Verfügbarkeit: Bio-nanoimaging

Bio-nanoimaging: protein misfolding & aggregation

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Bibliographische Detailangaben
Weitere Verfasser:	Uverskij, Vladimir N. (HerausgeberIn)
Format:	Buch
Sprache:	English
Veröffentlicht:	Amsterdam [u.a.] Elsevier, Academic Press 2014
Online-Zugang:	Inhaltsverzeichnis
Beschreibung:	XIX, 526 S. Ill., graph. Darst.
ISBN:	9780123944313

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Datensatz im Suchindex

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adam_text	Titel: Bio-nanoimaging Autor: Uverskij, Vladimir N Jahr: 2014 Contents Contributors xv 1. Molecular Mechanisms of Protein Misfolding Leonid Breydo and Vladimir N. Uversky Introduction 1 The Mechanism of Aggregation 1 Structures of Protein Aggregates 3 Protein Aggregation Pathways 5 Amyloid Beta, Aß 5 a-Synuclein 6 Yeast and Fungal Prions 7 Mammalian Prions 7 Insulin 8 Functional Amyloids 9 ß-2 Microglobulin 10 Other Amyloidogenic Proteins 10 Conclusions 10 References 10 Part I Nanoimaging and Nanotechnology of Aggregating Proteins: A. In Vitro Approaches 2. Amyloid Fibril Length Quantification by Atomic Force Microscopy Wei-Feng Xue Background 17 Acquiring Images for Length Quantification 17 Single-Particle Measurements of Individual Fibril Length 19 Distributions of Fibril Length 20 Prospects for Fibril Length Distribution Analysis 22 Acknowledgments 24 References 25 3. Imaging Nucleation, Growth and Heterogeneity in Self-Assembled Amyloid Phases Neil R. Anthony, Keith M. Berland, Anil K. Mehta, David G. Lynn and W. Seth Childers Introduction 27 Diversity in Cross-ß Assemblies 28 Particle Phases 29 Paracrystallization 31 Paracrystalline Polymorphism 33 Functional Energy Transfer 33 Closing Perspective 34 Acknowledgments 35 References 35 4. Molecular-Level Insights into Amyloid Polymorphism from Solid-State Nuclear Magnetic Resonance Robert Tycko Introduction 37 Self-Propagating Molecular-Level Polymorphism in Aß^o Fibrils 38 Competition between Parallel and Antiparallel ß-Sheets in D23N-Aß1.40 Fibrils 39 pH-Dependent Cross-ß Motif in Aß^s Fibrils 41 Polymorphism in Prion Fibrils 41 Future Directions 45 Acknowledgments 45 References 45 5. Single-Molecule Imaging of Amyloid-ß Protein (Aß) of Alzheimer s Disease: From Single-Molecule Structures to Aggregation Mechanisms and Membrane Interactions Marie-Isabel Aguilar, Xu Hou, Dusan Losic, Adam I. Mechler, Lisandra L. Martin and David H. Small v vi Contents Introduction 47 Principles of High-Resolution Imaging by STM and AFM 48 Monomeric and Oligomeric Structures of Aß Determined by STM and AFM 48 Mechanism of Aß Fibrillogenesis Examined by AFM 51 Aß Structure on Model Membranes Examined by High-Resolution AFM 52 Models of Aß Structure Based on High-Resolution Imaging 52 References 54 6. Nanomechanics of Neurotoxic Proteins: Insights at the Start of the Neurodegeneration Cascade Rubén Hervás, María del Carmen Fernández- Ramírez, Laura Esther Abelleira, Mariano Carrión-Vázquez and Douglas V. Laurents Introduction 57 Intrinsically Disordered Proteins: Central Roles and Fatal Diseases 57 Amyloidogenic Neurodegenerative Diseases: A Subset of Conformational Diseases 58 Single-Molecule Analysis of Neurotoxic Proteins 60 AFM-Based Single-Molecule Force Spectroscopy: Principle and Modes 60 Single-Molecule Markers: The Carrier-Guest Strategy 61 Testing the Amyloidogenic Behavior of Fusion Proteins and the Integrity of the Carrier Protein 61 Conformational Polymorphism of Neurotoxic Proteins 62 Application of SMFS to Test