0000000000085534

AUTHOR

Vilasi

showing 2 related works from this author

Stability and disassembly properties of human naïve Hsp60 and bacterial GroEL chaperonins.

2015

Human Hsp60 chaperonin and its bacterial homolog GroEL, in association with the corresponding co-chaperonins Hsp10 and GroES, constitute important chaperone systems promoting the proper folding of several mitochondrial proteins. Hsp60 is also currently described as a ubiquitous molecule with multiple roles both in health conditions and in several diseases. Naïve Hsp60 bearing the mitochondrial import signal has been recently demonstrated to present different oligomeric organizations with respect to GroEL, suggesting new possible physiological functions. Here we present a combined investigation with circular dichroism and small-angle X-ray scattering of structure, self-organization, and sta…

guanidiniun chloride0301 basic medicineGuanidinium chlorideSmall AngleCircular dichroismBiophysicsmacromolecular substancesBiochemistryGroELChaperoninScatteringMitochondrial Proteins03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsX-Ray DiffractionScattering Small AngleHumansGuanidinebiologyProtein StabilityCircular DichroismOrganic ChemistryTemperatureGroESSAXSChaperonin 60Hsp60GroELSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)CDcited By 5enzymes and coenzymes (carbohydrates)Denaturation030104 developmental biologychemistryBiochemistryChaperone (protein)biological sciencesbiology.proteinCD; Denaturation; GroEL; Guanidinium chloride; Hsp60; SAXS; Bacterial Proteins; Chaperonin 60; Circular Dichroism; Humans; Mitochondrial Proteins; Protein Stability; Scattering Small Angle; Temperature; X-Ray DiffractionbacteriaHSP60Guanidinium chlorideBiophysical chemistry
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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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