Amyloid Fibrils and Prefibrillar Aggregates: Molecular and Biological Properties

Amyloid Fibrils and Prefibrillar Aggregates: Molecular and Biological Properties

By: Daniel Erik Otzen (editor)Hardback

1 - 2 weeks availability

Description

Summing up almost a decade of biomedical research, this topical and eagerly awaited handbook is the first reference on the topic to incorporate recent breakthroughs in amyloid research. The first part covers the structural biology of amyloid fibrils and pre-fibrillar assemblies, including a description of current models for amyloid formation. The second part looks at the diagnosis and biomedical study of amyloid in humans and in animal models, while the final section discusses pharmacological approaches to manipulating amyloid and also looks at its physiological roles in lower and higher organisms. For Biochemists, Molecular Biologists, Neurobiologists, Neurophysiologists and those working in the Pharmaceutical Industry.

Create a review

About Author

Daniel Erik Otzen is Professor at the Interdisciplinary Nanoscience Centre of the Department of Molecular Biology at Aarhus University, Denmark. A graduate of Aarhus University, he obtained a Ph.D. in protein biophysics from the universities of Aarhus and Cambridge (UK). In 1995, he began work as a research chemist at Novo Nordisk, followed by post-doctoral work at Lund University (Sweden). In 2000, he joined the faculty of Aalborg University before taking up his current appointment at Aarhus in 2007. Professor Otzen has received several awards, including the Prize of the Alzheimer Research Foundation, the Carlsberg Biotechnology Prize and the Silver Medal of the Royal Danish Society. He has published more than 120 research articles and serves as an editor for the journals Biochimica Biophysica Acta and Biophysical Chemistry.

