Search results for "Avidin"

showing 10 items of 97 documents

Exploration of Fas S-Nitrosylation by the Biotin Switch Assay

2017

International audience; S-nitrosylation is the covalent attachment of nitric oxide radical to the thiol side chain of cysteine. The death receptor Fas/CD95 can be S-nitrosylated in cancer cell lines by NO donors or iNOS activation. This posttranslational modification (PTM) induces Fas aggregation into lipid rafts and enhances FasL-mediated signaling and apoptosis. In this report, we describe the detection of Fas S-nitrosylation by the most commonly used method, the biotin switch assay (BSA) technique, that allows the detection of this very labile covalent modification in cells or tissues. Briefly, this technique relies on the ability of ascorbate to reduce the covalent bond between the NO r…

0301 basic medicineBiotin switch assaybiologyChemistryNitrosylationNeutrAvidinNitric oxideS-NitrosylationFas receptorGlyceryl trinitrate3. Good health03 medical and health sciences030104 developmental biology0302 clinical medicineBiochemistryApoptosisCovalent bondFas S030220 oncology & carcinogenesisBiotinylationbiology.protein[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyLipid raft[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyCysteine
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Fishing for G-quadruplexes in solution with a perylene diimide derivative labeled with biotins

2018

A new fluorescent, non‐cytotoxic perylene diimide derivative with two biotins at the peri position, PDI2B, has been synthesized. This molecule is able to interact selectively with G‐quadruplexes with scarce or no affinity towards single‐ or double‐stranded DNA. These features have made it possible to design a simple, effective, safe, cheap, and selective method for fishing G‐quadruplex structures in solution by use of PDI2B and streptavidin coated magnetic beads. The new cyclic method reported leads to the recovery of more than 80 % of G‐quadruplex structures from solution, even in the presence of an excess of single‐stranded or duplex DNA as competitors. Moreover, PDI2B is a G4 ligand that…

0301 basic medicinePerilipin-1Surface PropertiesBiotinDNA Single-StrandedImidesLigandsCatalysisCatalysi03 medical and health sciencesheterocyclic compoundsPeryleneG-quadruplexeFluorescent DyesPerileneChemistryOrganic ChemistryQuímicaGeneral ChemistryDNAG-QuadruplexesSolutionsChemistry030104 developmental biologyBiophysicNucleic acidMagnetsChristian ministryStreptavidinHumanities
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Monitoring few molecular binding events in scalable confined aqueous compartments by raster image correlation spectroscopy (CADRICS)

2016

The assembly of scalable liquid compartments for binding assays in array formats constitutes a topic of fundamental importance in life sciences. This challenge can be addressed by mimicking the structure of cellular compartments with biological native conditions. Here, inkjet printing is employed to develop up to hundreds of picoliter aqueous droplet arrays stabilized by oil-confinement with mild surfactants (Tween-20). The aqueous environments constitute specialized compartments in which biomolecules may exploit their function and a wide range of molecular interactions can be quantitatively investigated. Raster Image Correlation Spectroscopy (RICS) is employed to monitor in each compartmen…

0301 basic medicineStreptavidinBiomedical EngineeringMolecular bindingBiotinBioengineeringNanotechnology02 engineering and technologydroplets microarrays inkjet printing Raster Image Correlation Spectroscopy water-in-oil emulsion StreptvidinBiochemistry03 medical and health scienceschemistry.chemical_compoundCompartment (pharmacokinetics)Cellular compartmentchemistry.chemical_classificationAqueous solutionSpectrum AnalysisBiomoleculeWaterGeneral Chemistrycomputer.file_formatMicroarray Analysis021001 nanoscience & nanotechnology030104 developmental biologychemistryPrintingInkStreptavidinRaster graphics0210 nano-technologycomputerTwo-dimensional nuclear magnetic resonance spectroscopyLab on a Chip
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Brain Delivery of Multifunctional Dendrimer Protein Bioconjugates

2018

Abstract Neurological disorders are undoubtedly among the most alarming diseases humans might face. In treatment of neurological disorders, the blood‐brain barrier (BBB) is a challenging obstacle preventing drug penetration into the brain. Advances in dendrimer chemistry for central nervous system (CNS) treatments are presented here. A poly(amido)amine (PAMAM) dendrimer bioconjugate with a streptavidin adapter for the attachment of dendrons or any biotinylated drug is constructed. In vitro studies on porcine or murine models and in vivo mouse studies are performed and reveal the permeation of dendronized streptavidin (DSA) into the CNS. The bioconjugate is taken up mainly by the caveolae pa…

