This work forms part of a new collaboration between the Schools of Pharmacy and Physics and Astronomy to study the properties of proteins when they are localised at surfaces and interfaces. We are currently using a combination of Atomic Force Microscopy, Attentuated Total Reflection Fourier Transform Infra-Red (FTIR-ATR) Spectroscopy and the Quartz Crystal Microbalance (QCM) to study the adsorption, conformational stability and aggregation properties of proteins on different surfaces. In particular, we hope to look at the effects of protein-surface interactions on the growth rates and external morphologies of amyloid fibrils as well as the effects of protein-metal interactions on the formation of these one dimensional aggregates. We will also extend these studies to look at the formation of amyloid fibrils in the presence of metallic nanoparticles to determine if these structures can be used to form self assembling nanowires.