Various proteins and peptides are able to self assemble into amyloid fibrils that are associated with disease.
Structural characterisation of these fibres is limited by their insoluble and heterogeneous nature. However, advances in
various techniques including X-ray diffraction, cryo-electron microscopy and solid state NMR have provided detailed
information on various amyloid fibrils, from the long range order and macromolecular structure to the atomic interactions
that promote assembly and stabilise the amyloid core. The cross-β model has been widely accepted as a generic structure
for most amyloid fibrils and is discussed in detail. It is clear, however, that polymorphisms are present, even in fibrils
formed from the same precursor protein, and that these may represent differences in packing at a molecular level. To fully
understand the roles of particular residues in amyloid formation and structure, short peptides can be used in conjunction
with mutagenesis studies to assess their effects. The structural insights gained using a combination of techniques to study
both full-length, disease related peptides and short fragments are essential if progress is to be made towards understanding
why these fibres form and how to prevent their formation.