Parry / Squire Fibrous Proteins: Structures and Mechanisms

1. Auflage 2017
ISBN: 978-3-319-49674-0
Verlag: Springer International Publishing
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, Band 82, 630 Seiten

Reihe: Subcellular Biochemistry

This book provides the readers with an up-to-date review of the design, structure and function of a representative selection of fibrous proteins in both health and disease. The importance of the a-helical coiled coil, a conformational motif based on the heptad repeat in the amino acid sequence of all a-fibrous proteins (and parts of some globular proteins) is underlined by three Chapters devoted to its design, structure, function and topology.  Specific proteins covered in the text and which depend on the coiled coil for their structure and function, include the intermediate filament proteins, tropomyosin, myosin, paramyosin, fibrin and members of the spectrin superfamily. Also described are fibrous proteins based on the ß-pleated sheet and collagen conformations. Recombinant structural proteins, especially of silk and collagen, are discussed in the context of developing new biomaterials with varied applications. Established researchers and postgraduate students in the fields of protein chemistry, biochemistry and structural biophysics will find Fibrous Proteins: Structures and Mechanisms to be an invaluable collection of topical reviews that describe the basic advances made in the field of fibrous proteins over the past decade. This book, written by recognized authorities in the field, provides a clear account of the current status of fibrous protein research and, in addition, establishes the basis for deciding the most appropriate directions for future activity, including the applications of protein engineering and the commercial exploitation of new biomaterials.

Autoren/Hrsg.

Parry, David A. D.

Squire, John M.

Inhaltsverzeichnis

1;Preface;6
2;Contents;8
3;Chapter 1: Fibrous Protein Structures: Hierarchy, History and Heroes;10
3.1;1.1 Introduction: Early History and Key Players;12
3.1.1;1.1.1 Simplicity and Complexity in Amino Acids;12
3.1.2;1.1.2 The ?-Helix;14
3.1.3;1.1.3 The Coiled Coil and Heptads;19
3.1.4;1.1.4 Features of the Heptad;22
3.1.5;1.1.5 Multi-stranded Coiled-Coils;22
3.1.6;1.1.6 Stutters, Stammers and Coiled Coils with Specific Discontinuities;26
3.2;1.2 Beta Structures;26
3.3;1.3 The Collagen Fold;30
3.4;1.4 Assembly of Building Blocks;31
3.4.1;1.4.1 Globular Proteins;31
3.4.2;1.4.2 Packing of Coiled Coils;33
3.4.3;1.4.3 Assembly of ?-Sheets;34
3.4.4;1.4.4 Collagen Fibrils;36
3.5;1.5 New Approaches to Solving Fibrous Protein Structures;37
3.6;1.6 The Future: Protein Engineering;39
3.7;References;39
4;Chapter 2: Coiled-Coil Design: Updated and Upgraded;43
4.1;2.1 Scope of This Review;44
4.2;2.2 The Basics of Coiled-Coil Sequence and Structure;45
4.3;2.3 Computational Tools for Analysing Coiled-Coil Sequences and Structures;46
4.4;2.4 Straightforward Rules for Coiled-Coil Prediction and Design;48
4.5;2.5 A Heptad of Completely de novo Helical Assemblies;50
4.5.1;2.5.1 Rationally Designed Dimers, Trimers and Tetramers;50
4.5.2;2.5.2 Expanding de novo Coiled Coils Past Tetramer;51
4.5.3;2.5.3 Structural Rationale for Higher-Order Oligomerization;53
4.6;2.6 Parametric and Computational Coiled-Coil Design;55
4.6.1;2.6.1 Background: Computational Methods Old and New;55