Putative Therapeutic Agents 64 Molecular Dynamics Simulations of Amyloidogenesis by Neurotoxic Proteins 64 Future Perspectives 65 Abbreviations 66 Acknowledgments 66 References 66 7. Reporters of Amyloid Structural Polymorphism Harry LeVine III, K. Peter, R. Nilsson and Per Hammarström Background and Rationale 69 Ligand-Binding Phenotype 69 Conformational/Configurational Antibodies 70 Ligand-Binding Sites 70 Probes that Report their Conformation and Environment 71 Flydrophobic Probes and Molecular Rotors 71 Luminescent Conjugated Oligo- and Polythiophenes 73 Assessing Pathology Spread and Quantification 75 Applications and Implications of Polymorphism-Sensitive Reporters 77 Diagnostics 77 Therapeutics 77 References 77 8. Conformation-Dependent Antibodies as Tools for Characterization of Amyloid Protein Aggregates Jessica W. Wu and Leonid Breydo Introduction Amyloid Fibrils and Oligomers have Defined, Unique Tertiary Structures and Molecular Polymorphisms that are Recognized by Conformation-Specific Antibodies Types of Conformation-Specific Antibodies Against Protein Aggregates Sequence-Specific Antibodies Sequence-Independent Antibodies Fibril-Specific Antibodies Oligomer-Specific Antibodies Conformation-Specific Antibodies as Probes for Studying Protein Structure and Changes in Conformation Underlying Protein Aggregation Conformation-Specific Antibodies Recognize Polymorphism within Amyloid Oligomers and Fibrils 87 Conformation-Specific Antibodies as Probes for Studying Protein-Folding Mechanisms 88 Therapeutic Applications of Conformation-Specific Antibodies in Neurodegenerative Diseases 89 Active Immunotherapy 89 Passive Immunotherapy 90 Conclusions 90 References 91 Part II Nanoimaging and Nanotechnology of Aggregating Proteins: B. In Vivo Approaches 9. Analyzing Alzheimer s Disease- Related Protein Deposition In Vivo By Multiphoton Laser Scanning Microscopy 81 82 84 85 86 86 86 87 Niki ta Rudinskiy and Tara L. Spires-Jones Protein Aggregation in Alzheimer s Disease 97 Contents vii In Vivo Multiphoton Imaging In Vivo Imaging of Amyloid Plaques and Neurofibrillary Tangles and Associated Neuroanatomic Pathology Imaging Functional Changes Induced by AD-Related Pathology Limitations of In Vivo Multiphoton Imaging Conclusions References 98 99 101 101 102 102 10. Probing Amyloid Aggregation and Morphology In Situ by Multiparameter Imaging and Super-Resolution Fluorescence Microscopy Gabriele S. Kaminski Schierle, Markus Sauer and Clemens F. Kaminski Introduction 105 Multi-Parameter Microscopy of Protein Aggregation Kinetics 106 Fusion Protein Labeling of Amyloidogenic Proteins 106 Principle of Multi-Parameter Imaging Techniques 107 Fluorescence Anisotropy Imaging 107 Fluorescence Lifetime Imaging of Protein Aggregation 108 Super-Resolution Imaging of Amyloid Aggregation 111 Single-Molecule-Based Localization Microscopy for Direct Visualization of Amyloid Morphology 111 Fluorophores for Localization Microscopy 112 Realization of Direct Stochastic Optical Reconstruction Microscopy Experiments 113 In Situ Imaging of Abeta 40 and Abeta 42 Self Assembly Reactions 113 Super-Resolution Imaging of Fluman Lysozyme 115 Conclusion 115 Acknowledgments 117 References 117 11. Imaging of Amyloid-ß Aggregation Using a Novel Quantum dot Nanoprobe and its Advanced Applications Kiyotaka Tokuraku and Tsuneya Ikezu Introduction of Amyloid-ß Peptide Biology and Quantum dot Properties 121 Preparation of the Quantum dot Nanoprobe 122 In Vitro Imaging and Quantification of Aß Aggregation 122 Imaging of Aß Behaviors in Live Cell Cultures 