The Biophysics group has devoted its main efforts to the problem of understanding the physico-chemical basis of protein misfolding and aggregation processes. These processes are of the utmost scientific and bio-medical relevance since they are related to the pathogenesis of severe diseases known as protein conformational disorders (PCDs), which include Alzheimer's and Parkinson’s diseases and the transmissible spongiform encephalopathies (TSEs). Protein aggregation is also a getting growing importance in food industry, since aggregation can be exploited to enhance protein ability to form gels or other structures useful for food digestibility and preservation.

Proteins aggregation is driven by a very complex dynamics that depends on several factors such as pH, temperature, the interaction with metal ions and small molecules. Our research is mainly focused on the influence of organic molecules and metal ions in modulating the aggregation of proteins involved in AD and TSEs.

Our investigation strategy consists in combining in vitro experimental techniques like X-ray absorption spectroscopy (XAS), fluorescence spectroscopy and atomic force microscopy, with modern in silico experiments based on first-principle simulations (mainly molecular dynamics of the Car-Parrinello type). We are also implementing and testing novel numerical methods aimed at performing ab initio calculation ofXAS spectra.