6533b826fe1ef96bd12851eb
RESEARCH PRODUCT
Valorization of apple peels through the study of the effects on the amyloid aggregation process of ?-casein
GuarrasiValeriaRappaGiacoma CinziaCostaMaria AssuntaLibrizziFabioRaimondoMarcoDi StefanoVitaGermanaMaria AntoniettaVilasiSilviasubject
Circular dichroismMalusAmyloidAmyloidSettore CHIM/10 - Chimica Degli AlimentiκINHIBITIONPharmaceutical 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 & neurosurgerydescription
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 fibril formation in a dose-dependent way. In particular, we found that the extract significantly reduced the protein aggregation rate and inhibited the secondary structure reorganization that accompanies ?-casein amyloid formation. Protein-aggregated species resulting from the incubation of ?-casein in the presence of polyphenols under amyloid aggregation conditions were reduced in number and different in morphology. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2021-04-01 |