Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease (Subcellular Biochemistry Book 65)

This volume of the Subcellular Biochemistry series is the result of the long-standing research interest of the editor in the molecular mechanism underlying Alzheimer’s disease and other amyloid diseases, indicated also by the earlier book in the series (Volume 38), devoted to Alzheimer’s disease. The broad coverage within the present amyloidogenesis book represents an attempt to collate current knowledge relating to the proteins and peptides involved in most of the known amyloid diseases, together with some amyloid/fibril-forming proteins and peptides that are not involved in diseases. Thus, the range of topics included is comprehensive and furthermore it was thought appropriate to include both basic science and clinical presentation of the subjects under discussion. Front Matter....Pages 1-1 Front Matter....Pages 1-1 Introduction and Technical Survey: Protein Aggregation and Fibrillogenesis....Pages 3-25 Front Matter....Pages 27-27 Fibril Formation by Short Synthetic Peptides....Pages 29-51 In vitro Oligomerization and Fibrillogenesis of Amyloid-beta Peptides....Pages 53-74 Tau Fibrillogenesis....Pages 75-90 Prion Protein Aggregation and Fibrillogenesis In Vitro ....Pages 91-108 α-Synuclein Aggregation and Modulating Factors....Pages 109-164 Pathological Self-Aggregation ofb 2 -Microglobulin: A Challenge for Protein Biophysics....Pages 165-183 Islet Amyloid Polypeptide: Aggregation and Fibrillogenesis in vitro and Its Inhibition....Pages 185-209 Mechanisms of Transthyretin Aggregation and Toxicity....Pages 211-224 Fibrillogenesis of Huntingtin and Other Glutamine Containing Proteins....Pages 225-251 Aggregation and Fibrillogenesis of Proteins not Associated with Disease: A Few Case Studies....Pages 253-270 Experimental Inhibition of Peptide Fibrillogenesis by Synthetic Peptides, Carbohydrates and Drugs....Pages 271-294 Experimental Inhibition of Fibrillogenesis and Neurotoxicity by amyloid-beta (Aβ) and Other Disease-Related Peptides/Proteins by Plant Extracts and Herbal Compounds....Pages 295-326 Front Matter....Pages 327-327 Alzheimer’s Disease....Pages 329-352 Modeling the Polyglutamine Aggregation Pathway in Huntington’s Disease: From Basic Studies to Clinical Applications....Pages 353-388 Parkinson’s Disease....Pages 389-455 Human Prion Diseases: From Kuru to Variant Creutzfeldt-Jakob Disease....Pages 457-496 Animal Prion Diseases....Pages 497-516 β 2 -Microglobulin Amyloidosis....Pages 517-540 Systemic AA Amyloidosis....Pages 541-564 Front Matter....Pages 327-327 Familial Amyloidotic Polyneuropathy and Transthyretin....Pages 565-607 The Challenge of Systemic Immunoglobulin Light-Chain Amyloidosis (AL)....Pages 609-642 Back Matter....Pages 634-634 This volume of the Subcellular Biochemistry series is devoted to the aggregation and fibrillogenesis of the amyloid-forming peptides and proteins, including emphasis on oligomer formation as well as fibril formation. The diverse topics included here are presented within 22 chapters, covering many of the relevant topics from both a basic science and clinical perspective. The authorship of these chapters is thoroughly international, with authoritative contributions from active researchers. Fundamental structural and cellular studies using many different technical approaches are presented, leading through to clinical and therapeutic aspects of the amyloid diseases, considered from both pharmaceutical and natural product view points. It is hoped that this book will be of use to both biomedical scientists and clinicians wishing to keep abreast of this rapidly advancing field, of direct importance to the understanding of cerebral neurodegenerative disease and systemic amyloid disease This volume is the result of the long-standing research interest of J. Robin Harris in the molecular mechanism underlying Alzheimer's disease and other amyloid diseases. The broad coverage represents an attempt to collate current knowledge relating to the proteins and peptides involved in most of the known amyloid diseases, together with some amyloid/fibril-forming proteins and peptides that are not involved in diseases