Fibril formation by short synthetic peptides

Nature produces an array of self-assembled fibres from proteins and peptides with a wide range of functionalities. This has inspired scientists to design peptides that exploit specific protein folds to form simple yet multi-functional self-assembled fibres. Of the various protein folds the most commonly used has been the β-sheet fold as it is easily accessible and produces nanoscale fibres which have a wide range of stabilities. Research has also been driven by the relationship to the various amyloid diseases, which produce β-sheet rich fibres. Here we will discuss the use of natural protein sequences as the basis of peptides that self-assemble to β-sheet rich fibres followed by peptide sequences that have been designed de novo purely based on the rules for the formation of a β-sheet. How changes in the amino acid sequence of these various peptides affects the properties of the fibres and also the macroscopic materials formed by these peptides will be discussed in each case. We will then look into how these structures have been utilized for applications as scaffolds for cell culture and tissue regeneration, followed by their use in the nanotechnology field.