124 High-Throughput Microscreening of Substances Inhibitory to Aß Aggregation 127 Current Problems and Future Possibilities of this Imaging Technology 129 References 130 12. Studying the Molecular Determinants of Protein Oligomerization in Neurodegenerative Disorders by Bimolecular Fluorescence Complementation Federico Herrera, Susana Gonçalves, Joana Branco dos Santos and Tiago Fleming Outeiro Introduction 133 Neurodegenerative Disorders and Protein Misfolding 134 Protein Oligomerization, Aggregation and Toxicity 134 Protein Complementation Assays: History and Latest Developments 134 Advantages of BiFC Systems for Studying Protein Interactions 136 Protein Complementation Assays for the Study of Neurodegenerative Disorders 139 Methods 140 Design 140 Development 141 Troubleshooting 141 Acknowledgments 142 References 142 13. Structure-Specific Intrinsic Fluorescence of Protein Amyloids Used to Study their Kinetics of Aggregation Fiona T.S. Chan, Dorothea Pinotsi, Gabriele S. Kaminski Schierle and Clemens F. Kaminski Introduction Characterization of Oligomers Using Tryptophan and Tyrosine Fluorescence Certain Protein Crystals and Aggregates Develop Intrinsic Fluorescence in the Visible Range Intrinsic Fluorescence Arising from Disease- Related Protein Amyloids During Aggregation Does the Intrinsic Fluorescence of Protein Amyloids Provide Novel Insights into their Remarkable Stability? Intrinsic Amyloid Fluorescence Informs on the Kinetics of Amyloid Formation and Mechanisms of Protein Misfolding Diseases Conclusions Future Work Acknowledgments References 147 148 149 149 151 152 153 154 154 154 viii Contents 14. Real-Time Monitoring of Inclusion Formation in Living Zebrafish Sophie Rothhämei, Katrin Strecker, Christian Haass and Bettina Schmid Introduction 157 Zebrafish as a Model Organism 158 Techniques for Generating Aggregation Models in Zebrafish 158 Time-Lapse In Vivo Imaging Techniques 159 Modeling Inclusion Formation in an HD Model in Zebrafish 162 In Vivo Imaging of Inclusion Formation in Zebrafish 163 Concluding Remarks and Outlook 163 References 164 15. Scanning for Intensely Fluorescent Targets (SIFT) in the Study of Protein Aggregation at the Single-Particle Level Georg Nübling and Armin Giese The Role of Protein Aggregation in Neurodegeneration 167 Measuring Protein Aggregation: From Fibril Formation to Single-Particle Analysis 168 The SIFT Method: Introduction and Technical Background 168 Methods of Analysis 168 Autocorrelation and Cross-Correlation Analysis 168 Fluorescence Intensity Distribution Analysis (FIDA) 169 SIFT and SIFT-2D Analysis 170 Förster Resonance Energy Transfer (FRET) 170 Practical Applications 170 Monitoring Protein Aggregation in the Single-Color Mode 170 Advantages of Dual-Color Monitoring of Protein Aggregation 171 High-Throughput Screening Assays 171 Protein Aggregation - Specificity and Dynamics of Aggregation Processes 172 Interactions between Different Particle Species 172 Monitoring Effects of Post-Translational Modifications 174 Pitfalls and Common Misconceptions 174 Technical Issues and Protein Handling 174 Data Interpretation 175 References 176 Part III Polymorphism of Protein Misfolding and Aggregated Species 16. The Molecular Basis for TGFBIp- Related Corneal Dystrophies Marcel Stenvang, Maria Andreasen, Jan Johannes Enghild and Daniel E. Otzen Introduction 179 Challenges in Understanding the Role of TGFBIp in Corneal Dystrophies 180 Molecular Properties of TGFBIp: A Multidomain Protein with Four Homologous Domains 180 TGFBIp and Corneal Dystrophy 182 CD Mutations