The denaturation and aggregation of proteins into amyloid aggregates play important roles in the development of various degenerative diseases including Alzheimer's disease, Parkinson's disease, and type 2 diabetes mellitus. In the course of these diseases, partially unfolded proteins associate with one another and form nanoscale fibrillar structures with different morphologies. Amyloid aggregation kinetics and aggregate structure are affected by many different factors, including pH, ionic strength, protein concentration, and the interaction with interfaces. We are, therefore, investigating the molecular mechanisms responsible for the aggregation of different medically relevant proteins and peptides. We are particularly interested in the role of surface effects that may promote or inhibit amyloid fibril formation.