Search results for "bilayers"

showing 10 items of 140 documents

Derivation of coarse-grained simulation models of chlorophyll molecules in lipid bilayers for applications in light harvesting systems

2015

The correct interplay of interactions between protein, pigment and lipid molecules is highly relevant for our understanding of the association behavior of the light harvesting complex (LHCII) of green plants. To cover the relevant time and length scales in this multicomponent system, a multi-scale simulation ansatz is employed that subsequently uses a classical all atomistic (AA) model to derive a suitable coarse grained (CG) model which can be backmapped into the AA resolution, aiming for a seamless conversion between two scales. Such an approach requires a faithful description of not only the protein and lipid components, but also the interaction functions for the indispensable pigment mo…

ChlorophyllModels MolecularChlorophyll bChlorophyll aChlorophyll ABilayerLipid BilayersLight-Harvesting Protein ComplexesGeneral Physics and AstronomyLight-harvesting complexchemistry.chemical_compoundCrystallographychemistryChemical physicsChlorophyllddc:540MoleculeProtein MultimerizationPhysical and Theoretical ChemistryProtein Structure QuaternaryLipid bilayerAnsatz
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Coupling of Cholesterol and Cone-shaped Lipids in Bilayers Augments Membrane Permeabilization by the Cholesterol-specific Toxins Streptolysin O and V…

2001

Abstract Vibrio cholerae cytolysin (VCC) forms oligomeric pores in lipid bilayers containing cholesterol. Membrane permeabilization is inefficient if the sterol is embedded within bilayers prepared from phosphatidylcholine only but is greatly enhanced if the target membrane also contains ceramide. Although the enhancement of VCC action is stereospecific with respect to cholesterol, we show here that no such specificity applies to the two stereocenters in ceramide; all four stereoisomers of ceramide enhanced VCC activity in cholesterol-containing bilayers. A wide variety of ceramide analogs were as effective asd-erythro-ceramide, as was diacylglycerol, suggesting that the effect of ceramide …

Cholera ToxinCeramideCell Membrane PermeabilityLipid BilayersBiologyCeramidesBiochemistrychemistry.chemical_compoundBacterial ProteinsPhosphatidylcholineLipid bilayerNuclear Magnetic Resonance BiomolecularVibrio choleraeMolecular BiologyDiacylglycerol kinaseCytotoxinsCell BiologyLipid MetabolismLipidsSphingolipidSterolCholesterolchemistryBiochemistryStreptolysinslipids (amino acids peptides and proteins)StreptolysinCytolysinJournal of Biological Chemistry
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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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Conformational transitions of gramicidin A in phospholipid model membranes. A high-performance liquid chromatography assessment.

1991

We have investigated the conformation of gramicidin A reconstituted in different phospholipid environments, small unilamellar vesicles, extensive bilayers, and micelles by exploiting a recently proposed experimental approach based on high-performance liquid chromatography [Bano et al. (1988) J. Chromatogr. 458, 105; Bano et al. (1989) FEBS Lett. 250, 67]. The method allows the separation of conformational species of the peptide namely, antiparallel double-stranded (APDS) dimers and β 6.3 -helical monomers, and quantitation of their proportions in the lipid environment. Various experimental parameters (e.g., nature of organic solvent, time of incubation in organic solvent, lipid-to-peptide m…

Circular dichroismChromatographyProtein ConformationLipid BilayersSynthetic membranePhospholipidGramicidinBiochemistryMicellePeptide ConformationTurn (biochemistry)chemistry.chemical_compoundKineticsSonicationMembranechemistryGramicidinSolventsChromatography High Pressure LiquidPhospholipidsBiochemistry
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A semi-empirical approach for the simulation of circular dichroism spectra of gramicidin A in a model membrane

1992

In an extension of our previous work (Bañó, M. C., Braco, L., and Abad, C. 1991. Biochemistry. 30:886-94), the kinetics of dissociation of gramicidin A double-stranded dimers into beta 6.3-helical monomers in small unilamellar vesicles prepared following different protocols, were investigated using in combination circular dichroism (CD) and high-performance liquid chromatography (HPLC). The analysis of the data from both techniques according to a two-component model strongly supports that any given CD pattern of gramicidin incorporated in the phospholipid bilayer can be deconvoluted essentially as a linear combination of the reference subspectra calculated for the double-stranded dimer and …