Induce Different TGFBIp Aggregation Mechanisms 182 CD and Changes in Proteolytic Processing of TGFBIp 183 TGFBIp Oligomerization 183 TGFBIp and Macromolecular Interactions 184 Aggregation Mechanism and Phenotypes 184 Future Treatment 185 Acknowledgments 186 References 186 17. Aß Fibril Polymorphism and Alzheimer s Disease Magdalena Bereza and Marcus Fändrich Alzheimer s Disease: Relevance, Neuropathology and Etiology 189 Cellular Formation and Chemical Variability of Aß Peptide 189 The Amyloid Hypothesis and the Putative Mechanism of Pathogenesis 190 General Topology and Polymorphism of Aß Fibrils 190 Towards the Atomic Structures of Different Aß Fibril Polymorphs 191 The Molecular Basis of Aß Fibril Polymorphism 193 Biologic Relevance of Polymorphic Fibril Structures 194 Acknowledgments 195 References 195 18. Structural Heterogeneity and Bioimaging of S100 Amyloid Assemblies Sofia B. Carvalho, Hugo M. Botelho, Cláudio M. Gomes, Isabel Cardoso, Kiran Yanamandra, Ludmilla A. Morozova-Roche and Gunter Fritz Contents ix Introduction 197 Structural Diversity of S100 Monomers and Multimers 198 S100 Structure and Folding 198 Ca2+ and Other Metal-Binding Properties 199 S100 Oligomers, Aggregates and Amyloids 200 S100 Functional Oligomers 200 Amyloidogenic and Aggregation Potential of S100 Proteins 201 Effects of SI 00 on Aggregation Cross-Seeding 201 Role of Metal Ions in Aggregation Pathways 202 Bioimaging of S100 Amyloids by AFM and TEM 202 Techniques to Study Protein Amyloid Formation 202 Sources of Amyloid - In Vivo and In Vitro 203 S100A8/A9 Amyloids 203 Amyloidogenic Properties of SI 00A6 Studied by TEM 204 S100B Amyloid Formation In Vitro 206 Ex Vivo S100A8/A9 Amyloids Imaged by AFM and TEM 207 Macroscopic Amyloid Properties of Corpora Amylacea Studied by Optical Microscopy 208 Conclusions 209 Abbreviations 209 Acknowledgments 209 References 210 19. Polymorphism of Tau Fibrils Yoshiaki Furukawa Introduction 213 Polymorphic Nature of Pathologic Tau Fibrils 213 Factors Affecting the Morphology of Tau Fibrils 214 Splicing Isoforms of Tau 214 Inducers of Tau Fibrillation 216 A Thiol-Disulfide Status of Tau 217 A Core Hypothesis for Generating Fibril Polymorphism 218 Perspectives 219 References 220 20. Amyloid-Like Protofibrils with Different Physical Properties Annalisa Relini Introduction Protofibril Polymorphism Coexistence of Different Protofibril Populations Mechanical Properties of Protofibrils Concluding Remarks Acknowledgments References 223 224 225 227 229 230 230 21. Insulin Oligomers: Detection, Characterization and Quantification Using Different Analytical Methods Mirco Sorci and Georges Belfort Introduction 233 Spectroscopy 234 Mass Spectrometry (MS) 234 Electrospray Differential Mobility Analysis (ES-DMA) 234 Nuclear Magnetic Resonance (NMR) 234 Scattering Techniques 235 Dynamic Light Scattering (DLS) 235 Small-Angle Neutron Scattering (SANS) 237 Small-Angle X-Ray Scattering (SAXS) 238 Microscopy 238 Atomic Force Microscopy (AFM) 238 Cryogenic Transmission Electron Microscopy (cryo-TEM) 238 Separation Techniques 238 Size-Exclusion Chromatography (SEC) 238 Electrophoresis (NuPACE) 240 Capillary Electrophoresis (CE) 240 Membrane Filtration (MF) 240 Indirect Measurements 241 Cooling and Seeding Experiments 241 Theoretical Calculation 241 Conclusions 241 References 243 22. Imaging the Morphology and Structure of Apolipoprotein Amyloid Fibrils Yee-Foong Mok, Chai Lean Teoh, Geoffrey J. Flowlett and Michael D.W. Griffin Introduction 247 ApoA-l 247 ApoE 247 ApoC-ll 248 Structural Analysis of ApoC-ll Amyloid