Fibres, crystals and polymorphism: the structural promiscuity of amyloidogenic peptides

Abstract

The ability to assemble to form β-sheet rich fibrils in vitro is shared by a broad range of precursor proteins and peptides. The ordered aggregation and deposition of a number of specific polypeptides are associated with diseases including Alzheimer's disease and Diabetes type 2 and recently it has been shown that the highly stable nature of amyloid fibrils has been exploited by organisms as functional materials. Here we describe the capacity of peptides to form various different β-sheet rich structures, each sharing the amyloid-like structure, but differing in specific arrangements and side-chain interactions.