Fibrillar protein self-assembly has potential in fabricating materials for biomedical applications. Via almost an identical assembling pathway, different physico-chemical properties of protein-based materials can be tailored. It is extensively utilised for constructing biomaterials from artificial peptides. The underlying motivation for our group research activities has been to strive towards a quantitative picture of the behavior of biological macromolecules, and in particular of their self-assembly into highly ordered polymers such as aggregation-prone proteins and peptides. Our current scientific interests are directed towards deep understanding of the link between functional and disease-associated protein assemblies and their processing, by looking at biochemical and biophysical properties. This requires rethinking of the relationship between aggregation and function and the correlation between amyloid aggregation and toxicity.