Fibrils 249 Flexibility and Tangling of ApoC-ll Amyloid Fibrils 250 Characterization of Straight ApoC-ll Fibrils 251 Summary 253 References 253 23. Polymorphism of Amyloid Fibrils and their Complexes with Catatase Nathaniel G.N. Milton and J. Robin Harris Introduction Catatase Interactions with Amyloid-ß, Islet Amyloid Polypeptide and Prion Protein Fragments 255 256 X Contents Binding of Catalase to Aß, IAPP and PrP Fibrils 257 The Shared Amyloid Catalase Recognition Sequence and Other Potential Amyloid Fibril Interactions 259 Use of Catalase Binding to Amyloid Fibrils in Drug Discovery 259 Conclusion 260 References 260 24. On Possible Function and Toxicity of Multiple Oligomeric/Conformational States of a Globular Protein - Human Stefin B Eva ¿erovnik 263 Introduction Defining Intermediate States from which Amyloid Fibrils were Initiated 263 Kinetic Model and Morphologies of Amyloid Fibril Formation 265 Structural Data on Stefin Oligomers and the Role of Proline Isomerism 266 Selective Interaction of the Tetramer of Stefin B with Aß 267 The Role of Copper 268 Membrane Binding and Pore Formation 268 Conclusions and Perspective 268 Acknowledgments 268 References 268 25. Fibrillar Structures of Yeast Prion Sup35 In Vivo Hideki Taguchi and Shigeko Kawai-Noma Introduction 271 Yeast Prion Sup35 as a Model Amyloid- Forming Protein in Cells 271 In Vitro Fibril Formation of Sup35 272 Structures of Sup35 Amyloids in Yeast Cells 272 Transmission Electron Microscopy (TEM) 273 Correlative Light Electron Microscopy (CLEM) 274 Cryo-Electron Tomography 274 Dynamic Properties of Sup35 Amyloids in Living Yeast Cells 275 Single-Cell Imaging System for Monitoring the Fate of Sup35-CFP Foci 275 Fluorescence Correlation Spectroscopy (FCS) 276 Fluorescence Recovery after Photobleaching (FRAP) 278 Concluding Remarks 278 References 278 26. Glycosaminoglycans and Fibrillar Polymorphism Kirsten G. Malmos and Daniel E. Otzen Introduction 281 Proteoglycan Components Responsible for Protein Binding and Fibril Enhancement 282 The Polymeric Nature of CACs is Important for Inducing Mature Amyloid Fibrils 283 GAGs Affect Fibril Morphology in Different Ways 283 Specificity of GAG-Protein Interactions 285 GAGs can Induce Fibrils in Non- Amyloidogenic Proteins 285 GAGs can Accelerate Fibrillation by Binding Monomers or by Interacting with Oligomers 285 Future Perspectives and Challenges: The Importance of Molecular Insights 288 Acknowledgments 288 References 288 27. Dopamine-Induced a-Synuclein Oligomers Agata Rekas, Roberto Cappai, Cyril Curtain and Chi Le Lan Pham The Role of Dopamine in a Healthy Brain and in Parkinson s Disease 291 a-Synuclein:DA Oligomers - Discovery and Properties 292 Shape and Structure of a-Syn:DA Oligomers 293 How Does DA Link a-Syn Molecules? 293 How Does DA Inhibit a-Synuclein Fibril Formation? 297 Biologic Significance of a-Syn:DA Oligomers 298 References 299 28. The Formation of Amyloid-Like Superstructures: On the Growth of Amyloid Spherulites Vito Foderà and Athene M. Donald Large-Scale Polymorphism in Protein Aggregation 301 Amyloid Spherulites: Hypotheses on the Structural Arrangement 302 Factors Affecting the Formation of Insulin Amyloid Spherulites 304 Effect of Temperature and Salt 304 Effect of p H 306 Effect of Protein Concentration 307 Conclusions and Perspectives 307 Contents xi Acknowledgments 308 References 308 29. Characterizing Nanoscale Morphologic and Mechanical Properties of a-SynucIein Amyloid Fibrils with Atomic Force Microscopy Kim K.M. Sweers, Martin Stockt, Martin L. Bennink and Vinod Subramaniam