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. Many different factors may act as the initial trigger of the protein misfolding and subsequent aggregation, including pH, ionic strength, and protein concentration. Furthermore, also the presence of a surface may induce the formation of initial aggregation seeds and affect the assembly rate and the structure of the aggregates. We are, therefore, investigating the molecular mechanisms responsible for the aggregation of different medically relevant proteins and peptides such as the islet amyloid polypeptide (IAPP), which plays a crucial role in the development of type II diabetes. We are particularly interested in the role of surface effects that may promote or inhibit amyloid fibril formation.