Amyloid fibrils and prefibrillar aggregates: molecular and biological properties
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2013
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| 245 | 1 | 0 | |a Amyloid fibrils and prefibrillar aggregates |b molecular and biological properties |c ed. by Daniel Erik Otzen |
| 264 | 1 | |a Weinheim |b Wiley-VCH |c 2013 | |
| 300 | |a XXVIII, 481 S. |b Ill., graph. Darst. |c 24 cm x 17 cm | ||
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IMAGE 1
V I I
CONTENTS
PREFACE X I X
LIST O F CONTRIBUTORS XXIII
1 THE AMYLOID PHENOMENON AND ITS SIGNIFICANCE 1
CHRISTOPHER M. DOBSON
1.1 INTRODUCTION 1
1.2 THE NATURE O F THE AMYLOID STATE O F PROTEINS 1
1.3 THE STRUCTURE A N D PROPERTIES O F AMYLOID SPECIES 5
1.4 THE KINETICS A N D MECHANISM O F AMYLOID FORMATION 7
1.5 THE LINK BETWEEN AMYLOID FORMATION A N D 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 O F
SEGMENTS O F AMYLOID-FORMING PROTEINS 21 2.1.1 PROTEIN SEGMENTS THAT
FORM AMYLOID-RELATED CRYSTALS 21 2.1.2 ATOMIC STRUCTURES O F FIBER-LIKE
MICROCRYSTALS 23
2.2 STABILITY O F AMYLOID FIBERS 25
2.3 WHICH PROTEINS ENTER THE AMYLOID STATE? 26
2.4 MOLECULAR BASIS O F AMYLOID POLYMORPHISM A N D PRION STRAINS 2 7 2.5
ATOMIC STRUCTURES O F STERIC ZIPPERS SUGGEST MODELS FOR AMYLOID FIBERS O
F PARENT PROTEINS 28 2.6 ATOMIC STRUCTURES O F STERIC ZIPPERS OFFER
APPROACHES FOR CHEMICAL
INTERVENTIONS AGAINST AMYLOID FORMATION 31 2.7 SUMMARY 34
ACKNOWLEDGMENTS 36 REFERENCES 36
HTTP://D-NB.INFO/1024048233
IMAGE 2
V I I I I CONTENTS
3 WHAT DOES SOLID-STATE NMR TELL US ABOUT AMYLOID STRUCTURES? 3 9
WOLFGANG HOYER AND HENRIKE HEISE 3.1 INTRODUCTION 39
3.2 PRINCIPLES O F SOLID-STATE NMR SPECTROSCOPY A N D EXPERIMENTS FOR
STRUCTURAL CONSTRAINTS 40 3.2.1 ISOTOPE LABELING, MAGIC ANGLE SPINNING,
DIPOLAR COUPLING, A N D RESONANCE ASSIGNMENT 40 3.2.2 DEFINING THE
AMYLOID CORE BY MAGNETIZATION TRANSFER FROM
WATER 43
3.2.3 DETERMINING THE FIBRIL REGISTRY 43
3.2.4 SEEDED VERSUS UNSEEDED FIBRILS 44
3.3 AMYLOID FIBRILS INVESTIGATED BY SOLID-STATE NMR SPECTROSCOPY 45
3.3.1 AF5 PEPTIDES O F DIFFERENT LENGTH 46
3.3.2 ISLET AMYLOID POLYPEPTIDE (IAPP/AMYLIN): PARALLEL A N D
ANTIPARALLEL STERIC ZIPPERS 47 3.3.3 A-SYNUCLEIN: POLYMORPHISM WITH
FLEXIBLE TERMINAL REGIONS 49 3.3.4 PRP: REARRANGEMENTS TO MAINTAIN A
FIBRILLAR CORE REGION 51 3.3.5 YEAST PRIONS WITH
GLUTAMINE/ASPARAGINE-RICH PRION DOMAINS:
SUP35P, URE2P, A N D R N Q L P 52 3.3.6 FUNCTIONAL AMYLOID: THE YEAST
PRION HET-S 52 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
4.2.1 THE HISTORICAL USE O F X-RAY FIBER DIFFRACTION 65
4.2.2 THE HISTORICAL USE O F TRANSMISSION ELECTRON MICROSCOPY 67 4.3
METHODOLOGY 68