Introduction 309 aS Fibrils on Different Solid Surfaces 310 Preparation of Supported Lipid Bilayers on Mica 311 a-Synuclein Monomers on Supported Bilayers 312 a-Synuclein Fibrils on POPC-Supported Bilayers 312 Inferring the Mechanical Properties of Fibrils from Images 317 Wild-Type Fibrils on a POPC-POPC Supported Bilayer 319 Conclusions 320 Materials and Methods 320 a-Synuclein and Fibril Preparation 320 Sample Preparation 320 Atomic Force Microscopy 320 References 320 30. Polymorphism in Casein Protein Aggregation and Amyloid Fibril Formation David C. Thorn, Heath Ecroyd and John A. Carver Introduction to the Casein Proteins 323 Biological Functions of Casein Proteins 323 Structural Features of Casein Proteins 323 Chapetone Ability of Casein Proteins 324 Amyloid Fibril-Forming Propensity of K- and as2-Casein and the Preventative Role of the Casein Micelle 324 Amorphous Aggregation Properties of Casein Proteins Under Native Conditions 324 The Casein Micelle 324 The Individual Casein Proteins 325 Amyloid Fibril Formation by k- and as2-Casein Proteins 325 Modification and Inhibition of k- and as2-Casein Amyloid Fibril Formation by ß- and as1-Caseins 328 Potential Bio-Nanomaterial Applications of Casein Amyloid Fibrils 329 Conclusions 330 Acknowledgments 330 References 330 31. Structural Basis for the Polymorphism of ß-Lactoglobulin Amyloid-Like Fibrils Corianne C van den Akker, Michael Schleeger, Mischa Bonn and Gijsje H Koenderink Why ß-Lactoglobulin? 333 Formation Mechanisms of Amyloid-Like Fibrils from ß-Lactoglobulin 333 Polymorphism of ß-Lactoglobulin Amyloids: Rod-Like, Worm-Like and Straight Fibrils 334 Protein Concentration 334 Solution pH 335 Solvent 336 Ionic Strength 336 Shear Forces 336 Reaction Time 336 Molecular Structure of Amyloid Fibrils 336 Circular Dichroism Spectroscopy 336 FT-IR Spectroscopy 338 Raman Spectroscopy 338 VSFG Spectroscopy 339 Tip-Enhanced Raman Spectroscopy (TERS) 340 Conclusions 341 Acknowledgment 341 References 341 32. Fibrillation and Polymorphism of Human Serum Albumin Silvia Barbosa, Pablo Taboada and Víctor Mosquera Introduction 345 The Origin of Protein Misfolding 346 Protein Misfolding and Fibrillation 346 Relevant Characteristics of Prefibrillar and Fibrillar States 347 The Fibrillation Process of Human Serum Albumin 350 The Structure of Human Serum Albumin 350 The Influence of External Factors on HSA Fibrillation 351 Fibrillation Kinetics of HSA 352 The Fibrillation Pathway of HSA 353 Some Potential Technologic Applications of HSA Fibrils 358 Conclusions and Outlook 359 References 360 33. Formation of a-Helix-Based Twisted Ribbon-Like Fibrils from Ionic- Complementary Peptides Meng Qin, Dawei Zou, Yi Cao and Wei Wang x¡¡ Contents Introduction EMK8-II with Protected Terminus Forms Twisted Ribbon-Like Fibrils Structural Characteristics of EMK8-II Fibrils Assembly Dynamics of EMK8-II Fibrils Cooperative Balance of Hydrophobicity and Ionic Interactions The Assembly Mechanism of a-Helix-Based Fibrils Acknowledgments References 34. Polymorphism, Metastable Species and Interconversion: The Many States of Glucagon Fibrils Shirin D. Ghodke, Grethe V. Jensen, Anna S.P. Svane, Katrin Weise, Anne Sondergaard, Manja A. Behrens, Jan Skov Pedersen, Niels Chr Nielsen, Jesper S0ndergaard Pedersen, Roland Winter and Daniel E. Otzen 363 364 364 366 368 370 370 370 374 Introduction The Basis of Fibril Polymorphism: Different Protofilament Packing and/or Different Protofilaments 374 How to Obtain Different Types of Glucagon Fibril: An Overview of the Current Literature 374 A Time-Resolved