Contents

Preface XIX List of Contributors XXIII 1 The Amyloid Phenomenon and Its Significance 1 Christopher M. Dobson 1.1 Introduction 1 1.2 The Nature of the Amyloid State of Proteins 1 1.3 The Structure and Properties of Amyloid Species 5 1.4 The Kinetics and Mechanism of Amyloid Formation 7 1.5 The Link between Amyloid Formation and Disease 9 1.6 Strategies for Therapeutic Intervention 11 1.7 Looking to the Future 14 1.8 Summary 15 Acknowledgments 16 References 16 2 Amyloid Structures at the Atomic Level: Insights from Crystallography 21 Michael R. Sawaya and David Eisenberg 2.1 Atomic Structures of Segments of Amyloid-Forming Proteins 21 2.2 Stability of Amyloid Fibers 25 2.3 Which Proteins Enter the Amyloid State? 26 2.4 Molecular basis of Amyloid Polymorphism and Protein Strains 27 2.5 Atomic Structures of Steric Zippers Suggest Models for Amyloid Fibers of Parent Proteins 28 2.6 Atomic Structures of Steric Zippers Offer Approaches for Chemical Interventions against Amyloid Formation 31 2.7 Summary 34 Acknowledgments 36 References 36 3 What Does Solid-State NMR Tell Us about Amyloid Structures ? 39 Wolfgang Hoyer and Henrike Heise 3.1 Introduction 39 3.2 Principles of Solid-State NMR Spectroscopy and Experiments for Structural Constraints 40 3.3 Amyloid Fibrils Investigated by Solid-State NMR Spectroscopy 45 3.4 Summary 53 References 54 4 From Molecular to Supramolecular Amyloid Structures: Contributions from Fiber Diffraction and Electron Microscopy 63 Kyle L. Morris and Louise C. Serpell 4.1 Introduction 63 4.2 History 65 4.3 Methodology 68 4.4 Recent Advances in Amyloid Structure Determination 73 4.5 Summary 78 Acknowledgments 79 References 79 5 Structures of Aggregating Species by Small-Angle X-Ray Scattering 85 Cristiano L. P. Oliveira and Jan Skov Pedersen 5.1 Introduction 85 5.2 Theoretical and Experimental Aspects 85 5.3 Data Analysis and Modeling Methods 88 5.4 Studying Protein Aggregation and Fibrillation Using SAXS 91 5.5 General Strategies for Modeling SAXS Data from Protein Complexes 98 5.6 Summary and Final Remarks 100 Acknowledgments 101 References 101 6 Structural and Compositional Information about Pre-Amyloid Oligomers 103 Niels Zijstra and Vinod Subramaniam 6.1 General Introduction 103 6.2 Biophysical Techniques to Study Amyloid Oligomers 104 6.3 The Structure and Composition of Amyloid Oligomers 109 6.4 Concluding Remarks 116 Acknowledgments 118 References 118 7 The Oligomer Species: Mechanistics and Biochemistry 127 Massimo Stefani 7.1 Introduction 127 7.2 The Structure-Toxicity Relation of Early Amyloids 128 7.3 The Oligomer-Membrane complex 131 7.4 Biochemical Modification Underlying Amyloid Toxicity 134 7.5 Summary 141 References 141 8 Pathways of Amyloid Formation 151 Francesco Bemporad and Fabrizio Chiti 8.1 Introduction 151 8.2 Nomenclature of the Various Conformational States 152 8.3 Graphical Representations of the Mechanisms Leading to Amyloid 153 8.4 Pathways of Amyloid Fibril Formation 159 8.5 Nucleation Growth versus Nucleated Conformational Conversion 161 8.6 Summary 163 References 163 9 Sequence-Based Prediction of Protein Behavior 167 Gian Gaetano Tartagli and Michele Vendruscolo 9.1 Introduction 167 9.2 The Strategy of Zyggregator Predictions 167 9.3 Aggregation Under Other Conditions 173 9.4 Prediction of the Cellular Toxicity of Protein Aggregates 174 9.5 Relationship to Other Methods of Predicting Protein Aggregation Propensities 175 9.6 Competition between Folding and Aggregation of Proteins 177 9.7 Prediction of Protein Solubility from the Competition between Folding and Aggregation 177 9.8 Sequence-Based Prediction of Protein Interactions with Molecular Chaperones 179 9.9 Summary 179 References 180 10 The Kinetics and Mechanisms of Amyloid Formation 183 Samuel I. A. Cohen, Michele Vendruscolo, Christopher M. Dobson and Tuomas P. J. Knowles 10.1 Introduction 183 10.2 Classical Theory of Nucleated Polymerization 184 10.3 The Theory of Filamentous Growth with Secondary Pathways 193 10.4 Self-Consistent Solutions for the Complete Reaction Time Course 200 10.5 Summary 205 References 205 11 Fluorescence Spectroscopy as a Tool to Characterize Amyloid Oligomers and Fibrils 211 Per Hammarstrom, Mikael Lindgren and K. Peter R. Nilson 11.1 Introduction 211 11.2 Fluorescence Spectroscopy for Studies of Amyloid Reactions In vitro 212 11.3 Cysteine-Reactive Fluorescent Probes 214 11.4 Amyloidotropic Probes for Amyloid Fibrils and Oligomeric States 218 11.5 Luminescent Conjugated Poly and Oligothiophenes LCPs and LCOs 228 11.6 Summary 236 Acknowledgments 237 References 239 12. Animal Models of Amyloid Diseases 245 Stanislav Ott and Damian C. Crowther 12.1 Introduction 245 12.2 Some Big Questions