Search results for " Bovine"

showing 10 items of 151 documents

Biocompatibility and staining properties of CdSe\CdS\SiO2 nanoparticles for in-vitro biomaterials characterization

2015

Semiconductor nanocrystals, known as quantum dots (QDs) display well-tuned emission spectra from ultraviolet to the infrared region. Their photostability is greatly enhanced compared to fluorophores making them suitable for optical bio-imaging. In this work we have studied the cytocompatibility of CdSe\CdS\SiO2 QDs towards bovine articular chondrocytes in order to establish if these nanoparticles could be used as staining system forcells in tissue engineering purposes. Studies of QDs uptake and cell viability were conducted through morphology evaluation and MTS test. The adhesion behavior of chondrocytes deposited onto scaffolds of a derivative of hyaluronic acid functionalized with octadec…

Settore CHIM/09 - Farmaceutico Tecnologico ApplicativoSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Silica Quantum Dots Bovine chondrocytes cell hyaluronic acid fluorescence confocal microscopy
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Protein delivery based on uncoated and chitosan-coated mesoporous silicon microparticles

2011

Mesoporous silicon is a biocompatible, biodegradable material that is receiving increased attention for pharmaceutical applications due to its extensive specific surface. This feature enables to load a variety of drugs in mesoporous silicon devices by simple adsorption-based procedures. In this work, we have addressed the fabrication and characterization of two new mesoporous silicon devices prepared by electrochemistry and intended for protein delivery, namely: (i) mesoporous silicon microparticles and (ii) chitosan-coated mesoporous silicon microparticles. Both carriers were investigated for their capacity to load a therapeutic protein (insulin) and a model antigen (bovine serum albumin) …

SiliconMaterials scienceSiliconBSAchemistry.chemical_elementNanotechnology02 engineering and technology010402 general chemistryPorous silicon01 natural sciencesChitosanchemistry.chemical_compoundDrug Delivery SystemsColloid and Surface ChemistryAdsorptionPorous siliconElectrochemistryAnimalsInsulinPhysical and Theoretical ChemistryBovine serum albuminChitosanbiologyProteintechnology industry and agricultureProteinsSerum Albumin BovineSurfaces and InterfacesGeneral Medicine021001 nanoscience & nanotechnologyequipment and suppliesControlled release0104 chemical sciencesMesoporous organosilicachemistryMicroscopy Electron Scanningbiology.proteinElectrochemical pore formationCattle:Investigación::33 Ciencias tecnológicas::3312 Tecnología de materiales [Materias]0210 nano-technologyMesoporous materialBiotechnology
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Synthetic Haptens and Monoclonal Antibodies to the Cyanotoxin Anatoxin‐a

2019

Early warning systems for monitoring toxic events may benefit from the availability of monoclonal antibodies enabling the sensitive and specific detection of anatoxin-a, a cyanotoxin involved in numerous cases of animal poisoning resulting from toxic algal blooms in freshwaters. Through the synthesis of three functionalized derivatives of anatoxin-a, we have succeeded in generating the first-ever reported immunoreagents (bioconjugates and antibodies) suitable for the development of immunoanalytical approaches aimed at rapid and onsite detection of this harmful cyanotoxin.

Specific detectionmedicine.drug_classHarmful Algal BloomEnzyme-Linked Immunosorbent AssayAnimal poisoningBiology010402 general chemistryMonoclonal antibody01 natural sciencesAlgal bloomCatalysisAnatoxin-aMicrobiologychemistry.chemical_compoundmedicineAnimalsCyanobacteria Toxins010405 organic chemistryAntibodies MonoclonalSerum Albumin BovineStereoisomerismGeneral ChemistryCyanotoxin0104 chemical scienceschemistrybiology.proteinCattleAntibodyHaptensHaptenTropanesAngewandte Chemie International Edition
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Albumin-driven disassembly of lipidic nanoparticles: the specific case of the squalene-adenosine nanodrug

2020

International audience; In the field of nanomedicine, nanostructured nanoparticles (NPs) made of self-assembling prodrugs emerged in the recent years with promising properties. In particular, squalene-based drug nanoparticles have already shown their efficiency through in vivo experiments. However, a complete pattern of their stability and interactions in the blood stream is still lacking. In this work we assess the behavior of squalene-adenosine (SQAd) nanoparticles-whose neuroprotective effect has already been demonstrated in murine models-in the presence of fetal bovine serum (FBS) and of bovine serum albumin (BSA), the main protein of blood plasma. Extensive physicochemical characteriza…