4.6.2;2.6.2 Parametric Coiled-Coil Designs Achieved to Date;56
4.7;2.7 Improving Heterospecificity in Coiled-Coil Design;57
4.8;2.8 Adding Antiparallel Coiled Coils to the Mix;59
4.9;2.9 Building with Coiled-Coil Modules: Protein Origami, Synthetic Biology and Materials;59
4.10;2.10 Concluding Remarks;62
4.11;References;63
5;Chapter 3: Functional and Structural Roles of Coiled Coils;70
5.1;3.1 The Basic Architecture of Coiled Coils;71
5.2;3.2 Classical Roles of Coiled Coils;73
5.2.1;3.2.1 Filament-Forming Coiled-Coil Proteins;73
5.2.2;3.2.2 From Static Oligomerization to Dynamic Molecular Recognition;75
5.2.3;3.2.3 Intra-chain Coiled Coils;77
5.3;3.3 Molecular Spacers – Dynamic and Resilient;78
5.3.1;3.3.1 The Complex Nature of Trimeric Autotransporter Adhesins;78
5.3.2;3.3.2 Polar Core Residues – Between Specificity, Stability, and Foldability;80
5.3.3;3.3.3 Resilience Towards Insertions and Deletions – Boosting Evolvability;82
5.4;3.4 Non-specific Molecular Recognition;84
5.4.1;3.4.1 Molecular Recognition in Protein Folding and Disaggregation;85
5.4.2;3.4.2 Molecular Recognition in Protein Unfolding and Degradation;86
5.5;3.5 Coiled Coils in Signal Transduction;87
5.5.1;3.5.1 Basic Architecture and Signal Propagation in Histidine Kinases;89
5.5.2;3.5.2 Signal Propagation Through HAMP Domains;90
5.5.3;3.5.3 The Role of Asymmetry;92
5.6;3.6 Concluding Remarks;93
5.7;References;94
6;Chapter 4: The Structure and Topology of ?-Helical Coiled Coils;101
6.1;4.1 Introduction;102
6.2;4.2 Structural Parameters;105
6.2.1;4.2.1 The Standard Model;105
6.2.2;4.2.2 Prediction and Analysis Programs;106
6.2.3;4.2.3 Coiled Coils with Variant Core Geometry;108
6.2.4;4.2.4 Non-heptad Coiled Coils;110
6.3;4.3 Structural Determinants of Folding and Stability;117
6.3.1;4.3.1 Number and Orientation of Helices;117
6.3.2;4.3.2 Folding and Stability;120
6.4;4.4 Structural Diversity;123
6.4.1;4.4.1 Fibres and Zippers;123
6.4.2;4.4.2 Tubes, Sheets, Spirals, and Rings;127
6.5;4.5 Evolution and Phylogenetic Diversity;128
6.6;References;131
7;Chapter 5: Structural Transition of Trichocyte Keratin Intermediate Filaments During Development in the Hair Follicle;136
7.1;5.1 Introduction;137
7.2;5.2 Axial Structure of the IF;141
7.2.1;5.2.1 X-Ray Diffraction;141
7.2.2;5.2.2 Crosslinking;141
7.3;5.3 Lateral Structure of the IF;147
7.4;5.4 Radial Projection and Surface Lattice of Trichocyte IF;148
7.5;5.5 Summary;151
7.6;References;151
8;Chapter 6: Crystallographic Studies of Intermediate Filament Proteins;155
8.1;6.1 Introduction;156
8.2;6.2 Primary Structure of IF Proteins;159
8.3;6.3 Experimental Studies of the Elementary Dimer;162
8.4;6.4 Crystallographic Challenges of Coiled-Coil Fragments;165
8.5;6.5 Elementary Dimer Structure;167
8.6;6.6 Conclusions and Outlook;170
8.7;References;171
9;Chapter 7: Lessons from Animal Models of Cytoplasmic Intermediate Filament Proteins;175
9.1;7.1 Introduction;177
9.2;7.2 Analysis of Keratins;179
9.2.1;7.2.1 Simple Epithelial Keratins;180
9.2.1.1;7.2.1.1 Expression and Architectural Functions of Simple Epithelial Keratins;180
9.2.1.2;7.2.1.2 Scaffolding and Regulatory Functions of Simple Epithelial Keratins;183
9.2.2;7.2.2 Epidermal Keratins;189
9.2.2.1;7.2.2.1 Expression and Architectural Functions of Epidermal Keratins;189
9.2.2.1.1;Analysis of K5, K14 and K15 in the Basal Epidermis;189
9.2.2.1.2;Analysis of Suprabasal Epidermal Keratins;190
