Search results for "bilayer"

showing 10 items of 391 documents

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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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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Cholesterol reporter molecules.

2007

Cholesterol is a major constituent of the membranes in most eukaryotic cells where it fulfills multiple functions. Cholesterol regulates the physical state of the phospholipid bilayer, affects the activity of several membrane proteins, and is the precursor for steroid hormones and bile acids. Cholesterol plays a crucial role in the formation of membrane microdomains such as “lipid rafts” and caveolae. However, our current understanding on the membrane organization, intracellular distribution and trafficking of cholesterol is rather poor. This is mainly due to inherent difficulties to label and track this small lipid. In this review, we describe different approaches to detect cholesterol in …

Cholesterol oxidaseBacterial ToxinsBiophysicsBiologyBiochemistryFilipinchemistry.chemical_compoundHemolysin ProteinsMembrane MicrodomainsCaveolaeAnimalsHumansFilipinLipid bilayerMolecular BiologyLipid raftFluorescent DyesCholesterolCholesterol OxidaseCholesterol bindingCell BiologyCholesterolEukaryotic CellschemistryMembrane proteinBiochemistryMolecular Probeslipids (amino acids peptides and proteins)Bioscience reports
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Cholesterol–Protein Interaction: Methods and Cholesterol Reporter Molecules

2010

Cholesterol is a major constituent of the plasma membrane in eukaryotic cells. It regulates the physical state of the phospholipid bilayer and is crucially involved in the formation of membrane microdomains. Cholesterol also affects the activity of several membrane proteins, and is the precursor for steroid hormones and bile acids. Here, methods are described that are used to explore the binding and/or interaction of proteins to cholesterol. For this purpose, a variety of cholesterol probes bearing radio-, spin-, photoaffinity- or fluorescent labels are currently available. Examples of proven cholesterol binding molecules are polyene compounds, cholesterol-dependent cytolysins, enzymes acce…

Cholesterolmedicine.medical_treatmentCholesterol bindingSteroidProtein–protein interactionchemistry.chemical_compoundchemistryMembrane proteinBiochemistryMembrane fluiditymedicinelipids (amino acids peptides and proteins)Cholesterol 24-hydroxylaseLipid bilayer
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Development of predictive retention-activity relationship models of non-steroidal anti-inflammatory drugs by micellar liquid chromatography: comparis…

2000

The predictive and interpretative capability of quantitative chromatographic retention-biological activity models is supported by the fact that under adequate experimental conditions the solute partitioning into chromatographic system can emulate the solute partitioning into lipid bilayers of biological membranes, which is the basis for drug and metabolite uptake, passive transport across membranes and bioaccumulation. The use of micellar solutions of Brij35 as mobile phases in reversed-phase liquid chromatography has proven to be valid to predict some biological activities of different kinds of drugs. In this study, quantitative retention-activity relationship (QRAR) models to describe som…

ChromatographyPassive transportMetaboliteAnti-Inflammatory Agents Non-SteroidalSynthetic membraneBiological membraneMembranes ArtificialGeneral Chemistrychemistry.chemical_compoundStructure-Activity RelationshipMembranechemistryMicellar liquid chromatographyPredictive Value of TestsMicellar solutionsLipid bilayerChromatography LiquidJournal of chromatography. B, Biomedical sciences and applications
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How copper ions and membrane environment influence the structure of the human and chicken tandem repeats domain?

2019

Abstract Prion proteins (PrPs) from different species have the enormous ability to anchor copper ions. The N-terminal domain of human prion protein (hPrP) contains four tandem repeats of the –PHGGGWGQ– octapeptide sequence. This octarepeat domain can bind up to four Cu2+ ions. Similarly to hPrP, chicken prion protein (chPrP) is able to interact with Cu2+ through the tandem hexapeptide -HNPGYP- region (residues 53–94). In this work, we focused on the human octapeptide repeat (human Octa4, hPrP60–91) (Ac-PHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQ-NH2) and chicken hexapeptide repeat (chicken Hexa4, chPrP54–77) (Ac-HNPGYPHNPGYPHNPGYPHNPGYP-NH2) prion protein fragments. Due to the fact that PrP is a membr…

Circular dichroism010402 general chemistry01 natural sciencesBiochemistryMicelleInorganic Chemistrychemistry.chemical_compoundMembrane LipidsTandem repeatPeptide bondAnimalsHumansAmino Acid SequenceSodium dodecyl sulfateLipid bilayerMembrane mimicking environmentMicelleschemistry.chemical_classification010405 organic chemistryChemistryCopper ionsSodium Dodecyl SulfateHistidine residues0104 chemical sciencesPrion proteinsMembraneTandem Repeat SequencesBiophysicsPotentiometryThermodynamicsGlycoproteinChickensCopper
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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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