Circular dichroismProtein ConformationChemistryCircular DichroismDimerLipid BilayersGramicidinSynthetic membraneBiophysicsMembranes ArtificialBiophysical PhenomenaDissociation (chemistry)KineticsCrystallographychemistry.chemical_compoundMembraneMonomerModels ChemicalGramicidinLipid bilayerResearch ArticleBiophysical Journal
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Structural characterisation of the natural membrane-bound state of melittin: a fluorescence study of a dansylated analogue

1997

Abstract The binding of a dansylated analogue of melittin (DNC–melittin) to natural membranes is described. The cytolytic peptide from honey bee venom melittin was enzymatically labelled in its glutamine-25 with the fluorescent probe monodansylcadaverine using guinea pig liver transglutaminase. The labelled peptide was characterised functionally in cytolytic assays, and spectroscopically by circular dichroism and fluorescence. The behaviour of DNC–melittin was, in all respects, indistinguishable from that of the naturally occurring peptide. We used resonance energy transfer to measure the state of aggregation of melittin on the membrane plane in synthetic and natural lipid bilayers. When bo…

Circular dichroismProtein ConformationGlutamineGuinea PigsLipid BilayersBiophysicsPeptideHemolysiscomplex mixturesBiochemistryMelittinchemistry.chemical_compoundCadaverinePhosphatidylcholineAnimalsHumansLipid bilayerFluorescent Dyeschemistry.chemical_classificationBinding SitesTransglutaminasesCircular DichroismDansyl labelingtechnology industry and agricultureMembrane structureMelittinFluorescence energy transferCell BiologyMelittenFluorescenceSpectrometry FluorescenceMembraneEnergy TransferLiverBiochemistrychemistryBiophysicslipids (amino acids peptides and proteins)Natural membraneLipid-protein interactionProtein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
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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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Probes for studying cholesterol binding and cell biology.

2011

Cholesterol is a multifunctional lipid in eukaryotic cells. It regulates the physical state of the phospholipid bilayer, is crucially involved in the formation of membrane microdomains, affects the activity of many membrane proteins, and is the precursor for steroid hormones and bile acids. Thus, cholesterol plays a profound role in the physiology and pathophysiology of eukaryotic cells. The cholesterol molecule has achieved evolutionary perfection to fulfill its different functions in membrane organization. Here, we review basic approaches to explore the interaction of cholesterol with proteins, with a particular focus on the high diversity of fluorescent and photoreactive cholesterol prob…

Clinical BiochemistryLipid BilayersBiologyBiochemistryCell membranechemistry.chemical_compoundEndocrinologyMembrane MicrodomainsmedicineAnimalsHumansLipid bilayerMolecular BiologyPhospholipidsG protein-coupled receptorFluorescent DyesPharmacologyCyclodextrinsBinding SitesCholesterolOrganic ChemistryCholesterol bindingCell MembraneMembrane ProteinsSterolSterol regulatory element-binding proteinCell biologymedicine.anatomical_structureCholesterolEukaryotic CellsMembrane proteinBiochemistrychemistryMolecular Probeslipids (amino acids peptides and proteins)Steroids
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Structural investigation of the confinement of finite amounts of trehalose in water-containing sodium bis(2-ethylhexyl)sulfosuccinate reversed micell…

2006

The structural effect of trehalose confined in water-containing sodium bis(2-ethylhexyl)sulfosuccinate (AOT) reversed micelles at water to AOT molar ratio W = 5 and 10 as a function of the trehalose to AOT molar ratio T (0 < T < 0.1) has been investigated by small-angle neutron scattering (SANS). SANS data analysis is consistent with the hypothesis that trehalose is encapsulated within the quite spherical hydrophilic micellar cores of water-containing reversed micelles, causing an increase of the aggregate size and a decrease of the polydispersion. Moreover, SANS results suggest that the trehalose confinement in water-containing reversed micelles involves marked changes on the molecular pac…

DYNAMICSBILAYERSPROTEINSSodiumIntercalation (chemistry)chemistry.chemical_elementVITRIFICATIONMicelleANGLE NEUTRON-SCATTERINGchemistry.chemical_compoundPulmonary surfactantMICROEMULSIONSPhase (matter)Materials ChemistrymedicineMoleculeOrganic chemistryDehydrationPhysical and Theoretical ChemistrySUCROSEChemistryHYDRATIONmedicine.diseaseTrehaloseSurfaces Coatings and FilmsChemical engineering
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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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