Search results for "muramidase"

showing 10 items of 45 documents

Nanoparticle Assembly of Surface-Modified Proteins

2016

Nature's biomaterials such as peptides and proteins represent a valuable source of highly defined macromolecules. Herein we developed a nanoparticle drug delivery system based on the assembly of surface-modified proteins that can be transferred into organic solvents and represent the structural material of the carrier system. The particles are prepared by an oil-in-water nanoemulsion technique without the need of additional denaturation or cross-linking steps for stabilization. We achieve the necessary lipophilic solubility switch of the protein material by high surface PEGylation under conservation of the native three-dimensional protein structure. This study focuses on lysozyme as model e…

Carrier systemCell SurvivalSurface PropertiesNanoparticleNanotechnology02 engineering and technology010402 general chemistry01 natural sciencesBiochemistryCatalysisStructure-Activity RelationshipColloid and Surface ChemistryProtein structureHumansDenaturation (biochemistry)Particle SizeSolubilityDrug CarriersDose-Response Relationship DrugChemistryGeneral Chemistry021001 nanoscience & nanotechnology0104 chemical sciencesDoxorubicinDrug deliveryBiophysicsPEGylationNanoparticlesMuramidase0210 nano-technologyHeLa CellsMacromoleculeJournal of the American Chemical Society
researchProduct

Existence of metastable intermediate lysozyme conformation highlights the role of alcohols in altering protein stability.

2011

Alcohols have a manifold effect on the conformational and thermodynamic stability of native proteins. Here, we study the effect of moderate concentrations of trifluoroethanol (TFE) on the thermal stability of hen egg-white lysozyme (HEWL), by far-UV circular dichroism and by steady-state and time-resolved photoluminescence of intrinsic tryptophans. Our results highlight that TFE affects lysozyme stability by preferential solvation of the protein molecule. Furthermore, we discovered the existence at 20% TFE of an equilibrium partially folded state of lysozyme, intermediate between the native and the unfolded state. A three-state model is therefore used to interpolate the thermal denaturation…

Circular dichroismProtein DenaturationSupramolecular chemistryProtein Structure Secondarychemistry.chemical_compoundProtein structureMaterials ChemistryMoleculeAnimalsThermal stabilityPhysical and Theoretical ChemistryProtein UnfoldingProtein StabilityLysozyme TFE Stability FibrillationCircular DichroismSolvationTemperatureTrifluoroethanolSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Surfaces Coatings and FilmsCrystallographychemistryAlcoholsChemical stabilityMuramidaseLysozymeChickensThe journal of physical chemistry. B
researchProduct

Squaric Acid Mediated Synthesis and Biological Activity of a Library of Linear and Hyperbranched Poly(Glycerol)-Protein Conjugates

2012

Polymer-protein conjugates generated from side chain functional synthetic polymers are attractive because they can be easily further modified with, for example, labeling groups or targeting ligands. The residue specific modification of proteins with side chain functional synthetic polymers using the traditional coupling strategies may be compromised due to the nonorthogonality of the side-chain and chain-end functional groups of the synthetic polymer, which may lead to side reactions. This study explores the feasibility of the squaric acid diethyl ester mediated coupling as an amine selective, hydroxyl tolerant, and hydrolysis insensitive route for the preparation of side-chain functional, …

GlycerolModels MolecularCovalent AttachmentPolymers and PlasticsPolymersBioengineeringSquaric acidImmunological PropertiesLigandsSmall Molecule LibrariesBiomaterialsHydrolysischemistry.chemical_compoundResidue (chemistry)Thiazolidine-2-ThioneMaterials ChemistrySide chainCopolymerOrganic chemistryBovine Serum-Albuminchemistry.chemical_classificationPoly(Ethylene Glycol)Molecular StructureCopolymersPolymer StructureSerum Albumin BovinePolymerPolyethylene-GlycolMolecular WeightPolyglycerolschemistryMuramidaseAmine gas treatingFunctional polymersCyclobutanesDerivatives
researchProduct

Inhibition of ubiquitin-dependent proteolysis by a synthetic glycine-alanine repeat peptide that mimics an inhibitory viral sequence.