4.3.1 X-RAY FIBER DIFFRACTION 68
4.3.2 TRANSMISSION ELECTRON MICROSCOPY 72
4.4 RECENT ADVANCES IN AMYLOID STRUCTURE DETERMINATION 73 4.4.1 X-RAY
FIBER DIFFRACTION 73
4.4.2 TRANSMISSION ELECTRON MICROSCOPY 76
4.5 SUMMARY 78
ACKNOWLEDGMENTS 79 REFERENCES 79
5 STRUCTURES O F AGGREGATING SPECIES BY SMALL-ANGLE X-RAY SCATTERING 85
CRISTIANO L. P. OLIVEIRA AND JAN SKOV PEDERSEN 5.1 INTRODUCTION 85
5.2 THEORETICAL A N D EXPERIMENTAL ASPECTS 85
5.3 DATA ANALYSIS A N D MODELING METHODS 88
IMAGE 3
CONTENTS I X
5.4 STUDYING PROTEIN AGGREGATION AND FIBRILLATION USING SAXS 91
5.4.1 SOME GENERAL CONSIDERATIONS 91
5.4.2 SAXS STUDIES O F INSULIN, GLUCAGON, AND A-SYNUCLEIN 92 5.4.3
SDS-INDUCED AGGREGATION O F A-SYNUCLEIN 96 5.4.4 MULTI-COMPONENT FITTING
A N D ANALYSIS O F SAXS DATA 97
5.5 GENERAL STRATEGIES FOR MODELING SAXS DATA FROM PROTEIN COMPLEXES 98
5.6 SUMMARY A N D FINAL REMARKS 100
ACKNOWLEDGMENTS 101 REFERENCES 101
6 STRUCTURAL AND COMPOSITIONAL INFORMATION ABOUT PRE-AMYLOID OLIGOMERS
103 NIELS ZIJLSTRA AND VINOD SUBRAMANIAM 6.1 GENERAL INTRODUCTION 103
6.2 BIOPHYSICAL TECHNIQUES TO STUDY AMYLOID OLIGOMERS 104 6.2.1
FLUORESCENCE SPECTROSCOPY 104
6.2.1.1 ENSEMBLE SPECTROSCOPY 105 6.2.1.2 SINGLE-MOLECULE SPECTROSCOPY
105 6.2.2 ATOMIC FORCE MICROSCOPY 107
6.2.3 ABSORBANCE AND CIRCULAR DICHROISM SPECTROSCOPY 108 6.2.4
SMALL-ANGLE X-RAY SCATTERING 108 6.2.5 MASS SPECTROMETRY 109
6.3 THE STRUCTURE A N D COMPOSITION O F AMYLOID OLIGOMERS 109 6.3.1
A-SYNUCLEIN OLIGOMERS 109
6.3.1.1 MORPHOLOGY 110
6.3.1.2 OLIGOMER STRUCTURE 111
6.3.1.3 OLIGOMER COMPOSITION 113 6.3.2 AP PEPTIDE OLIGOMERS 115
6.3.2.1 MORPHOLOGY 115
6.3.2.2 COMPOSITION 116
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 O F EARLY AMYLOIDS 128 7.2.1
ANTIBODIES DEFINE DIFFERENT STRUCTURAL CLASSES O F OLIGOMERS A N D
FIBRILS 128 7.2.2 PROTEINS MAY FORM DIFFERENT KINDS O F OLIGOMERS WITH
DIFFERENT
STRUCTURAL A N D BIOLOGICAL ACTIVITIES 129 7.3 THE OLIGOMER-MEMBRANE
COMPLEX 131
7.3.1 THE EFFECT O F SURFACES O N PROTEIN MISFOLDING A N D AGGREGATION
131
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X I CONTENTS
7.3.2 THE MEMBRANE COMPOSITION AFFECTS BINDING A N D AGGREGATION
PROCESSES 132
7.3.3 COMPLEX ROLES O F CHOLESTEROL A N D GANGLIOSIDES I N OLIGOMER
CYTOTOXICITY 133 7.4 BIOCHEMICAL MODIFICATIONS UNDERLYING AMYLOID
TOXICITY 134 7.4.1 A NEW VIEW O F THE AMYLOID CASCADE HYPOTHESIS 134
7.4.2 AMYLOID PORES: A MECHANISM FOR CYTOTOXICITY? 135 7.4.3 OTHER
MECHANISMS FOR OLIGOMER CYTOTOXICITY 137 7.4.3.1 OXIDATIVE STRESS A N D
AMYLOID AGGREGATES 138 7.4.3.2 LIPID MODIFICATION A N D C A 2 + ENTRY
139 7.4.3.3 THE COMPLEXITY O F AMYLOID A N D OLIGOMER POLYMORPHISM 140
7.5 SUMMARY 141