SqualeneAdenosinecomplexationserum albuminSerum albumin02 engineering and technologyPlasma protein binding010402 general chemistry01 natural sciencesMiceDrug StabilitymedicineAnimalsHumansGeneral Materials ScienceProdrugsColloidsBovine serum albuminComputingMilieux_MISCELLANEOUSBinding Sitesbiology[CHIM.ORGA]Chemical Sciences/Organic chemistryChemistryAlbuminIsothermal titration calorimetry[CHIM.MATE]Chemical Sciences/Material chemistry021001 nanoscience & nanotechnologyHuman serum albumindisassembly0104 chemical sciencesnanodrugbiology.proteinBiophysicsNanomedicineNanoparticles0210 nano-technologyFetal bovine serummedicine.drugProtein Binding
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A POLYCARBOXYLIC/AMINO FUNCTIONALIZED HYALURONIC ACID DERIVATIVE FOR THE PRODUCTION OF pH SENSIBLE HYDROGELS IN THE PREVENTION OF BACTERIAL ADHESION …

2014

A graft copolymer derivative of hyaluronic acid bearing pendant amino and short polymethacrylate portions (HA-EDA-BMP-MANa) has been employed for the production of a pH sensible vancomycin releasing hydrogel and studied in vitro to test its potential anti adhesive property against Staphylococcus aureus colonization. The copolymer obtained through atom transfer radical polymerization bears chargeable (carboxyl and amino groups) portions and it could be formulated as a hydrogel at a concentration of 10% w/v. The HA-EDA-BMP-MANa hydrogels, produced at three different pH values (5, 6 and 7, respectively), were formulated with or without the addition of vancomycin (2% w/v). The vancomycin releas…

Staphylococcus aureushydrogels HYALURONIC ACID BACTERIAL ADHESIONPharmaceutical Sciencemedicine.disease_causeSettore BIO/19 - Microbiologia GeneraleBacterial Adhesionchemistry.chemical_compoundVancomycinHyaluronic acidmedicineCopolymerOrganic chemistryHyaluronic AcidTitaniumAtom-transfer radical-polymerizationtechnology industry and agricultureHydrogelsSerum Albumin BovineAdhesionHydrogen-Ion ConcentrationEthylenediaminesQuaternary Ammonium CompoundsDrug LiberationchemistryStaphylococcus aureusSettore CHIM/09 - Farmaceutico Tecnologico ApplicativoSelf-healing hydrogelsMicroscopy Electron ScanningVancomycinMethacrylatesPropionatesDerivative (chemistry)medicine.drugNuclear chemistry
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Thermal Aggregation of Bovine Serum Albumin in Trehalose and Sucrose Aqueous Solutions

2012

We report results of static and dynamic light scattering measurements performed on bovine serum albumin (BSA) in saccharide (trehalose and sucrose) solutions. Our aim is to study the effects of the two disaccharides on the first steps of thermal aggregation of BSA in aqueous solutions at two protein concentrations (1 and 30 mg/mL) at increasing sugar/water ratio. Results show that sugars modify early stages of aggregation mainly by perturbing the thermodynamic behavior of the solvent (i.e., general solvent effects) without involving direct, specific sugar-protein interactions. This agrees with current hypotheses on sugar action in protein solutions. (1-3) The linear correlation detected bet…

SucroseSucrosechemistry.chemical_compoundDynamic light scatteringMaterials ChemistryAnimalsTransition TemperaturePhysical and Theoretical ChemistryBovine serum albuminProtein Structure QuaternarySugarChromatographyAqueous solutionbiologyTemperatureTrehaloseWaterSerum Albumin BovineTrehaloseSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Surfaces Coatings and FilmsSolutionsSolventtrehalose protein aggregation solvent effects light scatteringchemistrySolventsbiology.proteinCattleProtein MultimerizationSolvent effectsThe Journal of Physical Chemistry B
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Synthetic vaccines consisting of tumor-associated MUC1 glycopeptide antigens and bovine serum albumin.

