Search results for "AGGREGATION"

showing 10 items of 566 documents

Gas chromatographic analysis of resveratrol in plasma, lipoproteins and cells after in vitro incubations

1998

Resveratrol is a trihydroxystilbene present in certain red wines. It may play a role in the inhibition of lipoprotein oxidation and platelet activity. We have developed the first method to measure resveratrol in animal and human samples and to study its incorporation in vitro. After adding epicoprostanol as an internal standard, samples are subjected to lipid extraction in the presence of antioxidant and under dim light to minimize both denaturation and isomerization of the trans-resveratrol to the cis-form. Extracts were purified by cold acetone precipitation and the resveratrol-containing acetone phase was evaporated under nitrogen. The resveratrol was analyzed as a trimethylsilyl derivat…

Chromatography GasErythrocytesAntioxidantendocrine system diseasesmedicine.medical_treatmentResveratrolSensitivity and Specificitychemistry.chemical_compoundStilbenesAcetonemedicineAnimalsHumansPlatelet activationLipoprotein oxidationDetection limitChromatographyorganic chemicalsReproducibility of Resultsfood and beveragesStereoisomerismGeneral ChemistryRatsLipoproteins LDLchemistryResveratrolCalibrationLinear ModelsGas chromatographyQuantitative analysis (chemistry)Platelet Aggregation InhibitorsJournal of Chromatography B: Biomedical Sciences and Applications
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Amyloid fibrils formation and amorphous aggregation in Concanavalin A

2007

We here report an experimental study on the thermal aggregation process of concanavalin A, a protein belonging to the legume lectins family. The aggregation process and the involved conformational changes of the protein molecules were followed by means of fluorescence techniques, light scattering, circular dichroism, zeta potential measurements and atomic force microscopy. Our results show that the aggregation process of concanavalin A may evolve through two distinct pathways leading, respectively, to the formation of amyloids or amorphous aggregates. The relative extent of the two pathways is determined by pH, as amyloid aggregation is favored at high pH values ( approximately 9), while th…

Circular dichroismAmyloidLightBiophysicsProtein aggregationCircular dichroismMicroscopy Atomic ForceBiochemistryFluorescenceAtomic force microscopyZeta potentialConcanavalin AScattering RadiationBenzothiazolesProtein Structure QuaternaryFluorescent DyesbiologyChemistryAtomic force microscopyOrganic ChemistryThioflavin T fluorescenceHydrogen-Ion ConcentrationAmyloid fibrilFluorescenceAmorphous solidKineticsThiazolesCrystallographyConcanavalin Abiology.proteinProtein aggregation
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Irreversible formation of intermediate BSA oligomers requires and induces conformational changes.

2004

Understanding the relation between protein conformational changes and aggregation, and the physical mechanisms leading to such processes, is of primary importance, due to its direct relation to a vast class of severe pathologies. Growing evidence also suggests that oligomeric intermediates, which may occur early in the aggregation pathway, can be themselves pathogenic. The possible cytotoxicity of oligomers of non-disease-associated proteins adds generality to such suggestion and to the interest of studies of oligomer formation. Here we study the early stages of aggregation of Bovine Serum Albumin (BSA), a non pathogenic protein which has proved to be a useful model system. Dynamic light sc…

Circular dichroismAmyloidLightStereochemistryProtein ConformationProtein aggregationProcess interactionFibrilBiochemistryOligomerProtein Structure Secondarychemistry.chemical_compoundDynamic light scatteringStructural BiologyAnimalsScattering RadiationBovine serum albuminMolecular BiologybiologyCircular DichroismTemperatureSerum Albumin BovineKineticschemistrybiology.proteinCattleProteins
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Effects of succinylation on thermal induced amyloid formation in Concanavalin A.

2007

We have recently shown that upon slight thermal destabilization the legume lectin Concanavalin A may undergo two different aggregation processes, leading, respectively, to amyloid fibrils at high pH and amorphous aggregates at low pH. Here we present an experimental study on the amyloid aggregation of Succinyl Concanavalin A, which is a dimeric active variant of Concanavalin. The results show that, as for the native protein, the fibrillation process appears to be favoured by alkaline pH, far from the isoelectric point of the protein. Moreover, it strongly depends on temperature and requires large conformational changes both at secondary and tertiary structure level. With respect to the nati…

Circular dichroismAmyloidProtein DenaturationAmyloidbiologyChemistryCircular DichroismBiophysicsLegume lectinGeneral MedicineProtein aggregationHydrogen-Ion ConcentrationProtein tertiary structureProtein Structure SecondaryProtein Structure Tertiaryprotein aggregationSuccinylationIsoelectric pointBiochemistryConcanavalin Abiology.proteinConcanavalin AThermodynamicsDimerizationHydrophobic and Hydrophilic Interactions
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Inactivation and structural changes of polyphenol oxidase in quince ( Cydonia oblonga Miller) juice subjected to ultrasonic treatment