9.2.2.1.3;Analysis of Keratins Expressed in Corneal Epithelia;191
9.2.2.2;7.2.2.2 Regulatory Functions of Epidermal Keratins;191
9.2.2.2.1;Deletion of the Entire Keratin Protein Family;194
9.3;7.3 Analysis of Type III Intermediate Filament Proteins;195
9.3.1;7.3.1 Vimentin;195
9.3.2;7.3.2 Desmin;201
9.3.3;7.3.3 GFAP;203
9.3.4;7.3.4 Syncoilin and peripherin;205
9.4;7.4 Analysis of Type IV Intermediate Filaments;205
9.4.1;7.4.1 Neuronal Type IV IFs;205
9.4.2;7.4.2 Synemin;211
9.4.3;7.4.3 Nestin;212
9.5;7.5 Type VI Intermediate Filaments;213
9.5.1;7.5.1 Filensin (BFSP1) and Phakinin (BFSP2);213
9.6;7.6 Caenorhabditis elegans cytoplasmic IFs;213
9.7;7.7 Conclusion;216
9.8;References;217
10;Chapter 8: Filamentous Structure of Hard ?-Keratins in the Epidermal Appendages of Birds and Reptiles;235
10.1;8.1 Introduction;236
10.2;8.2 Sequence Similarities and Differences;239
10.2.1;8.2.1 Filament-Forming Central Domain;239
10.2.2;8.2.2 N-Terminal Domain;243
10.2.3;8.2.3 C-Terminal Domain;244
10.3;8.3 Information on the Molecular Structure Derived from X-Ray Diffraction Studies;245
10.4;8.4 Further Modelling of the Structure of the Filament;246
10.5;8.5 Packing of Filaments in Sheets in Feather Keratin;249
10.6;8.6 Physical Properties of ?-Keratins and Their Relationship to Sequence Characteristics;250
10.6.1;8.6.1 Highly Charged Cysteine-Rich Segments;251
10.6.2;8.6.2 Glycine-Tyrosine-Rich Segments;251
10.6.3;8.6.3 Glycine-Rich Segments;252
10.7;8.7 Summary;252
10.8;References;254
11;Chapter 9: Tropomyosin Structure, Function, and Interactions: A Dynamic Regulator;257
11.1;9.1 Introduction;258
11.2;9.2 The Structure of Tropomyosin;260
11.2.1;9.2.1 Alanine Clusters;262
11.2.2;9.2.2 Bends and Holes in Core Packing;264
11.2.3;9.2.3 The Overlap Complex;264
11.2.4;9.2.4 Tropomyosin Dynamics and Transmission of Structural Information;265
11.3;9.3 How Does Tropomyosin Bind to Actin? A Design for Weak and Dynamic Binding to the Actin Filament;267
11.3.1;9.3.1 What Constitutes an Actin Binding Site on Tropomyosin?;269
11.3.2;9.3.2 How Does Tropomyosin Assemble on the Actin Filament?;271
11.4;9.4 Regulation of the Actin-Myosin Interaction;272
11.4.1;9.4.1 Common Features of Regulation;275
11.4.2;9.4.2 Specific Regulation;275
11.5;9.5 Four Tropomyosin Genes, Many Isoforms and Diverse Binding Partners;276
11.5.1;9.5.1 Exon 9 Encodes Isoform-Specific Function;278
11.5.2;9.5.2 Complexes Between Tropomyosin and Tropomodulin;279
11.6;9.6 Conclusions;280
11.7;References;281
12;Chapter 10: Titin and Nebulin in Thick and Thin Filament Length Regulation;289
12.1;10.1 Introduction;290
12.2;10.2 Titin and Nebulin – The ‘‘Molecular Ruler’’ Hypotheses;292
12.2.1;10.2.1 Titin;293
12.2.2;10.2.2 Nebulin;293
12.2.3;10.2.3 The Ruler Hypotheses;295
12.3;10.3 Titin/Nebulin in Thick/Thin Filament Assembly During Sarcomerogenesis;295
12.3.1;10.3.1 Electron Microscopy;296
12.3.2;10.3.2 Immunofluorescent Microscopy;296
12.3.3;10.3.3 Relevance to the Titin/Nebulin Ruler-Template Hypotheses;297
12.4;10.4 Thick Filament Assembly with Absent/Truncated Titin/Nebulin;298
12.4.1;10.4.1 Titin Truncations;298
12.4.2;10.4.2 Nebulin Truncations;299
12.5;10.5 Thick and Thin Filament Length Control – Possible Involved Factors;300
12.5.1;10.5.1 Tropomodulin;300
12.5.2;10.5.2 N-RAP;300
12.5.3;10.5.3 Chaperones;301
12.5.4;10.5.4 Contractile Activity;302