REFERENCES 141
8 PATHWAYS O F AMYLOID FORMATION 151
FRANCESCO BEMPORAD AND FABRIZIO CHITI 8.1 INTRODUCTION 151
8.2 NOMENCLATURE O F THE VARIOUS CONFORMATIONAL STATES 152
8.3 GRAPHICAL REPRESENTATIONS O F THE MECHANISMS LEADING TO AMYLOID 153
8.3.1 TIME COURSE O F AMYLOID CONTENT 153
8.3.2 ENERGY LANDSCAPES O F AMYLOID FIBRIL FORMATION 155 8.3.3 REACTION
EQUILIBRIA INVOLVED I N AMYLOID FIBRIL FORMATION 157
8.4 PATHWAYS O F AMYLOID FIBRIL FORMATION 159
8.5 NUCLEATION GROWTH VERSUS NUCLEATED CONFORMATIONAL CONVERSION 161 8.6
SUMMARY 163
REFERENCES 163
9 SEQUENCE-BASED PREDICTION O F PROTEIN BEHAVIOR 167
GIAN GAETANO TARTAGLIA AND MICHELE VENDRUSCOLO 9.1 INTRODUCTION 167
9.2 THE STRATEGY O F THE ZYGGREGATOR PREDICTIONS 167
9.2.1 PREDICTION O F THE EFFECTS O F AMINO ACID SUBSTITUTIONS O N
PROTEIN AGGREGATION RATES 168 9.2.2 PREDICTION O F THE OVERALL
AGGREGATION RATES O F PEPTIDES A N D PROTEINS 170
9.2.3 PREDICTION O F AGGREGATION-PRONE REGIONS IN AMINO ACID SEQUENCES
171 9.3 AGGREGATION U N D E R OTHER CONDITIONS 173
9.3.1 PREDICTION O F PROTEIN AGGREGATION-PRONE REGIONS I N THE PRESENCE
O F DENATURANTS 173
IMAGE 5
CONTENTS I X I
9.3.2 PREDICTION O F AGGREGATION-PRONE REGIONS I N NATIVE STATES
O F PROTEINS 173
9.4 PREDICTION O F THE CELLULAR TOXICITY O F PROTEIN
AGGREGATES 174
9.5 RELATIONSHIP TO OTHER METHODS O F PREDICTING PROTEIN AGGREGATION
PROPENSITIES 175 9.6 COMPETITION BETWEEN FOLDING A N D AGGREGATION O F
PROTEINS 177 9.7 PREDICTION O F PROTEIN SOLUBILITY FROM THE COMPETITION
BETWEEN
FOLDING A N D AGGREGATION 177 9.7.1 SEQUENCE-BASED PREDICTION O F
PROTEIN SOLUBILITY 178 9.7.2 PREDICTION O F THE SOLUBILITY O F PROTEINS
BASED O N THEIR CELLULAR ABUNDANCE 178 9.8 SEQUENCE-BASED PREDICTION O F
PROTEIN INTERACTIONS WITH MOLECULAR
CHAPERONES 179
9.9 SUMMARY 179
REFERENCES 180
10 THE KINETICS AND MECHANISMS O F 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 O F NUCLEATED POLYMERIZATION 184 10.2.1 FROM
MICROSCOPIC PROCESSES TO A MASTER EQUATION 184 10.2.2 KINETIC EQUATIONS
FOR EXPERIMENTAL OBSERVABLES 187 10.2.3 CHARACTERISTICS O F OOSAWA-TYPE
GROWTH 189 10.2.3.1 NUDEATION
A N D GROWTH OCCUR SIMULTANEOUSLY 189 10.2.3.2 THE EARLY STAGES O F THE
REACTION TIME COURSE ARE DESCRIBED BY POLYNOMIAL GROWTH 189 10.2.3.3 T H
E LATE STAGES O F THE REACTION T I M E COURSE ARE DESCRIBED BY SIMPLE
FIRST-ORDER KINETICS 190 10.2.3.4 THE INTEGRATED RATE LAWS EXHIBIT
SCALING BEHAVIOR 191 10.2.4 GLOBAL ANALYSIS O F EXPERIMENTAL DATA USING
THE OOSAWA THEORY 192 10.3 THE THEORY O F FILAMENTOUS GROWTH WITH
SECONDARY PATHWAYS 193 10.3.1 EXTENDING THE OOSAWA FRAMEWORK TO INCLUDE
FRAGMENTATION
A N D SECONDARY NUCLEATION 193 10.3.2 EARLY TIME PERTURBATIVE SOLUTIONS
