Search results for "Biotin"

showing 10 items of 127 documents

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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Novel biosensor-based analytic device for the detection of anti-double-stranded DNA antibodies.

2007

AbstractBackground: Patients with systemic lupus erythematosus (SLE) develop a wide variety of serologic manifestations, including double-stranded DNA autoantibodies (anti-dsDNA). The determination of the potentially pathogenic autoantibodies is diagnostically relevant.Methods: We developed a novel surface plasmon resonance (SPR) biosensor chip for studies of dsDNA and anti-dsDNA binding. A synthetic oligonucleotide was coupled to biotinylated human transferrin, hybridized with the complementary antistrand, and ligated with a human recombinant dsDNA fragment 233 bp in length. After surface immobilization of this antigenic construct, diluted sera from SLE patients and healthy donors were ana…

Clinical BiochemistryPilot ProjectsBiosensing TechniquesBiologySensitivity and Specificitylaw.inventionchemistry.chemical_compoundAntigenimmune system diseaseslawHumansLupus Erythematosus SystemicSurface plasmon resonanceskin and connective tissue diseasesOligonucleotideBiochemistry (medical)DNASurface Plasmon ResonanceMolecular biologyReceptor–ligand kineticschemistryBiotinylationAntibodies AntinuclearRecombinant DNABiosensorDNAClinical chemistry
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Small-molecule affinity capture of DNA/RNA quadruplexes and their identification in vitro and in vivo through the G4RP protocol

2019

International audience; Guanine-rich DNA and RNA sequences can fold into higher-order structures known as G-quadruplexes (or G4-DNA and G4-RNA, respectively). The prevalence of the G4 landscapes in the human genome, transcriptome and ncRNAome (non-coding RNA), collectively known as G4ome, is strongly suggestive of biological relevance at multiple levels (gene expression , replication). Small-molecules can be used to track G4s in living cells for the functional characterization of G4s in both normal and disease-associated changes in cell biology. Here, we describe biotinylated biomimetic ligands referred to as Bio-TASQ and their use as molecular tools that allow for isolating G4s through aff…

Computational biologyBiologyG-quadruplexLigandsTranscriptome03 medical and health scienceschemistry.chemical_compound0302 clinical medicineChemical Biology and Nucleic Acid ChemistryGene expressionGeneticsHumansBiotinylation[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology030304 developmental biology0303 health sciencesGenome HumanReverse Transcriptase Polymerase Chain ReactionRNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyDNAG-QuadruplexeschemistryBiotinylationNucleic acidMCF-7 CellsRNAHuman genomeTranscriptome030217 neurology & neurosurgeryDNA
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Selective targeting of avidin/mannose 6-phosphate receptor chimeras to early or late endosomes

2000

Summary In this study we have used the Semliki forest virus expression system to transiently express chimeric proteins that contain transmembrane and cytoplasmic domains of the cation-independent mannose 6-phosphate receptor (CI-MPR) fused to chicken avidin. Immunofluorescence and electron microscopy studies showed that the chimeric protein with the entire cytoplasmic domain of CI-MPR was transported to late endosomes, where it accumulated. We made use of the biotin-binding capacity of lumenal avidin, and found that, in agreement with this distribution, the chimeric protein could be labelled with biotinylated HRP endocytosed for a long, but not a brief, period of time. However, truncation o…

CytoplasmTime FactorsHistologyEndosomeRecombinant Fusion ProteinsAmino Acid MotifsGreen Fluorescent ProteinsEndosomesEndocytosisReceptor IGF Type 2Pathology and Forensic Medicine03 medical and health sciencesCationsCricetinaeAnimalsBiotinylation030304 developmental biologyProtein Synthesis Inhibitors0303 health sciencesBrefeldin AMannose 6-phosphate receptorbiologyCell Membrane030302 biochemistry & molecular biologyPovidoneBiological TransportCell BiologyGeneral MedicineAvidinSilicon DioxideSemliki forest virusFusion proteinMolecular biologyEndocytosisTransmembrane proteinProtein Structure TertiaryLuminescent ProteinsMicroscopy ElectronTransmembrane domainCross-Linking ReagentsMicroscopy FluorescenceBiotinylationbiology.proteinCattleChickensDimerizationAvidinEuropean Journal of Cell Biology
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Dual-affinity avidin molecules

