Amyloid fibrils are notorious for their association with a group of debilitating and often incurable diseases called the amyloidosis. This group includes Alzheimer’s, Parkinson’s, and glaucoma, among others. These diseases have come under increasingly intense scrutiny in recent years owing to the devastating effect these particular diseases can wreak on aging populations. It is, therefore, surprising that amyloid fibrils have recently been found to have specific functions in a range of organisms from bacteria to humans. This has forced the scientific community to change the way we consider amyloid — from being a “mistake” caused by the aggregation of “misfolded” proteins to a structure that can be either physiological or pathogenic in a manner not yet fully understood.
This is the first book to bring together a wide variety of examples of functional amyloid in a single volume. Ten chapters provide comprehensive information on the importance of amyloid fibrils in fungi, bacteria, algae, invertebrate, and vertebrate animals for providing environmental protection, structural integrity, and regulating biochemical processes. Because of their functional manifestation, amyloid fibrils have a huge potential to form the basis of a new generation of proteinaceous biomaterials for a broad range of applications. The exploitation of functional amyloid as a strong, nanostructured biomaterial is included, as well as the consequences of their study for the treatment of amyloid-related diseases. This book highlights many of the extraordinary examples of functional amyloid found to date. It, therefore, provides an exciting perspective for the study of amyloid deposits as important and useful protein structures widespread in nature.