Regarding Amyloid Diseases and Some Answers from Animal Models 247 12.3 Identifying the Toxic Species in the Systemic Amyloidoses 248 12.4 Identifying the Toxic Species in Alzheimer s Disease 250 12.5 Infectious Protein Misfolding 252 12.6 Conclusions 256 References 257 13 The Role of A in Alzheimer s Disease 263 Timothy M. Ryan, Blaine R. Roberts, Victor A. Streltsov, Stewart D. Nuttall and Colin L. Masters 13.1 History of Amyloidsis 263 13.2 Biochemistry of A 264 13.3 Amyloid Fibrils 268 13.4 The Soluble Oligomer Theory of AD 269 13.5 Other Factors Involved in Amyloid Plaque Formation in AD 274 12.6 Metal Ions 278 13.7 Other Potential A Interactions 280 13.8 Other Neurodegenerative Diseases 280 13.9 Conclusion 280 References 281 14 Experimental Approaches to Inducing Amyloid Aggregate 295 Lise Giehm and Daniel Otzen 14.1 The Need for Reproducible Fibrillation Assays 295 14.2 Setting Up an Assay to Monitor Fibrillation 296 14.3 Conditions That Promote Protein Aggregation 298 14.4 Processing and Batch Differences 312 14.5 Toward High-Throughput Assays 313 14.6 Summary 314 References 314 15 Fibrillar Polymorphism 321 Marcus Fandrick, Melanie Wulff, Jesper Sondergaard Pedersen and Daniel Otzen 15.1 Detection of Fibrillar Polymorphism 321 15.2 The Structural Definition of Fibril Polymorphism 322 15.3 The Two Classes of Fibril Polymorphism 328 15.4 How Does Fibrilliar Polymorphism Arise? 332 15.5 The Interconversion of Fibril Polymorphs 334 15.6 The Biological Implications of Fibril Polymorphism 335 15.7 Summary 337 Acknowledgments 338 References 338 16 Inhibitors of Amyloid and Oligomer Formation 345 Nikolai Lorenzen, Erich E. Wanker and Daniel Otzen 16.1 Introduction: Amyloidoses versus Neurodegenerative Diseases 345 16.2 Summary 362 References 363 17 Development of Therapeutic Strategies for the Transthyretin Amyloidoses 373 Colleen Fearns, Stephen Connelly, Evan T. Powers and Jeffrey W. Kelly 17.1 Introduction to Transthyretin Structure and Function 373 17.2 Introduction to Amyloid Diseases in General 373 17.3 Mechanism of Transthyretin Amyloidogenesis 378 17.4 Kinetic Stabilization of the Transthyretin Tetramer Ameliorates Amyloid Disease Genetic Evidence 379 17.5 Assessment of Diflunisal for Treatment of Transthyretin Amyloidosis 385 17.6 Tafamidis, the First Approved Drug for Treatment of a Transthyretin Amyloidosis 385 17.7 Summary 387 References 387 18 Hormone Amyloids in Sickness and in Health 395 Carolin Seuring, Nadezhda Nespovitaya, Jonas Rutishauser, Martin Spies and Roland Riek 18.1 Introduction 395 18.2 Constitutive vs. Regulated Secretory Pathways 395 18.3 Secretory Granules Contain Aggregated Cargo 396 18.4 Secretory Granule Aggregation by Functional Amyloid Formation 401 18.5 Hormone Amyloids in Disease: Diabetes Insipidus 402 18.6 conclusions 405 References 405 19 Functional Amyloids in Bacteria 411 Morten S. Dueholm, Per Halkjaer Nielsen, Matthew Chapman and Daniel Otzen 19.1 Introduction 411 19.2 Functional Amyloids are Common in Nature 412 19.3 Identification and Characterization of Functional Amyloids 413 19.4 Functional Bacterial Amyloids Play Many Roles 415 19.5 Biogenesis and Regulation of Functional Bacterial Amyloids 418 19.6 Structural Composition of Functional Amyloids 421 19.7 Assembly Properties of Functional Amyloid In Vitro 425 19.8 Diversity and Distribution of Functional Amyloid Genes 426 19.9 Summary 431 References 433 20 Structural Properties and Applications of Self-Assembling Peptides 439 Zhongli Luo and Shuguang Zhang 20.1 Introduction to Self-Assembling Peptides 439 20.2 The Principles of Self-Assembling Peptides 439 20.3 Self-Assembling Peptide Nanofibers 443 20.4 Diverse Applications of Self-Assembling Peptide Nanofibers Scaffolds 446 20.5 Summary 451 Acknowledgments 452 References 452 21 Harnessing the Self-Assembling Properties of Proteins in Spider Silk and Lung Surfactant 455 Jan Johansson 21.1 Introduction 455 21.2 Amino Acid Sequences and Amyloid Formation 455 21.3 Spider Silk and How the Spiders Make It 458 21.4 Harnessing the Properties of Spider Silk and Its Constituent Proteins 461 21.5 Biosynthesis of an -Helix from One of the Most -Prone Sequences Known 462 21.6 Anti-Amyloid Properties of the BRICHOS Domain 464 21.7 Summary 465 Acknowledgments 465 References 466 Index 471

Product Details

  • publication date: 06/02/2013
  • ISBN13: 9783527332007
  • Format: Hardback
  • Number Of Pages: 464
  • ID: 9783527332007
  • weight: 1218
  • ISBN10: 3527332006

Delivery Information

  • Saver Delivery: Yes
  • 1st Class Delivery: Yes
  • Courier Delivery: Yes
  • Store Delivery: Yes

Prices are for internet purchases only. Prices and availability in WHSmith Stores may vary significantly

Close