Amyloid fibrils polypeptide self-assembly

This chapter describes the self-assembly of non-native protein fibers known as amyloid fibrils and the development of these fibrils for potential applications in nanotechnology and biomedicine. It extends an earlier review by the author on a related topic (Gras, 2007). In Section 1, the self-assembly of polypeptides into amyloid fibrils and efforts to control assembly and any subsequent disassembly are discussed. In Section 2, this review focuses on the important role of surfaces and interfaces during and after polypeptide assembly. It examines how different surfaces can influence fibril assembly, how surfaces can be used to direct self-assembly in order to create highly ordered structures, and how different techniques can be used to create aligned and patterned materials on surfaces following self-assembly. 

If amyloid fibrils and other self-assembling polypeptide systems are to be developed as new materials and components for nanotechnology and biomedicine, it is important that we understand the pathways and kinetics of their assembly. It will also be desirable to be able to control this assembly and any subsequent disassembly. 

In this section, the potential application for amyloid fibrils and other selfassembling fibrous protein structures are outlined. These include potential uses in electronics and photonics presented in Section 4.1, uses as platforms for the immobilization of enzymes and biosensors presented in Section 4.2, and uses as biocompatible materials presented in Section 4.3. Each of these applications makes use of the ability of polypeptides to self-assemble and form nanostructured materials, a process that can occur under aqueous conditions. These applications also seek to exploit the favorable properties of fibrils such as strength and durability, the ability to arrange ligands on a nanoscale, and their potential biocompatibility arising from the natural materials used for assembly. 

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