0000000000379012

AUTHOR

Isabella Tessari

0000-0002-5823-645x

showing 2 related works from this author

Pressure effects on α-synuclein amyloid fibrils: An experimental investigation on their dissociation and reversible nature

2017

α–synuclein amyloid fibrils are found in surviving neurons of Parkinson's disease affected patients, but the role they play in the disease development is still under debate. A growing number of evidences points to soluble oligomers as the major cytotoxic species, while insoluble fibrillar aggregates could even play a protection role. In this work, we investigate α–synuclein fibrils dissociation induced at high pressure by means of Small Angle X-ray Scattering and Fourier Transform Infrared Spectroscopy. Fibrils were produced from wild type α–synuclein and two familial mutants, A30P and A53T. Our results enlighten the different reversible nature of α–synuclein fibrils fragmentati…

0301 basic medicineSmall AngleAmyloidHigh-pressureMutantBiophysicsmacromolecular substances010402 general chemistryFibril01 natural sciencesBiochemistryDissociation (chemistry)Scattering03 medical and health scienceschemistry.chemical_compoundX-Ray DiffractionScattering Small AngleSpectroscopy Fourier Transform InfraredPressureHumansPoint MutationFourier transform infrared spectroscopyMolecular BiologySpectroscopyAlpha-synucleinAmyloid; FTIR; High-pressure; SAXS; α-synuclein; Amyloid; Humans; Parkinson Disease; Point Mutation; Pressure; Scattering Small Angle; Solubility; Spectroscopy Fourier Transform Infrared; X-Ray Diffraction; alpha-Synuclein; Biophysics; Biochemistry; Molecular BiologySmall-angle X-ray scatteringWild typeα-synucleinParkinson DiseaseSAXSAmyloid fibril0104 chemical sciences?-synucleinCrystallography030104 developmental biologyBiophysicchemistryFTIRSolubilityFourier Transform InfraredBiophysicsalpha-SynucleinHuman
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High-Pressure-Driven Reversible Dissociation of α-Synuclein Fibrils Reveals Structural Hierarchy

2017

The analysis of the α-synuclein (aS) aggregation process, which is involved in Parkinson's disease etiopathogenesis, and of the structural feature of the resulting amyloid fibrils may shed light on the relationship between the structure of aS aggregates and their toxicity. This may be considered a paradigm of the ground work needed to tackle the molecular basis of all the protein-aggregation-related diseases. With this aim, we used chemical and physical dissociation methods to explore the structural organization of wild-type aS fibrils. High pressure (in the kbar range) and alkaline pH were used to disassemble fibrils to collect information on the hierarchic pathway by which distinct β-sh…

0301 basic medicineModels MolecularCircular dichroismAmyloidProtein FoldingProtein domainBeta sheetBiophysicsFibrilMicroscopy Atomic ForceSpectrum Analysis RamanDissociation (chemistry)03 medical and health sciences0302 clinical medicineProtein structureMicroscopy Electron TransmissionProtein DomainsSpectroscopy Fourier Transform InfraredEscherichia coliPressureChemistryCircular DichroismEnergy landscapeProteinsalpha synuclein amyloid recombinant proteinHydrogen-Ion ConcentrationRecombinant ProteinsCrystallography030104 developmental biologyMutationalpha-SynucleinProtein foldingProtein Conformation beta-StrandProtein Multimerization030217 neurology & neurosurgery
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