2005

A recently reported dual-chain avidin was modified further to contain two distinct, independent types of ligand-binding sites within a single polypeptide chain. Chicken avidin is normally a tetrameric glycoprotein that binds water-soluble d-biotin with extreme affinity (Kd ≈ 10−15M). Avidin is utilized in various applications and techniques in the life sciences and in the nanosciences. In a recent study, we described a novel avidin monomer-fusion chimera that joins two circularly permuted monomers into a single polypeptide chain. Two of these dual-chain avidins were observed to associate spontaneously to form a dimer equivalent to the wt tetramer. In the present study, we successfully used …

DimerBiochemistryChromatography AffinityProtein Structure Secondarychemistry.chemical_compoundBiotinAffinity chromatographyTetramerStructural BiologyAnimalsBinding siteMolecular BiologyFluorescent Dyeschemistry.chemical_classificationBinding SitesbiologyChemistryTemperatureAvidinBiochemistryBiotinylationbiology.proteinThermodynamicsGlycoproteinChickensProtein BindingAvidinProteins: Structure, Function, and Bioinformatics
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Mode of action of Bacillus thuringiensis PS86Q3 strain in hymenopteran forest pests

2001

The mode of action of Cry toxins has been described principally in lepidopteran insects as a multistep process. In this work we describe the mode of action of a Cry toxin active in the common pine sawfly Diprion pini (Hymenoptera, Diprionidae), considered a major forest pest in Europe. Strain PS86Q3 contains a long bipyramidal crystal composed of five major proteins. The N-terminal sequence shows that the 155 kDa protein corresponds to Cry5B toxin and the other proteins belong to the Cry5A subgroup. PCR analysis indicates the presence of cry5Ac and cry5Ba genes, suggesting that Cry5A protein should be Cry5Ac. Activation of protoxins with trypsin or with midgut content from D. pini and Cepha…

DiprionidaeBacterial ToxinsBacillus thuringiensisBiotinmedicine.disease_causeBiochemistryMicrobiologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisEndopeptidasesmedicineAnimalsMode of actionMolecular BiologyBacillus thuringiensis ToxinsbiologyToxinfungiMidgutTrypsinbiology.organism_classificationHymenopteraEndotoxinsEnzyme ActivationSawflyLarvaInsect ScienceDiprion pinimedicine.drugInsect Biochemistry and Molecular Biology
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Construction of an agglutination tool: recombinant Fab fragments biotinylated in vitro.

2009

The pComb3H vector system is used for constructing and panning recombinant antibody libraries. It allows for expression of monovalent Fab fragments, either on the surface of M13 phage, or in the form of soluble proteins secreted into the periplasmic space of bacteria. We constructed a modified pComb3H vector containing cDNA encoding for a 23-amino acid fragment of the Escherichia coli biotin carboxy carrier protein (BCCP), which is an acceptor sequence for biotinylation. The vector was used to express the Fab fragment recognizing human glycophorin A. The purified Fab fragment containing this biotin acceptor sequence was effectively biotinylated in vitro using biotin ligase (BirA). The speci…

ErythrocytesBlotting WesternBioengineeringlaw.inventionchemistry.chemical_compoundImmunoglobulin Fab FragmentsBiotinlawAgglutination TestsGlycophorinHumansBiotinylationGlycophorinsMolecular BiologybiologyChemistryHemagglutinationGeneral MedicinePeriplasmic spaceAvidinMolecular biologyPrimary and secondary antibodiesRecombinant ProteinsAgglutination (biology)BiochemistryBiotinylationbiology.proteinRecombinant DNAChromatography GelElectrophoresis Polyacrylamide GelBiotechnologyAvidinProtein BindingNew biotechnology
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Highly Homogeneous Biotinylated Carbon Nanodots: Red-Emitting Nanoheaters as Theranostic Agents toward Precision Cancer Medicine

