CHAPTER 17 - Amyloid Fibrils – Self-Assembling Proteins

Abstract

The design of new materials through self-assembly of biomolecules is at the center of various fields in science, technology, and industry. It is important to distinguish between aggregation and self-assembly. Aggregation is a self-association reaction generally resulting in the formation of amorphous aggregates that are heterogeneous in structure. Molecular self-assembly is ubiquitous in biological systems and underlies the formation of various complex biological systems. Protein aggregation is of critical importance in a wide variety of biomedical situations ranging from conformational disorders associated with neurodegenerative disease, such as Alzheimer disease, to the production, stability, and delivery of protein drugs and food. There are multiple pathways to the protein folding and misfolding and several models have been proposed to explain the mechanism of amyloid fibril assembly. The main theories on the mechanism of fibril formation include the nucleation-dependent model and the conformational-dependent theory. This chapter describes the analytical techniques currently available to study the main processes in the fibril formation pathway: unfolding, protofilament formation, and fibril formation. Each stage of the fibril forming process will help in understanding the process to inhibit fibril formation or promote fibril formation for use in nanotechnology and bioprocessing.