Search results for "Fibril formation"

showing 3 items of 3 documents

Entrapment of A Beta 1-40 peptide in unstructured aggregates

2012

Recognizing the complexity of the fibrillogenesis process provides a solid ground for the development of therapeutic strategies aimed at preventing or inhibiting protein-protein aggregation. Under this perspective, it is meaningful to identify the possible aggregation pathways and their relative products. We found that Aβ-peptide dissolved in a pH 7.4 solution at small peptide concentration and low ionic strength forms globular aggregates without typical amyloid β-conformation. ThT binding kinetics was used to monitor aggregate formation. Circular dichroism spectroscopy, AFM imaging, static and dynamic light scattering were used for structural and morphological characterization of the aggre…

Circular dichroismAmyloidKineticsPeptideProtein Structure SecondaryFIBRIL FORMATIONDynamic light scatteringMEMBRANE DISRUPTIONGeneral Materials ScienceFiberATOMIC-FORCE MICROSCOPYchemistry.chemical_classificationAmyloid beta-PeptidesChemistryProtein StabilityOsmolar ConcentrationTemperatureFibrillogenesisCondensed Matter PhysicsReceptor–ligand kineticsPeptide FragmentsAMYLOID-BETA-PROTEINALZHEIMERS-DISEASECrystallographyKineticsSpectrometry FluorescenceBiophysicsProtein Multimerization
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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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Conical nanopores highlight the pro-aggregating effects of pyrimethanil fungicide on Aβ(1-42) peptides and dimeric splitting phenomena.

2022

International audience; The Aβ(1-42) aggregation is a key event in the physiopathology of Alzheimer's disease (AD). Exogenous factors such as environmental pollutants, and more particularly pesticides, can corrupt Aβ(1-42) assembly and could influence the occurrence and pathophysiology of AD. However, pesticide involvement in the early stages of Aβ(1-42) aggregation is still unknown. Here, we employed conical track-etched nanopore in order to analyse the Aβ(1-42) fibril formation in the presence of pyrimethanil, a widely used fungicide belonging to the anilinopyrimidine class. Our results evidenced a pro-aggregating effect of pyrimethanil on Aβ(1-42). Aβ(1-42) assemblies were successfully d…

Environmental EngineeringAmyloidHealth Toxicology and MutagenesisDimerSettore ING-IND/06track-etchedMolecular dynamicschemistry.chemical_compoundNanoporesFibril formationPEG ratio[CHIM] Chemical SciencesfungicideEnvironmental Chemistry[CHIM]Chemical SciencesnanoporeAmyloid beta-PeptidesChemistryPublic Health Environmental and Occupational HealthamyloidGeneral MedicineGeneral ChemistryPollutionresistive pulsePeptide FragmentsAβ(1-42)Fungicides IndustrialNanoporePyrimidinesAβ(1–42)Biophysicslag phasePyrimethanilChemosphere
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