2002

AbstractThe glycine–alanine repeat (GAr) of the Epstein–Barr virus nuclear antigen-1 is a cis-acting transferable element that inhibits ubiquitin/proteasome-dependent proteolysis in vitro and in vivo. We have here examined the effect of a synthetic 20-mer GAr oligopeptide on the degradation of iodinated or biotin labeled lysozyme in a rabbit reticulocyte lysates in vitro assay. Micromolar concentrations of the GA-20 peptide inhibited the hydrolysis of lysozyme without significant effect on ubiquitination. Addition of the peptide did not inhibit the hydrolysis of fluorogenic substrate by purified proteasomes and did not affect the ubiquitination of lysozyme. An excess of the peptide failed t…

Herpesvirus 4 HumanProteasome Endopeptidase ComplexGly–Ala repeatPolymersProteolysisMolecular Sequence DataBiophysicsGlycineBiotinPeptideBiochemistryIodine Radioisotopeschemistry.chemical_compoundS5aUbiquitinStructural BiologyMultienzyme ComplexesGeneticsmedicineAnimalsAmino Acid SequenceEnzyme InhibitorsMolecular BiologyPeptide sequenceUbiquitinsEpstein–Barr virus nuclear antigen-1Alaninechemistry.chemical_classificationOligopeptideAlaninebiologymedicine.diagnostic_testProteasomeMolecular MimicryUbiquitinationCell BiologyCysteine EndopeptidasesBiochemistryProteasomechemistryEpstein-Barr Virus Nuclear AntigensIsotope Labelingbiology.proteinMuramidaseRabbitsLysozymeCarrier ProteinsPeptidesOligopeptidesFEBS letters
researchProduct

Role of Solvent on Protein-Matrix Coupling in MbCO Embedded in Water-Saccharide Systems: A Fourier Transform Infrared Spectroscopy Study

2006

AbstractEmbedding protein in sugar systems of low water content enables one to investigate the protein dynamic-structure function in matrixes whose rigidity is modulated by varying the content of residual water. Accordingly, studying the dynamics and structure thermal evolution of a protein in sugar systems of different hydration constitutes a tool for disentangling solvent rigidity from temperature effects. Furthermore, studies performed using different sugars may give information on how the detailed composition of the surrounding solvent affects the internal protein dynamics and structural evolution. In this work, we compare Fourier transform infrared spectroscopy measurements (300–20K) o…

Hot TemperatureProtein ConformationBiophysicsLactosechemistry.chemical_compoundProtein structureRaffinosePolysaccharidesSpectroscopy Fourier Transform InfraredCarbohydrate ConformationFourier transform infrared spectroscopySugarSpectroscopyMaltosechemistry.chemical_classificationMyoglobinBiomoleculeProtein dynamicsTrehaloseWaterProteinsTrehaloseSolventCrystallographyGlucosechemistryChemical physicsSolventsMuramidaseBiophysical Journal
researchProduct

Additive effects of enhanced ambient ultraviolet B radiation and increased temperature on immune function, growth and physiological condition of juve…

2009

Climate change models predict increased ultraviolet B (UVB) radiation levels due to stratospheric ozone depletion and global warming. In order to study the impact of these two environmental stressors acting simultaneously on the physiology of fish, Atlantic salmon parr were exposed, for 8 weeks in outdoor tanks, to different combinations of UVB radiation (depleted and enhanced) and temperature (standard rearing temperature of 14 °C or 19 °C). The immune function (plasma IgM, lysozyme activity and complement bacteriolytic activity), growth (body weight) and physiological condition (haematocrit and plasma protein concentration) of the fish were determined. Increased UVB level, regardless of w…

Hot TemperatureUltraviolet RaysClimate ChangeSalmo salarAquatic ScienceHot Temperaturechemistry.chemical_compoundAnimal scienceImmune systemEnvironmental ChemistryAnimalsSalmoAnimal HusbandrybiologyEcologyPhysiological conditionBody WeightGeneral MedicineComplement System Proteinsbiology.organism_classificationOzone depletionBlood proteinschemistryImmunoglobulin MImmunoglobulin Mbiology.proteinMuramidaseLysozymeFishshellfish immunology
researchProduct

Poly(N-isopropylacrylamide)-gated Fe3O4/SiO2 core shell nanoparticles with expanded mesoporous structures for the temperature triggered release of ly…

2015

Core-shell nanoparticles comprised of Fe3O4 cores and a mesoporous silica shell with an average expanded pore size of 6.07 nm and coated with a poly(N-isopropylacrylamide) (PNIPAM) layer (CS MSNs EP PNIPAM) were prepared and characterized. The nanoparticles was loaded with (Ru(bipy)3 2+) dye or an antibacterial enzyme, lysozyme, to obtain CS MSNs EP PNIPAM Ru(bipy)3 2+ and CS MSNs EP PNIPAM Lys, respectively. The lysozyme loading was determined to be 160 mg/g of nanoparticle. It was seen that Ru(bipy)3 2+ and lysozyme release was minimal at a room temperature of 25 ºC while at physiological temperature (37 º C), abrupt release was observed. The applicability of the CS MSNs EP PNIPAM Lys was…