12.6;10.6 Thick and Thin Filaments Length Control in Striated Muscles of Invertebrates (Indirect Flight Muscles of Drosophila);304
12.7;10.7 Size Regulation in Non-muscle Biological Structures;306
12.8;10.8 Conclusion;308
12.9;References;309
13;Chapter 11: Myosin and Actin Filaments in Muscle: Structures and Interactions;323
13.1;11.1 Introduction and Overview of the Sarcomere;324
13.2;11.2 Actin Filament Structure;330
13.2.1;11.2.1 3D Reconstruction of Actin Filaments;330
13.2.2;11.2.2 Checking the Steric Blocking Model;330
13.2.3;11.2.3 X-Ray Crystallography of Actin and Myosin;331
13.2.4;11.2.4 Recent High Resolution Thin Filament Helical Reconstructions;333
13.2.5;11.2.5 Finding Troponin – Single Particle Analysis;335
13.2.6;11.2.6 The Thin Filament Regulation Mechanism;340
13.2.7;11.2.7 Nebulin;340
13.3;11.3 Myosin Filament Structure;343
13.3.1;11.3.1 Myosin Filament Symmetries;343
13.3.2;11.3.2 Myosin Head Organisation;345
13.3.3;11.3.3 Myosin Filaments in Vertebrate Striated Muscles: MyBP-C and Titin;351
13.3.4;11.3.4 Myosin Filaments in Vertebrate Striated Muscles: The Myosin Head Array;353
13.3.5;11.3.5 Myosin Filaments in Insect Flight Muscle;355
13.3.6;11.3.6 The Myosin Filament Backbone;358
13.3.7;11.3.7 The Vertebrate Myosin Filament Bare Zone;361
13.3.8;11.3.8 Paramyosin Filaments;362
13.3.9;11.3.9 Myosin Filaments in Vertebrate Smooth Muscles;364
13.3.10;11.3.10 Nematode and Limulus Muscles;366
13.4;11.4 Future Prospects;367
13.5;11.5 Late Breaking Results;368
13.6;References;368
14;Chapter 12: Dystrophin and Spectrin, Two Highly Dissimilar Sisters of the Same Family;376
14.1;12.1 Introduction;377
14.2;12.2 Dystrophin, Utrophin and Spectrin Structural Domains;378
14.2.1;12.2.1 Common Features of Dystrophin and Spectrin;381
14.2.1.1;12.2.1.1 Classical ABD Domains at the N-terminal End of Dystrophin, Utrophin and ?-spectrin;381
14.2.1.2;12.2.1.2 Central Domains are Composed of Repeats with Similar Folds in Triple Helical Coiled-Coils;383
14.2.1.3;12.2.1.3 EF Domains at the C-Terminal End of Dystrophin, Utrophin and ?-spectrin;384
14.2.2;12.2.2 Dystrophin and Spectrin Structural Dissimilarities;385
14.3;12.3 The Scaffolding Function of Dystrophin and Spectrins: Binding to Phospholipids and Organizing Protein-­Protein Assemblies;387
14.3.1;12.3.1 Dystrophin and Spectrin: Two Coiled-Coil Filaments Interacting with Membrane Lipids;387
14.3.2;12.3.2 Examples of Protein Partners of Dystrophin and Spectrin;390
14.4;12.4 Dystrophin and Spectrin Mutations Related to Pathologies;393
14.5;12.5 Conclusion;397
14.6;References;398
15;Chapter 13: Fibrin Formation, Structure and Properties;407
15.1;13.1 Introduction;409
15.2;13.2 Biochemistry of Fibrinogen, the Precursor to Fibrin;410
15.2.1;13.2.1 Biosynthesis of Fibrinogen in Hepatocytes;410
15.2.2;13.2.2 Fibrinogen Metabolism;411
15.2.3;13.2.3 Polypeptide Chain Composition of Fibrin(ogen);412
15.2.4;13.2.4 Overall Structure of Fibrinogen Molecules;414
15.2.5;13.2.5 Domain Structure of Fibrinogen;414
15.2.6;13.2.6 ?-Helical Coiled-Coils of Fibrinogen;415
15.2.7;13.2.7 Ca2+-Binding Sites in Fibrinogen;416
15.2.8;13.2.8 Carbohydrate Moieties of Fibrinogen;417
15.3;13.3 Molecular Mechanisms of the Conversion of Fibrinogen to Fibrin;417
15.3.1;13.3.1 General Remarks;417
15.3.2;13.3.2 Enzymatic Release of Fibrinopeptides from Fibrinogen;419
15.3.3;13.3.3 ‘A-a’ Knob-Hole Interactions in Fibrin;419
15.3.4;13.3.4 Fibrin Oligomers and Protofibrils;421