SAXS Study of the Effect of Shaking on Fibrillation and Fibril Structure: Different Degrees of Protofilament Association Under Quiescent and Shaking Conditions 375 Interconversion between Fibril Morphologies: Metastable Fibril States Destabilized by Elevated Temperatures 376 Hydration and Packing Modulate Fibrillation and Fibril Stability 379 Inhibition of Glucagon Fibrillation by Modified Cyclodextrins 382 Perspectives: Stable or Unstable Fibrils In Vivói 384 Acknowledgments 384 References 384 Part IV Polymorphism of Protein Misfolding and Aggregation Processes 35. Multiple Pathways of Lysozyme Aggregation Martin Muschol, Shannon E. Hill and Mentor Mulaj Introduction 389 Polymorphism of Amyloid Intermediates and Multiple Assembly Pathways 389 Atomic Force Microscopy for Studying Amyloid Self-Assembly 390 Characterizing Lysozyme Assembly Pathways and their Respective Intermediates with Atomic Force Microscopy 390 Lysozyme Fibril Assembly Follows Distinct Assembly Pathways 390 Morphology of Amyloid Intermediates in Either Pathway 391 Physical Characterization of Transient Intermediates 392 Conclusions and Discussion 394 References 395 36. Structure-Function Studies of Amyloid Pores in Alzheimer s Disease as a Case Example of Neurodegenerative Diseases Fernando Teran Arce, Hyunbum Jang, Laura Connelly, Srinivasan Ramachandran, Bruce L. Kagan, Ruth Nussinov and Ratnesh Lai General Properties of Amyloids 397 Amyloids in Alzheimer s Disease 398 Interaction of Peptides with the Cell Membrane 398 Pore Hypothesis 399 Structural and Functional Studies of Amyloid Pores 400 Functional Studies 400 Structural Studies 401 Alternative Mechanisms 403 Acknowledgments 404 References 404 37. Nanoscale Optical Imaging of Protein Amyloids Samrat Mukhopadhyay, Vijit Dalai and Shruti Arya Introduction 409 Structural Biology of Amyloids 410 Nanoscale Biophysics of Amyloid Fibrils Using Super-Resolution Optical Imaging 412 Near-Field Scanning Optical Microscopy 412 Apertureless Near-Field Scanning Infra-Red Microscopy 414 Direct Stochastic Optical Reconstruction Microscopy 417 Photoactivation Localization Microscopy 419 Nanoscale Raman Imaging: Tip-Enhanced Raman Scattering and Coherent Anti-Stokes Raman Scattering 421 Contents xiii Conclusions and Future Projections Acknowledgments References 424 425 425 38. Assembly of Amyloid ß-Protein Variants Containing Familial Alzheimer s Disease- Linked Amino Acid Substitutions Aida Attar, Derya Meral, Brigita Urbane and Gal Bitan Introduction: Minor Changes have Major Effects Point Mutations Affecting the Aß Sequence Substitutions in Positions 21-23 N-terminal and C-terminal Substitutions Conclusions Acknowledgments References 39. Role of Aberrant a-Synuclein- Membrane Interactions in Parkinson s Disease Amy M. Griggs, Daniel Ysselstein and Jean-Christophe Rochet Introduction Evidence for Membrane-Induced a-Syn Self-Assembly Conformations of a-Syn at the Membrane Surface A Role for Aberrant a-Syn-Membrane Interactions in Neurotoxicity Concluding Remarks References 40. ELOA- Equine Lysozyme Complexes with Oleic Acid: Structure and Cytotoxicity Studied by Bio-Imaging Techniques Vladana Vukojevió, Alexei Klechikov and Ludmilla A Morozova-Roche Introduction 453 HAMLET: Occurrence In Vivo and In Vitro 453 Structural Similarity of EL and a-Lactalbumins 454 The Production of HAMLET-Type Complexes 455 Protein Conformation in ELOA 455 ELOA Oligomeric Structure 456 ELOA Interaction with Lipid Bilayers 457 ELOA Cellular Toxicity 458 Conclusions 460 Acknowledgments 460 References 460 41. Structure