2005

Vaccines SyntheticbiologyChemistryMolecular Sequence DataMucin-1Serum albuminGlycopeptidesSerum Albumin BovineStereoisomerismGeneral ChemistryCancer VaccinesCatalysisGlycopeptideBiochemistryAntigenCarbohydrate Sequencebiology.proteinCarbohydrate ConformationAnimalsHumansCattleCarbohydrate conformationBovine serum albuminMUC1Angewandte Chemie (International ed. in English)
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Synthetic vaccines of tumor-associated glycopeptide antigens by immune-compatible thioether linkage to bovine serum albumin.

2007

Vaccines SyntheticbiologyMolecular StructureGlycopeptidesSerum Albumin BovineGeneral ChemistrySulfidesCancer VaccinesCatalysisGlycopeptidechemistry.chemical_compoundImmune systemBiochemistryAntigenThioetherchemistryAntigens Neoplasmbiology.proteinAnimalsCattleBovine serum albuminAngewandte Chemie (International ed. in English)
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The foaming properties of camel and bovine whey: The impact of pH and heat treatment

2018

International audience; he effect of heat treatment (70 degrees C or 90 degrees C for 30 min) on the foaming and interfacial properties of acid and sweet whey obtained from bovine and camel fresh milk was examined. The maximum foamability and foam stability were observed for acid whey when compared to sweet whey for both milks, with higher values for the camel whey. This behavior for acid whey was explained by the proximity of the pI of whey protein (4.9-5.2), where proteins were found to carry the lowest negative charge as confirmed by the zeta potential measurements. Interfacial properties of acid camel whey and acid bovine whey were preserved at air water interface even after a heat trea…

Whey proteinHot TemperatureAir water interfaceCamel and bovine wheyAnalytical Chemistryfluids and secretions[SDV.IDA]Life Sciences [q-bio]/Food engineeringZeta potentialmixed layersFood scienceBeta-lactoglobulinbiologybeta-lactoglobulinChemistrypHdigestive oral and skin physiology[ SDV.IDA ] Life Sciences [q-bio]/Food engineeringaggregationfood and beverages04 agricultural and veterinary sciencesGeneral MedicineHydrogen-Ion Concentration040401 food science[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]lactoferrinmilk-proteinsendocrine systemCamelusanimal structuresHeat treatmentinterfacesFresh milk0404 agricultural biotechnologyWheyNegative chargeFoaming propertiesalpha-lactalbuminAnimals[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]adsorption behaviorChromatographydromedarius milkViscoelastic modulus0402 animal and dairy sciencestability040201 dairy & animal scienceWhey ProteinsAlpha-lactalbuminbiology.proteinCattle[SDV.AEN]Life Sciences [q-bio]/Food and NutritionFood Science
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Flavour retention and release from protein solutions

2006

International audience; This paper briefly presents the main results obtained up to now on protein–flavour binding and release in relation with flavour perception. Among the food proteins, β-lactoglobulin is the most extensively studied for its binding properties, which involve both hydrophobic and hydrogen binding. Recent developments using molecular modelling and Quantitative Structure–Activity Relationship confirmed the existence of two different binding sites for flavour compounds on β-lactoglobulin. During the aroma release process in the mouth, not only free aroma compounds are released but also those reversibly bound by the protein, pointing out the fact that flavour perception is on…

[SDV.BIO]Life Sciences [q-bio]/BiotechnologyPROTEINSFlavourBioengineeringLactoglobulins01 natural sciencesApplied Microbiology and Biotechnology0404 agricultural biotechnologyComputational chemistryCyclohexenesHumansBinding siteAromaStrong bindingFlavorBinding SitesbiologyFLAVOUR RELEASETerpenesChemistry010401 analytical chemistryBinding propertiesfood and beveragesSerum Albumin Bovine04 agricultural and veterinary sciencesHydrogen-Ion ConcentrationMilk Proteinsbiology.organism_classification040401 food science0104 chemical sciences[SDV.BIO] Life Sciences [q-bio]/BiotechnologyFlavoring AgentsBiochemistryBenzaldehydesTasteFLAVOUR BINDINGSoybean ProteinsFood TechnologyLimoneneProtein BindingBiotechnology
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