0301 basic medicineStreptavidinblood‐brain barrierGeneral Chemical EngineeringGeneral Physics and AstronomyMedicine (miscellaneous)02 engineering and technologyBlood–brain barrierBiochemistry Genetics and Molecular Biology (miscellaneous)03 medical and health scienceschemistry.chemical_compoundIn vivoDendrimermedicinestreptavidinGeneral Materials SciencePAMAM dendrimerFull PaperGeneral EngineeringFull Papers021001 nanoscience & nanotechnologyIn vitro3. Good health030104 developmental biologymedicine.anatomical_structureTranscytosischemistryBiotinylationDrug deliverydrug deliveryBiophysics0210 nano-technologyAdvanced Science
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Double Thermoresponsive Block Copolymers Featuring a Biotin End Group

2010

A poly(oligo(ethylene glycol) monomethyl ether methacrylate)-block-poly(N-isopropyl methacrylamide) (POEGMA-b-PNIPMAM) block copolymer with a biotin end group on the PNIPMAM block as a biotarget was synthesized as a model system for temperature-controlled polymer immobilization. The synthesis was based on RAFT polymerization followed by postpolymerization modification of an activated ester precursor block and an exchange of the dithioester end group within one step. NMR, differential scanning calorimetry (DSC), dynamic light scattering (DLS), and turbidimetry measurements were performed to investigate the stimulus-responsive properties. The double thermoresponsive POEGMA-b-PNIPMAM with biot…

AcrylamidesMagnetic Resonance SpectroscopyCalorimetry Differential ScanningPolymers and PlasticsPolymersRadical polymerizationTemperaturetechnology industry and agricultureBiotinBioengineeringChain transferLower critical solution temperaturePolymerizationBiomaterialschemistry.chemical_compoundEnd-groupchemistryPolymer chemistryMaterials ChemistryCopolymerMethacrylamideReversible addition−fragmentation chain-transfer polymerizationStreptavidinEthylene glycolMicellesBiomacromolecules
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Mutation of the important Tyr-33 residue of chicken avidin: functional and structural consequences

2002

The strong interaction between avidin and biotin is so tight (dissociation constant 10-15M) that conditions usually sufficient for protein denaturing fail to dislodge biotin from the avidin—biotin complex. This kind of irreversible binding hinders the use of avidin in applications such as affinity purification or protein immobilization. To address this concern, we have constructed a series of mutants of the strategically positioned Tyr-33 in order to study the role of this residue in biotin binding, and to create avidin variants with more reversible ligand-binding properties. Unexpectedly, an avidin mutant in which Tyr-33 was replaced with phenylalanine (Avm-Y33F) displayed similar biotin-b…

Biotin bindingBiotinPlasma protein bindingLigandsBiochemistrychemistry.chemical_compoundBiotinAnimalsBinding siteMolecular BiologyBinding SitesMolecular StructurebiologyChemistryTemperatureHydrogen BondingCell BiologyHydrogen-Ion ConcentrationAvidinOxygenDissociation constantBiochemistryBiotinylationMutationMutagenesis Site-Directedbiology.proteinTyrosineProtein quaternary structureEndopeptidase KChickensProtein BindingResearch ArticleAvidinBiochemical Journal
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Enhanced Gene Delivery by Avidin-Displaying Baculovirus

2004

Flexible alteration of virus surface properties would be beneficial for enhanced and targeted gene delivery. A useful approach could be based on a high-affinity receptor–ligand pair, such as avidin and biotin. In this study, we have constructed an avidin-displaying baculovirus, Baavi. Avidin display was expected to enhance cell transduction due to the high positive charge of avidin in physiological pH and to provide a binding site for covering the virus with desired biotinylated ligands. Successful incorporation of avidin on the virus envelope was detected by immunoblotting and electron microscopy. Multiple biotin-binding sites per virus were detected with fluorescence-correlation spectrosc…

Biotin bindingGenetic VectorsBiotinBiosensing TechniquesBiologyGene deliveryCell Linechemistry.chemical_compoundTransduction (genetics)BiotinViral envelopeTransduction GeneticCell Line TumorDrug DiscoveryGeneticsAnimalsBiotinylationBinding siteMolecular BiologyPharmacologyEpidermal Growth FactorGene Transfer TechniquesAvidinMolecular biologyCell biologyRatsErbB ReceptorsSpectrometry FluorescencechemistryBiotinylationbiology.proteinMolecular MedicineRabbitsBaculoviridaeViral Fusion ProteinsAvidinProtein BindingMolecular Therapy
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Cloning and characterization of Scavidin, a fusion protein for the targeted delivery of biotinylated molecules.

