Search results for "Human serum"

showing 10 items of 59 documents

Enantiomeric quality control of antihistamines in pharmaceuticals by affinity electrokinetic chromatography with human serum albumin as chiral select…

2007

The present paper deals with the enantiomeric separation of six antihistaminic enantiomers by affinity electrokinetic chromatography (AEKC)-partial filling technique using human serum albumin (HSA) as chiral selector. A multivariate optimization approach of the most critical experimental variables in enantioresolution, running pH, HSA concentration and HSA plug length (SPL) was carried out since there are interactions between variables that could not be considered in an univariate optimization. The estimated and experimental resolution values obtained for antihistaminic enantiomers varied from 1.13 (for orphenadrine) to 2.15 (for brompheniramine). The optimum experimental conditions for ena…

Quality ControlSerum albuminElectronsBeta-CyclodextrinsBiochemistryChromatography AffinityAnalytical ChemistryChlorcyclizineAffinity chromatographyOrphenadrinemedicineHumansEnvironmental ChemistrySerum AlbuminSpectroscopyChromatographybiologyChemistrybeta-CyclodextrinsStereoisomerismBrompheniramineHuman serum albuminSolutionsbody regionsKineticsPharmaceutical PreparationsCalibrationembryonic structuresHistamine H1 Antagonistsbiology.proteinEnantiomermedicine.drugAnalytica Chimica Acta
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Potential of human serum albumin as chiral selector of basic drugs in affinity electrokinetic chromatography-partial filling technique

2006

The enantiomeric resolution of compounds using HSA by means of affinity EKC (AEKC)-partial filling technique is the result of a delicate balance between different experimental variables such as protein concentration, running pH (background electrophoretic buffer (BGE), protein, and compound solutions), and plug length. In this paper, the possibility of using HSA as chiral selector for enantioseparation of 28 basic drugs using this methodology is studied. The effect of the physicochemical parameters, the structural properties of compounds, and compound-HSA protein binding percentages over their chiral resolution with HSA is outlined. Based on the results obtained, a decision tree is proposed…

Resolution (mass spectrometry)Clinical BiochemistryPlasma protein bindingBuffersBiochemistryChromatography AffinityAnalytical ChemistryElectrokinetic phenomenaMolar volumemedicineHumansSerum AlbuminChromatography Micellar Electrokinetic CapillaryChromatographyMolecular StructureChemistryStereoisomerismHydrogen-Ion ConcentrationHuman serum albuminChiral resolutionbody regionsElectrophoresisPharmaceutical Preparationsembryonic structuresEnantiomerHydrophobic and Hydrophilic Interactionsmedicine.drugELECTROPHORESIS
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Poly-sarcosine and poly(ethylene-glycol) interactions with proteins investigated using molecular dynamics simulations

2018

Nanoparticles coated with hydrophilic polymers often show a reduction in unspecific interactions with the biological environment, which improves their biocompatibility. The molecular determinants of this reduction are not very well understood yet, and their knowledge may help improving nanoparticle design. Here we address, using molecular dynamics simulations, the interactions of human serum albumin, the most abundant serum protein, with two promising hydrophilic polymers used for the coating of therapeutic nanoparticles, poly(ethylene-glycol) and poly-sarcosine. By simulating the protein immersed in a polymer-water mixture, we show that the two polymers have a very similar affinity for the…

SarcosineBiocompatibilityPoly-peptoidlcsh:BiotechnologyBiophysicsFOS: Physical sciencesNanoparticle02 engineering and technologyCondensed Matter - Soft Condensed MatterProtein aggregation010402 general chemistry01 natural sciencesBiochemistryNanoparticle protein coronachemistry.chemical_compoundMolecular dynamicsAdsorptionStructural Biologylcsh:TP248.13-248.65GeneticsmedicinePhysics - Biological Physicschemistry.chemical_classificationBiomolecules (q-bio.BM)MD simulationPolymer021001 nanoscience & nanotechnologyHuman serum albuminPEG0104 chemical sciencesComputer Science ApplicationsQuantitative Biology - BiomoleculeschemistryChemical engineeringBiological Physics (physics.bio-ph)FOS: Biological sciencesSoft Condensed Matter (cond-mat.soft)Poly-sarcosine0210 nano-technologyResearch ArticleBiotechnologymedicine.drug
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Isolation of human milk whey proteins by solid phase extraction with a polymeric material modified with gold nanoparticles

