Amyloid fibrils are protein aggregates with typical diameter of few nanometers and length in the micrometer range. They are usually formed in consequence of a misfolding of the polypeptide chain. Amyloid aggregates are associated with severe pathological conditions, including Alzheimer’s and Parkinson’s diseases. It is not yet clear which steps of the aggregation process are cytotoxic and which toxicity mechanisms are involved. In addition, fibrils are potentially interesting for the construction of nanowires or other nanostructured devices.
Our research activity is aimed to understanding the molecular mechanisms of the aggregation process and the factors which affect it. We characterize the physical properties of the aggregates by a variety of biophysical techniques, such as scanning probe microscopy and spectroscopy, fluorescence spectroscopy, light scattering, small angle X-ray scattering. Using this approach we can also study the effects of anti-amyloidogenic agents. Studying the interaction of the aggregates with model membranes, such as Langmuir films, supported lipid bilayers and liposomes, can yield information on the mechanisms of cell membrane destabilization by protein aggregates.