195 10.3.3 CHARACTERISTICS O F EXPONENTIAL-TYPE GROWTH 196 10.3.3.1 T H
E EARLY STAGES O F THE REACTION T I M E COURSE ARE
EXPONENTIAL 196
10.3.3.2 THE SOLUTION EXHIBITS SCALING BEHAVIOR 198 10.3.4 GLOBAL
ANALYSIS O F EXPERIMENTAL DATA USING LINEARIZED SOLUTIONS 198
IMAGE 6
X I I | CONTENTS
10.4 SELF-CONSISTENT SOLUTIONS FOR THE COMPLETE REACTION T I M E
COURSE 200
10.4.1 THE KEY PHENOMENOLOGICAL PARAMETERS DEPEND O N COMBINATIONS O F
THE MICROSCOPIC RATE CONSTANTS 202 10.4.2 REACTION TIME COURSE WITH
DEPLETED MONOMER CONCENTRATION 202 10.4.3 GLOBAL ANALYSIS O F AMYLOID
REACTION KINETICS USING SELF-CONSISTENT
SOLUTIONS 204
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.
NILSSON 11.1 INTRODUCTION 211
11.2 FLUORESCENCE SPECTROSCOPY FOR STUDIES O F AMYLOID REACTIONS IN
VITRO 212
11.2.1 FLUORESCENCE OUTPUT FORMATS 212
11.2.2 FLUORESCENCE ANISOTROPY 212
11.2.3 SINGLE MOLECULE DETECTION 214
11.2.4 CONFORMATIONAL PROBES 214
11.3 CYSTEINE-REACTIVE FLUORESCENT PROBES 214 11.3.1 ENVIRONMENTALLY
SENSITIVE PROBES - SPECTROCHROMIC STOKES SHIFT ASSAY 214 11.3.2
FLUORESCENCE ANISOTROPY PROBES FOR AMYLOID
OLIGOMERIZATION 216
11.3.3 PYRENE EXCIMER FORMATION PROBES FOR AMYLOID OLIGOMER A N D FIBRIL
TOPOLOGY 217 11.3.4 BIFUNCTIONAL CYSTEINE REAGENTS AS PROBES FOR AMYLOID
OLIGOMERS A N D FIBRILS 217
11.4 AMYLOIDOTROPIC PROBES FOR AMYLOID FIBRILS A N D OLIGOMERIC STATES
218
11.4.1 ARE THERE SELECTIVE PROBES FOR PREFIBRILLAR OLIGOMERIC STATES?
223 11.4.2 FLUORESCENCE ANISOTROPY O F SMALL MOLECULE PROBES FOR
CAPTURING THE INTERMEDIATE OLIGOMERIC STATE 224 11.4.3 IN VIVO
FLUORESCENT PROBES FOR AMYLOID FIBRILS 225
11.5 LUMINESCENT CONJUGATED POLY A N D OLIGOTHIOPHENES LCPS A N D LCOS
228 11.5.1 OPTICAL PROPERTIES O F CHEMICALLY DEFINED LCOS 228 11.5.2
BRIDGING THE IMAGING A N D SPECTROSCOPY GAP - MICROSPECTROSCOPY
O F IN VIVO FORMED AMYLOIDS 230 11.5.3 BRIDGING THE IMAGING A N D
SPECTROSCOPY GAP: MICROSPECTROSOPY A N D REAL TIME IMAGING O F AMYLOID
FORMATION 232 11.5.4 NEW NANOSCOPIC A N D MULTIFUNCTIONAL
FLUORESCENCE-BASED IMAGING
TECHNOLOGIES 234
IMAGE 7
CONTENTS | X I I I
11.5.5 LCOS FOR OPTICAL IN VIVO IMAGING O F PROTEIN AGGREGATES I N
TRANSGENIC
MOUSE MODELS 234
11.6 SUMMARY 236
ACKNOWLEDGMENTS 237 REFERENCES 239
12 ANIMAL MODELS O F 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 I N THE SYSTEMIC
AMYLOIDOSES 248 12.4 IDENTIFYING THE TOXIC SPECIES IN ALZHEIMER'S
DISEASE 250 12.5 INFECTIOUS PROTEIN MISFOLDING 252
12.5.1 BONA FIDE PRION DISEASE 254
12.5.2 PRION-LIKE DISEASES 254
12.6 CONCLUSIONS 256
REFERENCES 257
13 THE ROLE O F A(3 IN ALZHEIMER'S DISEASE 263
TIMOTHY M. RYAN, BLAINE R. ROBERTS, VICTOR A. STRELTSOV, STEWART D.
