About the book
How can two chemically identical proteins have different biological functions? This is known to be possible through the process of amyloidosis. The ability of proteins to change their secondary structure and form insoluble fibrous material called amyloid is the focus of this book. Here we explore the phenomenon of amyloidosis and the consequences of this in biology focusing on the roles of amyloidogenic proteins in normal physiology and disease.
Beginning with an in-depth description of the structure and properties of amyloids, the book then addresses the formation and propagation of these structures in various contexts. First, we consider amyloids in disease. We look at how amyloids are associated with progressive neurodegenerative disorders such as Alzheimer’s disease and prion diseases (for example Creutzfeldt–Jakob disease). In the next chapters the focus shifts from disease to functional amyloids where the book explores the positive impact amyloids have in biology. Here we discuss how nature has exploited this stable and heritable protein structure to confer positive biological functions. We focus on eukaryotic proteins (such as yeast prions and mammalian amyloids) and prokaryotic functional amyloids such as bacteria. In the final chapter, we explore the recent advances that have been made in determining detailed structures of amyloid proteins and the impact this will have in understanding disease and developing therapeutics. The challenges involved in developing treatments against amyloid disorders are discussed as are the state-of-the-art techniques being utilised for drug discovery and therapeutics.
This book aims to give the reader a comprehensive overview of the importance of understanding amyloidosis from different perspectives providing both a historical background to the field and highlighting recent developments in research.