2020

Background Polyphenol oxidase (PPO) is considered a problem in the food industry because it starts browning reactions during fruit and vegetable processing. Ultrasonic treatment is a technology used to inactivate the enzyme; however, the mechanism behind PPO inactivation is still unclear. For this reason, the inactivation, aggregation, and structural changes in PPO from quince juice subjected to ultrasonic treatments were investigated. Different intensities and times of ultrasonic treatment were used. Changes in the activity, aggregation, conformation, and structure of PPO were investigated through different structural analyses. Results Compared to untreated juice, the PPO activity in treat…

Circular dichroismHot TemperatureChemical PhenomenaFood Handling030309 nutrition & dieteticsColorProtein aggregationPolyphenol oxidaseProtein Structure Secondary03 medical and health sciences0404 agricultural biotechnologyVegetablesBrowningUltrasonicsParticle SizeRosaceaeProtein secondary structurePlant Proteinschemistry.chemical_classification0303 health sciencesNutrition and Dieteticsbusiness.industryChemistryCircular DichroismUltrasound04 agricultural and veterinary sciencesHydrogen-Ion Concentration040401 food scienceProtein tertiary structureMaillard ReactionFruit and Vegetable JuicesEnzymeFruitBiophysicsbusinessAgronomy and Crop ScienceCatechol OxidaseFood ScienceBiotechnologyJournal of the Science of Food and Agriculture
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Combined spectroscopic and theoretical analysis of the binding of a water-soluble perylene diimide to DNA/RNA polynucleotides and G-quadruplexes.

2021

We present here a combined spectroscopic and theoretical analysis of the binding of N,N’-bis(2-(1-piperazino)ethyl)-3,4,9,10-perylenetetracarboxylic acid diimide dichloride (PZPERY) to different biosubstrates. Absorbance titrations and circular dichroism experiments, melting studies and isothermal calorimetry (ITC) titrations reveal a picture where the binding to natural double-stranded DNA is very different from that to double and triple-stranded RNAs (poly(A)∙poly(U) and poly(U)∙poly(A)⁎poly(U)). As confirmed also by the structural and energetic details clarified by density functional theory (DFT) calculations, intercalation occurs for DNA, with a process driven by the combination of aggr…

Circular dichroismIntercalation (chemistry)PolynucleotidesSupramolecular chemistryMolecular dynamicsG-quadruplexChemistry Physical and theoreticalAnalytical ChemistryAggregationchemistry.chemical_compoundDiimideQuímica físicaIntercalationHumansInstrumentationPeryleneSpectroscopyAggregation; Density functional theory; Intercalation; Molecular dynamics; Sitting atop; Circular Dichroism; DNA; Humans; Polynucleotides; RNA; Water; G-Quadruplexes; PeryleneCircular DichroismWaterIsothermal titration calorimetryDNAAtomic and Molecular Physics and OpticsSitting atopG-QuadruplexesCrystallographychemistrySettore CHIM/03 - Chimica Generale E InorganicaPolynucleotideDensity functional theoryRNAPeryleneSpectrochimica acta. Part A, Molecular and biomolecular spectroscopy
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Carnosine Inhibits Aβ42Aggregation by Perturbing the H-Bond Network in and around the Central Hydrophobic Cluster

2013

Aggregation of the amyloid-β peptide (Aβ) into fibrillar structures is a hallmark of Alzheimer's disease. Thus, preventing self-assembly of the Aβ peptide is an attractive therapeutic strategy. Here, we used experimental techniques and atomistic simulations to investigate the influence of carnosine, a dipeptide naturally occurring in the brain, on Aβ aggregation. Scanning force microscopy, circular dichroism and thioflavin T fluorescence experiments showed that carnosine does not modify the conformational features of Aβ42 but nonetheless inhibits amyloid growth. Molecular dynamics (MD) simulations indicated that carnosine interacts transiently with monomeric Aβ42 by salt bridges with charge…

