The misfolding of proteins into a toxic conformation is proposed to be at the molecular foundation of a number of neurodegenerative disorders including Alzheimer and Parkinson’s disease. One common and defining feature of protein misfolding diseases is the formation and deposition of amyloid-like fibrils. Currently, no preventive therapy is available for Parkinson and Alzheimer diseases. Identification of therapeutic drugs is not only complicated by a lack of understanding of many of the key aspects of the pathogenesis of these diseases but also by the multifactorial etiology of them. The aggregation pathway of the proteins linked to these disorders represents then an obvious target for therapeutic intervention. The detailed understanding of the phenomenon of amyloid fibrillation and its inhibition is therefore highly clinically important. The general purpose of this project research is to study the structural and toxic mechanisms related to amyloid formation and understand the structural and molecular basis behind the aggregation inhibitory effects of small molecules in order to advance in the rational design of a therapeutic strategy based on amyloid inhibitors. These goals will be achieved using a combination of biophysical and biochemical approaches as well as in vivo experiments.