An amyloid fibril is a highly ordered, insoluble form of protein that results when a normally soluble protein aggregates via a self-association process to form a structured nanotube. Such fibrils can now be routinely generated from purified proteins in the laboratory, and have attracted burgeoning interest due to their role in a variety of disease states. This article focusses on a new alternative direction in amyloid research, exploring the potential application of the amyloid fibril as a form of nanotubular scaffolding in bionanotechnology.