Abstract
Driven by the structural properties of a generic polypeptide chain, proteins have a natural tendency to form fibrillar aggregates. These fibrillar aggregates, called amyloid fibrils, are in the order of micrometers in length, about ten nanometers in width, and are stabilised by a network of hydrogen bonds and hydrophobic interactions. The protein-to-fibril self-assembly process can be highly efficient and the resulting amyloid fibrils have an extremely regular internal structure. These desirable properties have led researchers to explore their potential for technological applications, such as nanowire templating and 3D scaffolding for cell cultures. Moreover, amyloid formation is intimately related to numerous human diseases, including Alzheimer’s, Parkinson’s and other prion diseases. In this talk, I will discuss various physical properties of protein amyloid self-assembly and how they relate to amyloid technology and amyloid pathogenesis.