes in rat dorsal root ganglion neurons

2003

Expression of the heat sensitive cation channels TRPV1 and TRPV2 was investigated by immunofluorescence in rat dorsal root ganglion (DRG) neurons. TRPV1-positive neurons were more frequent and had smaller diameters than TRPV2-positive neurons (35.7% vs 7.3%; 22.3 microm vs 27.6 microm), but size distributions overlapped and significant co-expression was seen in 20.7% of TRPV2-positive neurons (1.7% of all). Expression patterns did not differ between tissue sections typically used in immunocytochemistry and dissociated DRG neurons typically used in electrophysiology. Rectangular temperature pulses revealed two patterns of heat-evoked inward currents in small DRG neurons: low-threshold rapidl…

NeuronsHot TemperatureReceptors DrugGeneral NeuroscienceTRPV2ImmunocytochemistryCentral nervous systemTRPV1TRPV Cation ChannelsBiologySpinal cordRatsRats Sprague-DawleyElectrophysiologymedicine.anatomical_structureGene Expression Regulationnervous systemDorsal root ganglionGanglia SpinalmedicineBiophysicsAnimalsNeuronNeuroscienceNeuroReport
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Conformational changes in acetylcholine binding protein investigated by temperature accelerated molecular dynamics.

2014

Despite the large number of studies available on nicotinic acetylcholine receptors, a complete account of the mechanistic aspects of their gating transition in response to ligand binding still remains elusive. As a first step toward dissecting the transition mechanism by accelerated sampling techniques, we study the ligand-induced conformational changes of the acetylcholine binding protein (AChBP), a widely accepted model for the full receptor extracellular domain. Using unbiased Molecular Dynamics (MD) and Temperature Accelerated Molecular Dynamics (TAMD) simulations we investigate the AChBP transition between the apo and the agonist-bound state. In long standard MD simulations, both confo…

Nicotinic Acetylcholine ReceptorsProtein ConformationGatingMolecular DynamicsLigandsBiochemistryBiophysics SimulationsIon ChannelsMolecular dynamicsAcetylcholine bindingComputational ChemistryBiochemical SimulationsNicotinic AgonistsBiomacromolecule-Ligand InteractionsBiochemistry SimulationsMultidisciplinaryHydrogen bondChemistryPhysicsQTemperatureRLigand (biochemistry)nicotinic receptor molecular dynamics tamd acethylcholine binding proteinChemistryNicotinic agonistBiochemistryMedicineBiophysic Al SimulationsResearch ArticleProtein BindingProtein subunitScienceBiophysicsMolecular Dynamics SimulationProtein ChemistryStatistical MechanicsChemical BiologyAnimalsBiologyAcetylcholine receptorBinding SitesProteinsComputational BiologyHydrogen BondingSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Protein SubunitsMolluscaAcetylcholine ReceptorsBiophysicsLobelineCarrier ProteinsPLoS ONE
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Desensitization is a property of the cholinergic binding region of the nicotinic acetylcholine receptor, not of the receptor-integral ion channel

1991

AbstractThe reversible acetylcholine esterase inhibitor (−)-physostigmine (eserine) is the prototype of a new class of nicotinic acetylcholine receptor (nAChR) activating ligands: it induces cation fluxes into nAChR-rich membrane vesicles from Torpedo marmorala electric tissue even under conditions of antagonist blocked acetylcholine binding sites (Okonjo, Kuhlmann, Maclicke, Neuron, in press). This suggests that eserine exerts its channel-activating property via binding sites at the nAChR separate from those of the natural transmitter. We now report that eserine can activate the channel even when the receptor has been preincubated (desensitized) with elevated concentrations of acetylcholin…

Nicotinic acetylcholine receptorStereochemistryAcetylcholine-gated cation channelPhysostigmineBiophysicsCesiumIon fluxDesensitizationIn Vitro TechniquesReceptors NicotinicTorpedoBiochemistryIon ChannelsAnticholinesteraseAcetylcholine bindingGanglion type nicotinic receptorStructural BiologyMuscarinic acetylcholine receptor M5GeneticsmedicineAnimalsMolecular BiologyAcetylcholine receptorBinding SitesChemistryCell BiologyBungarotoxinsAcetylcholineNicotinic acetylcholine receptorNicotinic agonistCarbamateBiophysicsCholinergicAcetylcholineEserinemedicine.drugFEBS Letters
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