6533b858fe1ef96bd12b65b4
RESEARCH PRODUCT
Entrapment of A Beta 1-40 peptide in unstructured aggregates
Gennara CavallaroDonatella BuloneSilvia VilasiAlessia ProvenzanoP.l. San BiagioRita CarrottaMaria Rosalia MangioneC Corsalesubject
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 Multimerizationdescription
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 aggregates. They appear stable or at least metastable with respect to fiber growth, therefore appearing as an incidental product in the pathway of fibrillogenesis.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2012-05-18 |