NUTTALL, AND COLIN L. MASTERS 13.1 HISTORY O F AMYLOIDOSIS 263
13.1.1 EARLY REPORTS O F AMYLOIDOSIS 263 13.1.2 ORIGINS O F MODERN
DEFINITION O F AMYLOID 264 13.2 BIOCHEMISTRY O F AP 264
13.2.1 IDENTIFICATION O F THE ALZHEIMER'S AMYLOID SUBUNIT 265 13.2.2 THE
PRODUCTION A N D PROCESSING O F THE A(3 PEPTIDE 267 13.3 AMYLOID FIBRILS
268
13.3.1 SYNTHETIC STRUCTURAL STUDIES 268
13.3.2 IN VIVO FIBRILLAR STRUCTURE 269
13.4 THE SOLUBLE OLIGOMER THEORY O F AD 269
13.4.1 THE DEVELOPMENT O F THE SOLUBLE OLIGOMER THEORY O F AD 269 13.4.2
SOLUBLE OLIGOMERS I N VIVO 270
13.4.3 RECOMBINANT SOLUBLE OLIGOMERS 271 13.4.4 SYNTHETIC A|S SOLUBLE
OLIGOMERS 271 13.5 OTHER FACTORS INVOLVED I N AMYLOID PLAQUE FORMATION
IN AD 274
13.5.1 INTERACTIONS WITH LIPIDS AND MEMBRANES 275 13.5.2 ELECTROSTATIC
MEMBRANE INTERACTIONS 275 13.5.3 INTEGRAL MEMBRANE INTERACTIONS 276
13.5.4 OTHER LIPID INTERACTIONS 277
13.5.5 APOLIPOPROTEIN INTERACTIONS 277
13.5.6 RECEPTOR INTERACTIONS 277
13.6 METAL IONS IN AD 278
IMAGE 8
X I V I CONTENTS
13.6.1 CU/AF} INTERACTIONS 278
13.6.2 ZN/AP INTERACTIONS 279
13.6.3 FE/AP INTERACTIONS 279
13.6.4 OTHER METALS INVOLVED IN AD 279
13.7 OTHER POTENTIAL AF5 INTERACTIONS 280
13.8 OTHER NEURODEGENERATIVE DISEASES 280
13.9 CONCLUSION 280
REFERENCES 281
14 EXPERIMENTAL APPROACHES TO INDUCING AMYLOID AGGREGATES 295 LISE GIEHM
AND DANIEL OTZEN 14.1 THE NEED FOR REPRODUCIBLE FIBRILLATION ASSAYS 295
14.2 SETTING U P A N ASSAY TO MONITOR FIBRILLATION 296
14.3 CONDITIONS THAT PROMOTE PROTEIN AGGREGATION 298 14.3.1 FORMATION O
F A N AGGREGATION-COMPETENT AMYLOIDOGENIC PRECURSOR 303 14.3.2 ASSEMBLY
O F AGGREGATION-PRONE COMPLEXES VIA ADDITIVES SUCH AS
SURFACTANTS OR LIPIDS 308 14.3.3 ABILITY TO RECRUIT NATIVE-LIKE MONOMERS
BY A N "INFECTIOUS" STATE 309
14.3.4 MINOR CONFORMATIONAL CHANGES I N A N ESSENTIALLY NATIVE-LIKE
PRECURSOR 311 14.3.5 PROMOTION O F ELONGATION A N D NUDEATION STEPS
THROUGH F RAGMENTATION 311 14.3.6 MISCELLANEOUS EFFECTS 312
14.4 PROCESSING A N D BATCH DIFFERENCES 312
14.5 TOWARD HIGH-THROUGHPUT ASSAYS 313
14.6 SUMMARY 314
REFERENCES 314
15 FIBRILLAR POLYMORPHISM 321
MARCUS FANDRICH, MELANIE WULFF, JESPER SENDERGAARD PEDERSEN, AND DANIEL
OTZEN 15.1 DETECTION O F F IBRILLAR POLYMORPHISM 321
15.2 THE STRUCTURAL DEFINITION O F FIBRIL POLYMORPHISM 322 15.2.1
INTER-SAMPLE POLYMORPHISM 322
15.2.2 INTRA-SAMPLE POLYMORPHISM 326 15.2.3 DEFORMATIONS FROM IDEAL
HELICAL SYMMETRY 326 15.3 THE TWO CLASSES O F FIBRIL POLYMORPHISM 328
15.3.1 PROTOFILAMENT ASSEMBLY POLYMORPHISMS: DIFFERENT ORIENTATIONS A N
D DIFFERENT NUMBERS O F PROTOFILAMENTS 328 15.3.1.1 DIFFERENT
ORIENTATION 328 15.3.1.2 DIFFERENT NUMBERS O F PROTOFILAMENTS 328
15.3.2 PROTOFILAMENT SUBSTRUCTURE POLYMORPHISMS A N D COMPOSITE FIBRIL