15.3.5;13.3.5 Lateral Aggregation of Protofibrils;422
15.3.6;13.3.6 Role of ‘B-b’ Knob-Hole Interactions;423
15.3.7;13.3.7 The Role of the ?C Regions in Fibrin Formation;424
15.3.8;13.3.8 Fibrin Branching and Network Architecture;425
15.3.9;13.3.9 Fibrin Structure and the Gelation Point;425
15.3.10;13.3.10 Factor XIIIa-Catalyzed Covalent Crosslinking of Fibrin;426
15.4;13.4 Variations and Modulation of Fibrin(ogen) Structure and Properties;427
15.4.1;13.4.1 Genetic Polymorphisms of Fibrinogen;427
15.4.2;13.4.2 Post-translational Modifications and Heterogeneity of Fibrinogen;428
15.4.3;13.4.3 Hereditary Fibrinogen Defects (Dysfibrinogenemias, Afibrinogenemia, and Hypofibrinogenemia);429
15.4.4;13.4.4 Environmental Conditions of Fibrin Formation;430
15.4.5;13.4.5 Fibrin Formation Under Hydrodynamic Flow;433
15.5;13.5 Fibrin Mechanical Properties and Their Structural Origins;433
15.5.1;13.5.1 General Remarks;433
15.5.2;13.5.2 Viscoelastic Properties of Fibrin;434
15.5.3;13.5.3 Non-linear Elasticity and High Extensibility of Fibrin;434
15.5.4;13.5.4 Multiscale Structural Mechanics of Fibrin Clots;436
15.5.5;13.5.5 Molecular Structural Origins of Fibrin Mechanical Properties;437
15.5.6;13.5.6 Fibrin as a Biomaterial;439
15.6;13.6 Lytic Stability of Fibrin;440
15.6.1;13.6.1 Molecular Mechanisms of Fibrinolysis;440
15.6.2;13.6.2 Modulators of Fibrinolysis;442
15.6.3;13.6.3 Internal and External Fibrinolysis;443
15.7;13.7 Conclusions;443
15.8;References;444
16;Chapter 14: Fibrillar Collagens;459
16.1;14.1 Introduction;460
16.2;14.2 Fibrillar and Non-fibrillar Collagens;461
16.3;14.3 Fibrillar Collagen Genes and Polypeptide Chains;461
16.4;14.4 Domain Structures of Fibrillar Collagen Chains;465
16.5;14.5 Molecular Structure and Stability of the Collagen Triple Helix;467
16.5.1;14.5.1 Overall Chain Conformation and Hydrogen Bonding;468
16.5.2;14.5.2 4-Hydroxyproline and Collagen Stability;469
16.5.3;14.5.3 Additional Mechanisms of Collagen Stabilization;471
16.5.4;14.5.4 Helical Twist of the Collagen Triple Helix;471
16.6;14.6 Chain Register in the Collagen Triple Helix;472
16.7;14.7 Fibrillar Collagen Biosynthesis;473
16.7.1;14.7.1 Role of 3-Hydroxyproline in Fibrillar Collagens;473
16.7.2;14.7.2 Collagen Chaperones;475
16.7.3;14.7.3 Fibrillar Procollagen C-Propeptide Trimer;476
16.7.4;14.7.4 Proteolytic Processing of Procollagen;477
16.8;14.8 Fibril Assembly;479
16.9;14.9 Fibril Structure;479
16.10;14.10 Fibril Cross-Linking and Degradation;481
16.11;14.11 Interactions of Fibrillar Collagens: Nucleators, Regulators and Organizers;482
16.11.1;14.11.1 Collagen Types V/XI Nucleate Heterotypic D-Period Collagen Fibrils;482
16.11.2;14.11.2 Collagen Fibril Regulators on the Fibril Surface;483
16.11.3;14.11.3 Collagen Cell-Surface Receptors;484
16.12;14.12 Concluding Remarks;485
16.13;References;485
17;Chapter 15: Recombinant Structural Proteins and Their Use in Future Materials;493
17.1;15.1 Introduction;494
17.2;15.2 Natural Protein Polymeric Materials: Lessons from Biology;495
17.2.1;15.2.1 Information in Structural Proteins;495
17.2.2;15.2.2 Elastin and Resilin;496
17.2.3;15.2.3 Spider Dragline, Silkworm Cocoon and Some Insect Silks;497
17.2.4;15.2.4 Collagen;497
17.2.5;15.2.5 Hair, Wool, and Some Insect Silks;498
17.3;15.3 Addition of Information into Structural Proteins;499
17.3.1;15.3.1 Examples of Designed Information-Containing Recombinant Proteins;502
