Abstract
Intermolecular self-assembly of a large number of polypeptide chains into macromolecular constructs occurs widely in biological systems. One of such macromolecular self-assemblages of great interest is the amyloid fibril. The amyloid fibril is a misfolded and undesirable state for proteins as biomolecules, since it has been proposed to be a causative agent of a variety of diseases known as amyloid diseases, such as Alzheimer's and prion diseases. However, it is considered that the fibril has a highly-ordered tertiary structure, in which numerous β-stranded polypeptide chains align regularly. Thus this kind of fibril has the potential to be engineered into proteinaceous materials. Using peptides forming amyloid-like fibrils, peptide β-sheet arrays have been constructed to give self-assemblages composed of single, double, triple or quadruple different species. Moreover, the inhibitors that prevent the structural transition and formation of amyloid fibrils have been developed.