2019

Very recent red-emissive carbon nanodots (CDs) have shown potential as near-infrared converting tools to produce local heat useful in cancer theranostics. Besides, CDs seem very appealing for clinical applications combining hyperthermia, imaging, and drug delivery in a single platform capable of selectively targeting cancer cells. However, CDs still suffer from dramatic dot-to-dot variability issues such that a rational design of their structural, optical, and chemical characteristics for medical applications has been impossible so far. Herein, we report for the first time a simple and highly controllable layer-by-layer synthesis of biotin-decorated CDs with monodisperse size distribution, …

Fluorescence-lifetime imaging microscopyphotothermal therapyMaterials scienceCell SurvivalAntineoplastic AgentsNanotechnology02 engineering and technology010402 general chemistrytargeted cancer therapy01 natural sciencesDrug Delivery Systemsbiotincarbon nanodotCell Line TumorCarbon nanodotsHumansGeneral Materials SciencePrecision MedicineRational designimagingPhotothermal therapy021001 nanoscience & nanotechnologyCarbonNanostructures0104 chemical sciencesbiotin; carbon nanodots; imaging; photothermal therapy; targeted cancer therapy.Settore CHIM/09 - Farmaceutico Tecnologico ApplicativoBiotinylationDrug deliveryCancer cellMCF-7 CellsSurface modification0210 nano-technologyACS Applied Materials & Interfaces
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Glycosylation deficiency at either one of the two glycan attachment sites of cellular prion protein preserves susceptibility to bovine spongiform enc…

2004

The conversion into abnormally folded prion protein (PrP) plays a key role in prion diseases. PrP(C) carries two N-linked glycan chains at amino acid residues 180 and 196 (mouse). Previous in vitro data indicated that the conversion process may not require glycosylation of PrP. However, it is conceivable that these glycans function as intermolecular binding sites during the de novo infection of cells on susceptible organisms and/or play a role for the interaction of both PrP isoforms. Such receptor-like properties could contribute to the formation of specific prion strains. However, in earlier studies, mutations at the glycosylation sites of PrP led to intracellular trafficking abnormalitie…

Genetically modified mouseGlycanGlycosylationGlycosylationPrionsanimal diseasesBovine spongiform encephalopathyMutantBlotting WesternScrapieMice TransgenicCHO CellsCell SeparationBiologyBiochemistryCell LinePrion Diseaseschemistry.chemical_compoundMicePolysaccharidesCell Line TumorCricetinaemedicineAnimalsImmunoprecipitationProtein IsoformsBiotinylationDisulfidesTransgenesCloning MolecularMolecular BiologyBinding SitesWild typeBrainCell Biologymedicine.diseaseFlow CytometryVirologyMolecular biologyIn vitronervous system diseasesEncephalopathy Bovine SpongiformMice Inbred C57BLchemistryMutationbiology.proteinCattleScrapieThe Journal of biological chemistry
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Synthesis and noncovalent protein conjugation of linear-hyperbranched PEG-poly(glycerol) alpha,omega(n)-telechelics.

2009

Linear-hyperbranched, heterobifunctional alpha,omega(n) telechelic block copolymers consisting of a linear poly(ethylene glycol) (PEG) chain and a hyperbranched polyglycerol (PG) block have been prepared in five steps, using a protected amino-functional initiator. The polyfunctionality omega(n) (OH groups) can be adjusted by the degree of polymerization (DP(n)) of the polyglycerol block. Subsequent introduction of a single biotin unit by amidation in alpha-position permitted noncovalent bioconjugation with avidin.

GlycerolBioconjugationbiologyPolymersProteinsGeneral ChemistryDegree of polymerizationBiochemistryCatalysisPolyethylene Glycolschemistry.chemical_compoundColloid and Surface ChemistrychemistryBiotinPEG ratioPolymer chemistryGlycerolbiology.proteinCopolymerBiotinylationEthylene glycolAvidinJournal of the American Chemical Society
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