STRUCTURES 329
IMAGE 9
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.2 .3 .3.1 .3.2 .3.2. .3.3 .3.3. .3.4 .4 .5
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CONTENTS I X V
H O W DOES FIBRILLAR POLYMORPHISM ARISE? 332
THE INTERCONVERSION O F FIBRIL POLYMORPHS 334 THE BIOLOGICAL
IMPLICATIONS O F FIBRIL POLYMORPHISM 335 SUMMARY 337 ACKNOWLEDGMENTS 338
REFERENCES 338
INHIBITORS O F AMYLOID AND OLIGOMER FORMATION 345 NIKOLAI LORENZEN,
ERICH E. WANKER, AND DANIEL OTZEN INTRODUCTION: AMYLOIDOSES VERSUS
NEURODEGENERATIVE DISEASES 345 ANTIBODY-MEDIATED IMMUNOTHERAPY 346
ACTIVE IMMUNIZATION 346 PASSIVE IMMUNOTHERAPY 348 THE BLOOD BRAIN
BARRIER 349 NUCLEIC ACID-BASED AGENTS AGAINST PROTEIN AGGREGATES 349
INHIBITION O F AMYLOID FORMATION BY SMALL MOLECULES 350 STABILIZING T H
E NATIVE STATE 350 STRUCTURAL PROPERTIES O F FIBRILLATION INHIBITORS 350
UNSPECIFIC EFFECTS BY COLLOIDAL AGENTS 356
POLYPHENOLS: A POTENT CLASS O F AMYLOID INHIBITORS 357 EPIGALLOCATECHIN
GALLATE: THE UNIVERSAL AMYLOID-INHIBITOR? 357 PROMOTING FIBRILLATION TO
AVOID TOXIC OLIGOMERS 359 PEPTIDES A N D PEPTIDE MIMETICS 360
NANOPARTICLES: UNTAMED DRAGONS WITH FIRE POWER TO HEAL? 361 SUMMARY 362
REFERENCES 363
DEVELOPMENT O F THERAPEUTIC STRATEGIES FOR T H E TRANSTHYRETIN
AMYLOIDOSES 373 COLLEEN FEARNS, STEPHEN CONNELLY, EVAN T. POWERS, AND
JEFFERY W. KELLY
INTRODUCTION TO TRANSTHYRETIN STRUCTURE A N D FUNCTION 373 INTRODUCTION
TO AMYLOID DISEASES I N GENERAL 373 TRANSTHYRETIN AMYLOID DISEASES 375
CURRENT STRATEGIES TO TREAT H U M A N AMYLOID DISEASES 377 MECHANISM O F
TRANSTHYRETIN AMYLOIDOGENESIS 378
KINETIC STABILIZATION O F THE TRANSTHYRETIN TETRAMER AMELIORATES AMYLOID
DISEASE - GENETIC EVIDENCE 379 KINETIC STABILIZATION O F THE
TRANSTHYRETIN TETRAMER THROUGH SMALL-MOLECULE BINDING 381
BIVALENT KINETIC STABILIZERS 384 KINETIC STABILIZERS MUST BIND
SELECTIVELY TO TRANSTHYRETIN 385 ASSESSMENT O F DIFLUNISAL FOR TREATMENT
O F TRANSTHYRETIN AMYLOIDOSIS 385 TAFAMIDIS, THE FIRST APPROVED DRUG FOR
TREATMENT O F A TRANSTHYRETIN AMYLOIDOSIS 385
IMAGE 10
X V I | CONTENTS
Y I N SUMMARY 387
REFERENCES 387
18 HORMONE AMYLOIDS IN SICKNESS AND IN HEALTH 395
CAROTIN SEURING, NADEZHDA NESPOVITAYA, JONAS RUTISHAUSER, MARTIN SPIESS,
AND ROLAND RIEK 18.1 INTRODUCTION 395
18.2 CONSTITUTIVE VS. REGULATED SECRETORY PATHWAYS 395 18.3 SECRETORY
GRANULES CONTAIN AGGREGATED CARGO 396 18.3.1 SECRETORY PROTEIN SORTING A
N D GRANULE FORMATION 396 18.3.2 TRIGGERING THE FORMATION O F SECRETORY
GRANULES 398 18.3.3 TRIGGERING THE FORMATION O F SECRETORY GRANULES BY
GLYCOSAMINOGLYCANS (GAGS) 399 18.4 SECRETORY GRANULE AGGREGATION BY
FUNCTIONAL AMYLOID FORMATION 401 18.5 H O R M O N E AMYLOIDS I N