INGENIERIA DE LA CONSTRUCCIONSilicon dioxideAcrylic ResinsBiomedical EngineeringNanoparticleBioengineeringchemistry.chemical_compoundPNIPAMQUIMICA ORGANICAColloid and Surface ChemistryBacillus cereusBIOQUIMICA Y BIOLOGIA MOLECULARNanotechnologyFerrous CompoundsPhysical and Theoretical ChemistryChemical PhysicsChromatographybiologyProtein deliveryQUIMICA INORGANICATemperatureTriggered releaseSurfaces and InterfacesGeneral MedicineChemical EngineeringMesoporous silicaSilicon Dioxidebiology.organism_classificationAnti-Bacterial AgentsMicrococcus luteuschemistryDrug deliveryPoly(N-isopropylacrylamide)NanoparticlesMuramidaseLysozymePore expansionMesoporous materialMicrococcus luteusPorosityMesoporous silicaPhysical Chemistry (incl. Structural)BiotechnologyNuclear chemistryColloids and Surfaces B: Biointerfaces
researchProduct

Influence of ligand density on the properties of metal-chelate affinity supports.

1993

A new procedure has been developed to immobilize iminodiacetic acid (IDA) onto the surface of silica supports, such as LiChrospher Si-1000 and 1.5-microns nonporous silica, for use in high-performance immobilized metal affinity chromatography (HPIMAC) of proteins. This IDA immobilization method has been achieved through the synthesis of a new silylation reagent, 1-(iminodiacetic acid di-tert-butylester)-3-glycidoxy-propyltrimethoxysilane (IDA-silane). Various modified silicas of different ligand densities have been prepared by using mixtures between 1 and 100% of the IDA-silane diluted with the corresponding 3-glycidoxy-propyltrimethoxysilane (GLYMO-silane). Frontal analysis was used with t…

Iminodiacetic acidInorganic chemistryBiophysicsLigandsBiochemistryChromatography AffinityCoordination complexMetalchemistry.chemical_compoundAdsorptionAffinity chromatographyConcanavalin AChelationMolecular BiologyChelating Agentschemistry.chemical_classificationChromatographyChemistryLigandImino AcidsProteinsCell BiologySilicon DioxideEvaluation Studies as Topicvisual_artReagentvisual_art.visual_art_mediumMuramidaseAdsorptionCopperAnalytical biochemistry
researchProduct

Interactions of lysozyme with hydrophilic and hydrophobic polymethacrylate stationary phases in reversed phase chromatography (RPC)

1994

Two silicas, one with a mean pore diameter of 30 nm and the other non-porous, were coated with polymethacrylates of increasing hydrophobicity in the sequence: poly-2-hydroxyethylmethacrylate (P2HEMA)1 polyethylmethacrylate (PEMA) and poly-n-octylmethacrylate (POMA). Association constants, Kass, between lysozyme and the coated silicas were determined by means of frontal analysis, and the apparent heats of adsorption, delta Happ, by means of microcalorimetry. Using Kass and delta Happ the changes in the apparent free energy, delta Gapp, and in the apparent entropy, delta Sapp, were calculated at a concentration of lysozyme < 10 mumol/l. The association between the lysozyme and the coated sili…

Isothermal microcalorimetryChromatographyChromatographyChemical PhenomenaChemistry PhysicalKineticsBiophysicsReversed-phase chromatographyElectrolyteCalorimetryCalorimetrySodium perchlorateBiochemistryKineticsCrystallographychemistry.chemical_compoundAdsorptionchemistryMethacrylatesMethylmethacrylatesThermodynamicsMuramidaseLysozymePolyhydroxyethyl MethacrylateJournal of Biochemical and Biophysical Methods
researchProduct

Characterization of the nucleation process of lysozyme at physiological pH: Primary but not sole process

2013

We report on a kinetic study of the heat-induced aggregation process of lysozyme at physiological pH. The time evolution of the aggregation extent and the conformational changes of the protein were followed by dynamic light scattering (DLS) and FTIR spectroscopy, respectively, whereas the morphology of the aggregates was observed by Atomic Force Microscopy (AFM). The conformational changes of the secondary and tertiary structures were simultaneous and distinct in time with respect to the formation of aggregates. Oligomer formation occurred through at least two different aggregation processes: a nucleation process and a homogeneous non-nucleative diffusion-controlled process. FTIR measuremen…

LightNucleation proceBiophysicsSupramolecular chemistryNucleationmacromolecular substancesProtein aggregationMicroscopy Atomic ForceBiochemistryOligomerProtein Structure Secondarychemistry.chemical_compoundDynamic light scatteringSpectroscopy Fourier Transform InfraredAnimalsScattering RadiationFourier transform infrared spectroscopyCircular DichroismOrganic ChemistryTemperaturetechnology industry and agricultureHydrogen-Ion ConcentrationProtein Structure TertiaryAmorphous solidFTIR spectroscopyCrystallographychemistryChemical engineeringDynamic light scatteringMuramidaseAFMProtein aggregationLysozymeChickensBiophysical Chemistry
researchProduct