17.3.2;15.3.2 Constraints Limiting Rational Design of Recombinant Structural Proteins;504
17.3.2.1;15.3.2.1 Tolerance to Addition of Information;504
17.3.2.2;15.3.2.2 Absence of a Precise Amino Acid Sequence-Structure Relationship;505
17.3.2.3;15.3.2.3 Our Understanding of Amino Acid Sequence-Structure-Function Relationship;505
17.4;15.4 Commercial Scale Production of Protein Polymers;506
17.4.1;15.4.1 Protein Production Platforms for High Level Expression;507
17.4.2;15.4.2 Downstream Processing Considerations;509
17.5;15.5 Formation of Proteins into Materials;509
17.5.1;15.5.1 Processing;510
17.5.1.1;15.5.1.1 Wet Spinning;510
17.5.1.2;15.5.1.2 Electrospinning;512
17.5.1.3;15.5.1.3 Casting of Films, Gels and Sponges;513
17.5.1.4;15.5.1.4 Spraying and Phase Separation;514
17.5.2;15.5.2 Cross-Linking;515
17.5.2.1;15.5.2.1 Reaction of Chemical Groups;515
17.5.2.2;15.5.2.2 Self-Assembly;516
17.6;15.6 Silk Proteins Studied in Our Laboratory;516
17.7;15.7 Conclusions;519
17.8;References;520
18;Chapter 16: Properties of Engineered and Fabricated Silks;529
18.1;16.1 Introduction;530
18.2;16.2 Biotechnological Production of Silk;533
18.2.1;16.2.1 Examples of Biotechnologically Produced Silk Proteins: Honey Bee Silk;536
18.2.1.1;16.2.1.1 Natural Honey Bee Silk;536
18.2.1.2;16.2.1.2 Recombinant Honey Bee Silk Production;538
18.2.2;16.2.2 Examples of Biotechnologically Produced Silk Proteins: Lacewing Silk;539
18.2.2.1;16.2.2.1 Natural Lacewing Silk;539
18.2.2.2;16.2.2.2 Recombinant Lacewing Silk;540
18.2.3;16.2.3 Examples of Biotechnologically Produced Silk Proteins: Caddisfly Silk;541
18.2.3.1;16.2.3.1 Natural Caddisfly Silk;541
18.2.3.2;16.2.3.2 Recombinant Caddisfly Silk;543
18.2.4;16.2.4 Examples of Biotechnologically Produced Silk Proteins: Silkworm Silk;544
18.2.4.1;16.2.4.1 Natural Silkworm Silk;544
18.2.4.2;16.2.4.2 Recombinant Silkworm Silk;545
18.2.5;16.2.5 Examples of Biotechnologically Produced Silk Proteins: Spider Silk;546
18.2.5.1;16.2.5.1 Natural Spider Silk;546
18.2.5.2;16.2.5.2 Recombinant Spider Silk;548
18.3;16.3 Processing and Properties of Silk Proteins;551
18.3.1;16.3.1 Fibers and Nonwoven Mats;552
18.3.2;16.3.2 Particles and Capsules;557
18.3.3;16.3.3 Hydrogels, Foams and Sponges;559
18.3.4;16.3.4 Films and Coatings;562
18.4;16.4 Conclusion and Outlook;564
18.5;References;565
19;Chapter 17: Biomaterials Made from Coiled-Coil Peptides;576
19.1;17.1 Introduction: The Emerging Role of Biomaterials;577
19.2;17.2 Coiled-Coil Therapeutics;579
19.3;17.3 Coiled-Coil Hydrogels;581
19.4;17.4 Immunogenic Coiled-Coil Assemblies;587
19.5;17.5 Coiled-Coil Based Nanotubes, Fibrils, and Fibres;588
19.6;17.6 Coiled-Coil Composites;595
19.7;17.7 Conclusion;597
19.8;References;597
20;Chapter 18: Bioengineered Collagens;602
20.1;18.1 Introduction;603
20.2;18.2 Background: Collagens;604
20.3;18.3 Recombinant Collagens and Expression Systems;606
20.4;18.4 Recombinant Collagens with Repeating Triple-Helix Segments;610
20.5;18.5 Recombinant Collagens: Binding to Cell Receptors and ECM Proteins;612
20.6;18.6 Recombinant Collagens: MMPs and Collagen Degradation;615
20.7;18.7 Recombinant Collagen Fusion Proteins;616
20.8;18.8 Applications for Designed Recombinant Collagens;617
20.8.1;18.8.1 Applications of Recombinant Animal Collagens;619
20.8.2;18.8.2 Applications of Bacterial Collagens;621
20.9;18.9 Summary and Future Directions;623
20.10;References;623