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 C O M M O N I N NATURE 412
19.3 IDENTIFICATION A N D CHARACTERIZATION O F FUNCTIONAL AMYLOIDS 413
19.4 FUNCTIONAL BACTERIAL AMYLOIDS PLAY MANY ROLES 415 19.4.1 BIOFILM
FORMATION A N D CELL CLUSTERING 415 19.4.2 BINDING TO EUKARYOTIC CELLS
416
19.4.3 OLIGOMERIC TOXINS 417
19.4.4 COATING O F SPORES A N D OTHER CELLS 417
19.5 BIOGENESIS A N D REGULATION O F FUNCTIONAL BACTERIAL AMYLOIDS 418
19.5.1 CURLI 418
19.5.2 FUNCTIONAL AMYLOIDS I N PSEUDOMONAS 418 19.5.3 CHAPLINS 420
19.5.4 HYDROPHOBINS 420
19.6 STRUCTURAL COMPOSITION O F FUNCTIONAL AMYLOIDS 421 19.6.1 CURLI:
FIVE REPEATING UNITS A N D ESSENTIAL GIN A N D ASN RESIDUES 421 19.6.2
FAPC LINKERS O F VARIABLE LENGTH: PSEUDOMONAS 423 19.6.3 CHAPLINS: GN
MOTIF AND CONSERVED CYS RESIDUES 423
19.6.4 HARPINS: SMALL A N D POLAR RESIDUES 425
19.7 ASSEMBLY PROPERTIES O F FUNCTIONAL AMYLOID I N VITRO 425 19.8
DIVERSITY A N D DISTRIBUTION O F FUNCTIONAL AMYLOID GENES 426 19.9
SUMMARY 431
ACKNOWLEDGMENTS 433 REFERENCES 433
IMAGE 11
CONTENTS | X V I I
20 STRUCTURAL PROPERTIES AND APPLICATIONS O F SELF-ASSEMBLING
PEPTIDES 439 ZHONGLI LUO AND SHUGUANG ZHANG 20.1 INTRODUCTION TO
SELF-ASSEMBLING PEPTIDES 439 20.2 THE PRINCIPLES O F SELF-ASSEMBLING
PEPTIDES 439 20.2.1 DESIGN PRINCIPLE FOR SELF-ASSEMBLING PEPTIDES 439
20.2.2 CONFORMATIONAL CHANGES UNDERGONE BY SELF-ASSEMBLING
PEPTIDES 441
20.2.2.1 EFFECT O F TEMPERATURE 441 20.2.2.2 EFFECT O F P H 442
20.2.2.3 EFFECT O F AMINO ACID SEQUENCE 442 20.3 SELF-ASSEMBLING PEPTIDE
NANOFIBERS 443 20.3.1 T H E NANOFIBER STRUCTURES O F THE PEPTIDE
SCAFFOLD 443 20.3.2 THE PROCESS O F PEPTIDE SCAFFOLD FORMATION 444
20.3.3 A PROPOSED MODEL FOR THE PROCESS O F NANOFIBER FORMATION 445 20.4
DIVERSE APPLICATIONS O F SELF-ASSEMBLING PEPTIDE NANOFIBERS
SCAFFOLDS 446
20.4.1 THREE-DIMENSIONAL TISSUE CELL CULTURES 446 20.4.2 CELL A N D
TISSUE ENGINEERING 448
20.4.3 CONTROLLED DRUG DELIVERY A N D REGENERATIVE MEDICINE 450 20.4.4 T
R A U M A EMERGENCY 451
20.5 SUMMARY 451
ACKNOWLEDGMENTS 452 REFERENCES 452
21 HARNESSING T H E SELF-ASSEMBLING PROPERTIES O F PROTEINS IN SPIDER
SILK AND LUNG SURFACTANT 455 J A N JOHANSSON 21.1 INTRODUCTION 455
21.2 AMINO ACID SEQUENCES A N D AMYLOID FORMATION 455 21.3 SPIDER SILK A
N D H O W THE SPIDERS MAKE IT 458
21.4 HARNESSING THE PROPERTIES O F SPIDER SILK A N D ITS CONSTITUENT
PROTEINS 461
21.5 BIOSYNTHESIS O F A N A-HELIX FROM O N E O F THE MOST P-PRONE
SEQUENCES KNOWN 462
21.6 ANTI-AMYLOID PROPERTIES O F THE BRICHOS DOMAIN 464 21.7 SUMMARY 465
ACKNOWLEDGMENTS 465 REFERENCES 466
INDEX 471 |
| any_adam_object | 1 |
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| dewey-full | 540 572.67 |
| dewey-hundreds | 500 - Natural sciences and mathematics |