2017

Abstract This work describes a method for the isolation of human milk whey proteins by solid-phase extraction (SPE) with a polymeric material modified with gold nanoparticles. Human serum albumin, α-lactalbumin, lactoferrin and lysozyme were selected as target proteins to establish the performance of SPE support. Several experimental variables (pH and ionic strength) that affect the SPE protocol were investigated to achieve the maximum extraction efficiency. Under optimal conditions, the SPE sorbent gave excellent recoveries, and offered a high permeability and reusability (> 20 times). The feasibility of this methodology was successfully demonstrated by isolating the target proteins in a m…

SorbentChromatography010401 analytical chemistryExtraction (chemistry)food and beverages02 engineering and technology021001 nanoscience & nanotechnologyHuman serum albumin01 natural sciences0104 chemical sciencesAnalytical Chemistrychemistry.chemical_compoundfluids and secretionsIsoelectric pointchemistryColloidal goldIonic strengthmedicineSolid phase extractionLysozyme0210 nano-technologySpectroscopymedicine.drugMicrochemical Journal
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High-performance liquid chromatography of amino acids, peptides and proteins

1990

Abstract The thermodynamic constants, associated with the interaction of three proteins with triazine dye affinity sorbents, have been derived from bath and frontal analysis experiments. In cases where mass-transfer restrictions are very high, calculation of the thermodynamic constants directly from frontal analysis experiments could not be achieved. In such cases, a portion of the adsorbate was always present in the effluent, a situation which has its effect as the split peak phenomenon. With Fractogel-based triazine dye affinity sorbents none of the test proteins applied in frontal analysis were adsorbed. A similar behaviour was observed for a Cellufine sorbent during the adsorption of hu…

SorbentChromatographyLigandChemistryDiffusionKineticsOrganic ChemistryGeneral MedicineHuman serum albuminBiochemistryHigh-performance liquid chromatographyAnalytical Chemistrychemistry.chemical_compoundAdsorptionmedicineParticleLysozymePorositySaturation (chemistry)medicine.drugTriazineJournal of Chromatography A
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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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Low density lipoproteins and human serum albumin as the carriers of squalenoylated drugs: insights from molecular simulations

2018

We have studied the interaction of three clinically promising squalenoylated drugs (gemcitabine-squalene, adenine-squalene, and doxorubicin-squalene) with low-density lipoproteins (LDL) by means of atomistic molecular dynamics simulations. It is shown that all studied squalenoylated drugs accumulate inside the LDL particles. This effect is promoted by the squalene moiety, which acts as an anchor and drives the hydrophilic drugs into the hydrophobic core of the LDL lipid droplet. Our data suggest that LDL particles could be a universal carriers of squalenoylated drugs in the bloodstream. Interaction of gemcitabine-squalene with human serum albumin (HSA) was also studied by ensemble of dockin…

Squalene[PHYS.PHYS.PHYS-BIO-PH]Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph]Drug CompoundingPharmaceutical ScienceSerum Albumin Human02 engineering and technologyPlasma protein bindingMolecular Dynamics Simulation010402 general chemistry01 natural sciencesMolecular Docking SimulationDeoxycytidineSqualenechemistry.chemical_compound[ PHYS.PHYS.PHYS-BIO-PH ] Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph]Lipid dropletDrug DiscoverymedicineMoietyHumansComputingMilieux_MISCELLANEOUSDrug CarriersBinding SitesAdenine[SDV.SP]Life Sciences [q-bio]/Pharmaceutical sciences021001 nanoscience & nanotechnologyHuman serum albuminGemcitabine3. Good health0104 chemical sciences[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistryLipoproteins LDLMolecular Docking Simulation[ SDV.SP ] Life Sciences [q-bio]/Pharmaceutical scienceschemistryDocking (molecular)Doxorubicin[ CHIM.THEO ] Chemical Sciences/Theoretical and/or physical chemistryBiophysicsMolecular MedicineNanoparticles0210 nano-technologyDrug carrierHydrophobic and Hydrophilic Interactionsmedicine.drugProtein Binding
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Characterization of the binding of benzodiazepines to human serum albumin