Circular dichroismMagnetic Resonance Spectroscopy1303 BiochemistryStereochemistryStatic ElectricityCarnosinePeptideMolecular Dynamics SimulationBiochemistryproteinprotein interactionsProtein–protein interactionchemistry.chemical_compoundMolecular dynamicsnutraceutical compounds10019 Department of Biochemistry1312 Molecular BiologyMolecular Biologychemistry.chemical_classificationAmyloid beta-PeptidesDipeptideHydrogen bondOrganic ChemistryIntermolecular forceTemperatureneuroprotective agentHydrogen BondingAlzheimer's diseasePeptide Fragmentsmolecular dynamicscarnosinechemistry1313 Molecular Medicine570 Life sciences; biologyMolecular MedicineHydrophobic and Hydrophilic Interactionsprotein aggregation fibrillogenesis carnosine AFM1605 Organic ChemistryChemBioChem
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Valorization of apple peels through the study of the effects on the amyloid aggregation process of ?-casein

2021

Waste valorization represents one of the main social challenges when promoting a circular economy and environmental sustainability. Here, we evaluated the effect of the polyphenols extracted from apple peels, normally disposed of as waste, on the amyloid aggregation process of ?-casein from bovine milk, a well-used amyloidogenic model system. The effect of the apple peel extract on protein aggregation was examined using a thioflavin T fluorescence assay, Congo red binding assay, circular dichroism, light scattering, and atomic force microscopy. We found that the phenolic extract from the peel of apples of the cultivar "Fuji", cultivated in Sicily (Caltavuturo, Italy), inhibited ?-casein fib…

Circular dichroismMalusAmyloidAmyloidSettore CHIM/10 - Chimica Degli Alimenti&#954INHIBITIONPharmaceutical ScienceOrganic chemistryPROTEINProtein aggregationMicroscopy Atomic ForceFIBRIL FORMATIONArticleAnalytical Chemistry03 medical and health scienceschemistry.chemical_compound0302 clinical medicineQD241-441OLIGOMERSCaseinTRANSTHYRETIN AMYLOIDOSISANTIOXIDANTDrug Discovery-casein amyloid aggregationFood sciencePhysical and Theoretical Chemistrypolyphenolic extract030304 developmental biology0303 health sciencesbiologyChemistryNATURAL POLYPHENOLSCaseinsκ-casein amyloid aggregationbiology.organism_classificationSTATECongo redfruit wasteChemistry (miscellaneous)PolyphenolFIBRILLOGENESISMalusFruit waste; Polyphenolic extract; ?-casein amyloid aggregationMolecular MedicineThioflavinTHIOFLAVIN-T030217 neurology & neurosurgery
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Copper(ii) and zinc(ii) dependent effects on Aβ42 aggregation: a CD, Th-T and SFM study

2013

A? aggregation is a central event in Alzheimer's disease (AD). In vitro evidence indicates that A? aggregation and fibrillogenesis are significantly influenced by the employed experimental conditions. Indeed, although it is widely established that metal ions, such as copper and zinc, have significant effects on the A? aggregation process, their actual role in A? fibrillogenesis is still debated. In this work the effects of a molar excess of zinc(ii) and/or copper(ii) ions on the A?42 aggregation process and the morphology of the resultant aggregates have been compared in samples exhibiting different initial conformations. CD spectroscopy, Th-T-induced fluorescence and Scanning Force Microsc…

Circular dichroismMetal ions in aqueous solutionInorganic chemistryaggregationmetal ionschemistry.chemical_elementCopper Zing protein aggregation AFM self-assemblyFibrillogenesisGeneral ChemistryZincFluorescenceCopperCatalysisIn vitroIonchemistryMaterials ChemistryBiophysicsamyloidsNew Journal of Chemistry
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Bovine Serum Albumin protofibril-like aggregates formation: Solo but not simple mechanism

2011

We report an experimental study on the model protein Bovine Serum Albumin (BSA), with the aim of elucidating the mechanisms by which a fully folded globular protein undergoes different aggregation pathways leading to the formation of amyloid fibrils or amorphous aggregates. We observe thermally induced formation of fibrillar structures at pH far from the protein isoelectric point. The increase of electrostatic repulsion results in protein destabilization and in modifications of inter and intra-molecular interactions leading to the growth of fibril-like aggregates stabilized by inter-molecular-β sheets. The aggregation kinetics is studied by means of fluorescence techniques, light scattering…

Circular dichroismProtein ConformationGlobular proteinStatic ElectricityBiophysicsProtein aggregationBiochemistryprotein aggregation amyloid fibril fluorescence conformational changeschemistry.chemical_compoundProtein structureAnimalsBenzothiazolesBovine serum albuminMolecular Biologychemistry.chemical_classificationbiologyTemperatureTryptophanSerum Albumin BovineHydrogen-Ion ConcentrationSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)KineticsThiazolesCrystallographyIsoelectric pointchemistryProtein destabilizationbiology.proteinThermodynamicsCattleThioflavinProtein Multimerization
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