| dewey-ones | 540 - Chemistry and allied sciences 572 - Biochemistry |
| dewey-raw | 540 572.67 |
| dewey-search | 540 572.67 |
| dewey-sort | 3540 |
| dewey-tens | 540 - Chemistry and allied sciences 570 - Biology |
| discipline | Chemie / Pharmazie Biologie Medizin |
| format | Book |
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| id | DE-604.BV041021942 |
| illustrated | Illustrated |
| indexdate | 2024-08-03T00:39:41Z |
| institution | BVB |
| isbn | 9783527332007 |
| language | English |
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| physical | XXVIII, 481 S. Ill., graph. Darst. 24 cm x 17 cm |
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| spelling | Amyloid fibrils and prefibrillar aggregates molecular and biological properties ed. by Daniel Erik Otzen Weinheim Wiley-VCH 2013 XXVIII, 481 S. Ill., graph. Darst. 24 cm x 17 cm txt rdacontent n rdamedia nc rdacarrier Fibrille (DE-588)4154296-4 gnd rswk-swf Amyloid (DE-588)4129431-2 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content Amyloid (DE-588)4129431-2 s Fibrille (DE-588)4154296-4 s DE-604 Otzen, Daniel Erik 1969- (DE-588)1032522585 edt X:MVB text/html http://deposit.dnb.de/cgi-bin/dokserv?id=4071687&prov=M&dok%5Fvar=1&dok%5Fext=htm Inhaltstext V:DE-576;X:wiley image/jpeg http://swbplus.bsz-bw.de/bsz378965557cov.htm Cover DNB Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=025999504&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Amyloid fibrils and prefibrillar aggregates molecular and biological properties Fibrille (DE-588)4154296-4 gnd Amyloid (DE-588)4129431-2 gnd |
| subject_GND | (DE-588)4154296-4 (DE-588)4129431-2 (DE-588)4143413-4 |
| title | Amyloid fibrils and prefibrillar aggregates molecular and biological properties |
| title_auth | Amyloid fibrils and prefibrillar aggregates molecular and biological properties |
| title_exact_search | Amyloid fibrils and prefibrillar aggregates molecular and biological properties |
| title_full | Amyloid fibrils and prefibrillar aggregates molecular and biological properties ed. by Daniel Erik Otzen |
| title_fullStr | Amyloid fibrils and prefibrillar aggregates molecular and biological properties ed. by Daniel Erik Otzen |
| title_full_unstemmed | Amyloid fibrils and prefibrillar aggregates molecular and biological properties ed. by Daniel Erik Otzen |
| title_short | Amyloid fibrils and prefibrillar aggregates |
| title_sort | amyloid fibrils and prefibrillar aggregates molecular and biological properties |
| title_sub | molecular and biological properties |
| topic | Fibrille (DE-588)4154296-4 gnd Amyloid (DE-588)4129431-2 gnd |
| topic_facet | Fibrille Amyloid Aufsatzsammlung |
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