0000000001337079
AUTHOR
Mangialardo, S
FTIR studies of the high pressure dissociation of insulin and alpha-synuclein amyloids
Amyloid fibrils are highly ordered aggregates whose formation occurs during the development of several serious disorders, like Althzeimer's and Parkinson's diseases. Even if most biophysical investigations of fibril formation have attempted to elucidate the structural events that occur during amyloid fibril assembly, relatively little is known about the thermodynamics of the aggregated protein state, and the kinetic mechanisms of its formation. Fibrillation is an irreversible process and a key challenge for the field is the development of therapeutic strategies able to inhibit or reverse the aggregation. The coupling of conventional Fourier Transform Infrared Spectroscopy (FTIR) and high Pr…
Infrared HP study of protein folding and aggregation @ the SISSI Elettra beamline
Fourier transform infrared spectroscopy (FTIR) coupled with High Hydrostatic Pressure technology is a suitable technique to investigate unfolding/misfolding processes providing useful information on the kinetics of aggregation of proteins. Since HHP doesn't affect the enthalpic contribution to the Gibbs free energy, it is able to perturb the secondary structure of proteins in a reversible way . The principle governing pressure effects is that it tends to shift a system towards the state that occupies the smallest volume, it causes the electrostriction of charged and polar groups, the elimination of packing defects, and the solvation of hydrophobic groups. Cavities and packing defects are ex…