of a Misfolded Intermediate of a PDZ Domain Alfonso De Simone, Stefano Gianni and Michele Vendruscolo Introduction Results The 0-value Approach to Determine the Structures of Protein 463 464 Intermediates 464 A Structural Model of the Misfolded 429 Intermediate 468 430 Validation of the Structural Model of 430 the Misfolded Intermediate 468 436 Structural Models of the TSN and TS/ 438 Transition States 469 439 Significance of the Structure of the 439 Misfolded Intermediate 471 Conclusions 472 Acknowledgments 472 References 473 42. Intranuclear Amyloid - Local and Quantitative Analysis of Protein Fibrillation in the Cell 443 Nucleus 444 Florian Arnhold and Anna von Mikecz Disease-Associated Protein Fibrillation 475 445 Functional Amyloid 475 Characterization of Nuclear Protein 447 Fibrillation 477 447 Conclusions 482 448 Acknowledgments 483 References 483 43. Conversion of a-Helical Proteins into an Alternative ß-Amyloid Fibril Conformation Jason C. Collins and Lesley H. Greene Introduction to the Fibril Field 485 Transition of a-Helical Proteins into Amyloid-Like Fibrils 487 Alpha-Helical Proteins Associated with Disease States 487 Alpha-Helical Proteins not Associated with Disease 490 Polymorphism of Fibrillar Species Associated with a-Helical Proteins 492 Polymorphic Investigations of a-Helical Proteins 493 Future Perspectives 499 References 499 xiv Contents 44. The Effect of Shear Flow on Amyloid Fibril Formation and Morphology Innocent B. Bekard and Dave E. Dunstan Introduction 503 Shear Flow and Protein Misfolding 504 Effect of Shear Flow on Fibril Formation 508 Observed Structures: Impact of Flow on Fibril Structure and Mechanics 510 Conclusions 511 References 512 Subject Index 515 Name Index 523
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illustrated	Illustrated
indexdate	2024-07-10T01:13:44Z
institution	BVB
isbn	9780123944313
language	English
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oclc_num	915482587
open_access_boolean
owner	DE-11 DE-29T
owner_facet	DE-11 DE-29T
physical	XIX, 526 S. Ill., graph. Darst.
publishDate	2014
publishDateSearch	2014
publishDateSort	2014
publisher	Elsevier, Academic Press
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spelling	Bio-nanoimaging protein misfolding & aggregation ed. by Vladimir N.Uversky , Yuri L. Lyubchenko Amsterdam [u.a.] Elsevier, Academic Press 2014 XIX, 526 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Uverskij, Vladimir N. (DE-588)13389651X edt HBZ Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=027582278&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis
spellingShingle	Bio-nanoimaging protein misfolding & aggregation
title	Bio-nanoimaging protein misfolding & aggregation
title_auth	Bio-nanoimaging protein misfolding & aggregation
title_exact_search	Bio-nanoimaging protein misfolding & aggregation
title_full	Bio-nanoimaging protein misfolding & aggregation ed. by Vladimir N.Uversky , Yuri L. Lyubchenko
title_fullStr	Bio-nanoimaging protein misfolding & aggregation ed. by Vladimir N.Uversky , Yuri L. Lyubchenko
title_full_unstemmed	Bio-nanoimaging protein misfolding & aggregation ed. by Vladimir N.Uversky , Yuri L. Lyubchenko
title_short	Bio-nanoimaging
title_sort	bio nanoimaging protein misfolding aggregation
title_sub	protein misfolding & aggregation
url	http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=027582278&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA
work_keys_str_mv	AT uverskijvladimirn bionanoimagingproteinmisfoldingaggregation

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