1973

The binding of eleven benzodiazepine derivatives to human serum albumin (HSA) was determined by means of sephadex gel filtration. The albumin binding of the substances was characterized by the percentage of bound drug, the binding constants k +, K 1 and m, the number of binding sites per albumin molecule, and the free binding energy. Under the conditions chosen in these experiments there seems to exist only one binding site of the same type for all investigated benzodiazepines at the HSA molecule. The affinities of the benzodiazepines to this binding site are very different. It is discussed which part of the benzodiazepine molecule represents the main binding group.

StereochemistryBinding energySerum albuminPlasma protein bindingFlurazepammedicineHumansNitrazepamBovine serum albuminBinding siteSerum AlbuminPharmacologyBinding SitesbiologyOxazepamChemistryAlbuminChlordiazepoxideGeneral MedicineBenzazepinesHuman serum albuminSephadexChromatography Gelbiology.proteinProtein Bindingmedicine.drugNaunyn-Schmiedeberg's Archives of Pharmacology
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Differential effects of cysteine and methionine residues in the antioxidant activity of human serum albumin

2005

Antioxidant properties of human serum albumin (HSA) may explain part of its beneficial role in various diseases related to free radical attack. In the present study, the antioxidant role of Cys and Met was studied by copper-mediated oxidation of human low density lipoproteins and by free radical-induced blood hemolysis which essentially assessed metal-chelating and free radical scavenging activities, respectively. Mild conditions were set up to specifically modify Cys and Met residues by N-ethylmaleimide (NEM) and chloramine T treatments, respectively. We found that Met and Cys accounted for 40-80% of total antioxidant activity of HSA. Copper binding to HSA was decreased by about 50% with c…

Time FactorsAntioxidantFree Radicalsmedicine.medical_treatmentDithionitrobenzoic AcidHemolysisBiochemistryAntioxidantsTosyl Compoundschemistry.chemical_compoundMethioninemedicineHumansChelationCysteineSerum AlbuminMethionineDose-Response Relationship DrugChloraminesFree Radical ScavengersGeneral MedicineFree radical scavengerHuman serum albuminmedicine.diseaseHemolysisLipoproteins LDLOxygenOxidative StresschemistryBiochemistryEthylmaleimideChloramine-TOxidation-ReductionCopperPhenanthrolinesProtein Bindingmedicine.drugCysteineFree Radical Research
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Enantioseparation of nuarimol by affinity electrokinetic chromatography-partial filling technique using human serum albumin as chiral selector

2008

The present paper deals with the enantiomeric separation of nuarimol enantiomers by affinity EKC-partial filling technique using HSA as chiral selector. Firstly, a study of nuarimol interactions with HSA by CE-frontal analysis was performed. The binding parameters obtained for the first site of interaction were n(1) = 0.84; K(1) = 9.7 +/- 0.3x10(3 )M(-1) and the protein binding percentage of nuarimol at physiological concentration of HSA was 75.2 +/- 0.2%. Due to the moderate affinity of nuarimol towards HSA the possibility of using this protein as chiral selector for the separation of nuarimol using the partial filling technique was evaluated. A multivariate optimization approach of the mo…

TrisResolution (mass spectrometry)Analytical chemistryFiltration and SeparationChromatography AffinityAnalytical ChemistryChemometricschemistry.chemical_compoundCapillary electrophoresismedicineAnimalsHumansSerum AlbuminChromatographyMolecular StructureReproducibility of ResultsStereoisomerismHuman serum albuminbody regionsElectrophoresisPyrimidineschemistryFemaleEnantiomerQuantitative analysis (chemistry)Softwaremedicine.drugJournal of Separation Science
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