2001

We have constructed a novel fusion protein "Scavidin" consisting of the macrophage scavenger receptor class A and avidin. The Scavidin fusion protein is transported to plasma membranes where the avidin portion of the fusion protein binds biotin with high affinity and forms the basis for the targeted delivery of biotinylated molecules. Subcellular fractionation analysis, immunostaining, and electron microscopy demonstrated endosomal localization of the fusion protein. According to pulse-labeling and cross-linking studies Scavidin is found as monomers (55 kDa), dimers, and multimers, of which the 220-kDa form was the most abundant. The biotin binding capacity and active endocytosis of the bio…

Biotin bindingRecombinant Fusion ProteinsBlotting WesternGenetic VectorsPlasma protein bindingBiologyEndocytosisLigandsBiochemistrychemistry.chemical_compoundProtein structureBiotinTransduction GeneticTumor Cells CulturedAnimalsBiotinylationCloning MolecularReceptors ImmunologicMicroscopy ImmunoelectronMolecular BiologyReceptors ScavengerModels GeneticCell MembraneGene Transfer TechniquesScavenger Receptors Class ACell BiologyGliomaAvidinBlotting NorthernFusion proteinImmunohistochemistryPrecipitin TestsEndocytosisProtein Structure TertiaryRatsCross-Linking ReagentsRetroviridaeBiochemistrychemistryMicroscopy FluorescenceBiotinylationbiology.proteinDimerizationAvidinProtein BindingThe Journal of biological chemistry
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Biotin Induces Tetramerization of a Recombinant Monomeric Avidin

2001

Chicken avidin, a homotetramer that binds four molecules of biotin was converted to a monomeric form by successive mutations of interface residues to alanine. The major contribution to monomer formation was the mutation of two aspartic acid residues, which together account for ten hydrogen bonding interactions at the 1-4 interface. Mutation of these residues, together with the three hydrophobic residues at the 1-3 interface, led to stable monomer formation in the absence of biotin. Upon addition of biotin, the monomeric avidin reassociated to the tetramer, which exhibited properties similar to those of native avidin, with respect to biotin binding, thermostability, and protease resistance. …

Biotin bindingbiologyProtein subunitCell BiologyBiochemistrychemistry.chemical_compoundMonomerchemistryBiotinTetramerBiochemistryBiotinylationbiology.proteinBiophysicsMolecular BiologyAvidinHomotetramerJournal of Biological Chemistry
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Organelle pH studies using targeted avidin and fluorescein–biotin

2000

Abstract Background: Mammalian organelles of the secretory pathway are of differing pH. The pH values form a decreasing gradient: the endoplasmic reticulum (ER) is nearly neutral, the Golgi is mildly acidic and the secretory granules are more acidic still (∼pH 5). The mechanisms that regulate pH in these organelles are still unknown. Results: Using a novel method, we tested whether differences in H + ‘leak' and/or counterion conductances contributed to the pH difference between two secretory pathway organelles. A pH-sensitive, membrane-permeable fluorescein–biotin was targeted to endoplasmic-reticulum- and Golgi-localized avidin-chimera proteins in HeLa cells. In live, intact cells, ER pH (…

Clinical BiochemistryBiotinGolgi ApparatusEndoplasmic ReticulumBiochemistrysymbols.namesakechemistry.chemical_compoundChloridesBiotinOrganelleDrug DiscoveryHumansMicroscopy ImmunoelectronMolecular BiologySecretory pathwayFluorescent DyesOrganellesPharmacologyIon TransportFlubi-2ChemistryEndoplasmic reticulumBafilomycinIntracellular MembranesGeneral MedicineHydrogen-Ion ConcentrationProton PumpsGolgi apparatusAvidinCytosolTargeted fluorescenceMembraneBiochemistryH+ pumpPotassiumsymbolsMolecular MedicineFluoresceinHeLa CellsH+ leakChemistry & Biology
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