Smith Biological Adhesives

2. Auflage 2016
ISBN: 978-3-319-46082-6
Verlag: Springer Nature Switzerland
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, 380 Seiten

Many creatures use adhesive polymers and structures to attach to inert substrates, to each other, or to other organisms. This is the first major review that brings together research on many of the well-known biological adhesives dealing with bacteria, fungi, algae, and marine and terrestrial animals. As we learn more about their molecular and mechanical properties we begin to understand why they adhere so well and with this comes broad applications in areas such as medicine, dentistry, and biotechnology.

Andrew M. Smith Professor Ithaca College Department of Biology
Specialty: Animal Physiology, Biomechanics Phone  [phone] E-mail: [e-mail] Office: 155 Ctr for Natural Sciences Ithaca, NY 14850

Autoren/Hrsg.

Smith, Andrew M.

Inhaltsverzeichnis

1;Preface;5
2;Contents;7
3;Chapter 1: Adhesive Bacterial Exopolysaccharides;9
3.1;1.1 Introduction;9
3.2;1.2 Characterization of Bacterial Exopolysaccharide Adhesins;10
3.2.1;1.2.1 Polysaccharide Purification;10
3.2.2;1.2.2 Polymer Length;12
3.2.3;1.2.3 Monosaccharide Composition;13
3.2.4;1.2.4 Alternative Composition Analysis Methods;13
3.2.5;1.2.5 Linkage Analysis;14
3.2.6;1.2.6 Tertiary Structural Analysis;14
3.3;1.3 Polysaccharide Biosynthesis Pathways;15
3.3.1;1.3.1 Wzx/Wzy-Dependent Pathway;15
3.3.2;1.3.2 ABC Transporter-Dependent Pathway;16
3.3.3;1.3.3 Synthase-Dependent Pathway;17
3.4;1.4 Adhesive Exopolysaccharides;17
3.4.1;1.4.1 Pel Polysaccharide (PEL);17
3.4.1.1;1.4.1.1 PEL Biosynthesis Pathway;18
3.4.1.2;1.4.1.2 Modifications;18
3.4.1.3;1.4.1.3 Interactions and Functions;19
3.4.2;1.4.2 Psl Polysaccharide;19
3.4.2.1;1.4.2.1 PSL Biosynthetic Pathway;20
3.4.2.2;1.4.2.2 Interactions and Functions;21
3.4.3;1.4.3 PNAG;21
3.4.3.1;1.4.3.1 Biosynthesis;22
3.4.3.2;1.4.3.2 Modification;23
3.4.3.3;1.4.3.3 Interactions and Functions;24
3.4.4;1.4.4 Holdfast;24
3.4.4.1;1.4.4.1 Biosynthesis;25
3.4.4.2;1.4.4.2 Modification;25
3.4.4.3;1.4.4.3 Interactions and Functions;26
3.5;1.5 Exopolysaccharide Adhesives in Infection;27
3.6;1.6 Conclusion;27
3.7;References;28
4;Chapter 2: Adhesion and Adhesives of Fungi and Oomycetes;33
4.1;2.1 Introduction;34
4.2;2.2 Prevalence and Importance of Adhesion in Fungi and Oomycetes;34
4.2.1;2.2.1 Adhesion as Part of Many Stages of Morphogenesis in Many Fungi;35
4.2.2;2.2.2 Functions of Adhesion;36
4.2.3;2.2.3 Selected Examples of Adhesiveness as a Part of a Developmental Sequence;38
4.2.3.1;2.2.3.1 Colletotrichum graminicola, Causal Agent of Anthracnose on Corn;38
4.2.3.2;2.2.3.2 Blumeria graminis f. sp. hordei and f. sp. tritici, Causal Agent of Powdery Mildew of Barley and Wheat, Respectively;39
4.2.3.3;2.2.3.3 Magnaporthe oryzae, Causal Agent of Rice Blast;39
4.3;2.3 Challenges in Identifying Adhesives in Fungi;40
4.3.1;2.3.1 Genetic ``Knockout,´´ ``Knockin,´´ and Overexpression Strategies;40
4.3.2;2.3.2 Biochemical Strategies;42
4.4;2.4 Fungal and Oomycete Glues;43
4.4.1;2.4.1 Features;43
4.4.2;2.4.2 Postulated Composition of Glues;43
4.4.3;2.4.3 Secretion and Cross-Linking, with a Focus on Transglutaminases;45
4.4.4;2.4.4 Cell Surface Macromolecules with Apparent Adhesive Properties;45
4.4.4.1;2.4.4.1 PcVsv1, a Protein on Encysting Zoospores of Phytophthora cinnamomi;45
4.4.4.2;2.4.4.2 90-kDa Mannoprotein on Macroconidia of Nectria haematococca (Anamorph Fusarium solani f. sp. cucurbitae);47
4.4.4.3;2.4.4.3 Hydrophobins: The Mannoprotein SC3, a Schizophyllum commune Hydrophobin; the Class I Hydrophobin BcHpb1 of Botrytis ci...;49
4.4.4.4;2.4.4.4 MAD1 and MAD2 (Metarhizium Adhesion-Like Proteins) in the Entomopathic Fungus Metarhizium anisopliae;50
4.4.4.5;2.4.4.5 Selected Glycosylphosphatidylinositol-Dependent (GPI) Cell Wall Proteins;51
4.5;2.5 Fungal Adhesins;53
4.6;2.6 Conclusions;54
4.7;References;54
5;Chapter 3: Diatom Adhesives: Molecular and Mechanical Properties;64
5.1;3.1 Diatoms and Adhesion;65
5.1.1;3.1.1 Diatom Morphology;65
5.1.2;3.1.2 Significance of Diatom Adhesion;65
5.1.3;3.1.3 Diatom Adhesion Strategies;67
5.1.4;3.1.4 General Composition of Diatom Mucilages;67
5.2;3.2 Adhesion and Gliding of Raphid Diatoms;68
5.2.1;3.2.1 Adhesion and Gliding Behavior;68
5.2.2;3.2.2 Mechanism of Raphid Diatom Adhesion and Gliding;69
5.2.3;3.2.3 Fine Structure of Raphid Diatom Mucilages;70
5.2.3.1;3.2.3.1 Cell Surface Mucilage;71
5.2.3.2;3.2.3.2 Raphe Mucilage;72
5.2.3.3;3.2.3.3 Secreted Trails;74
5.2.4;3.2.4 Nanomechanical Properties Determined by AFM and QCM-D;76
5.2.4.1;3.2.4.1 AFM;76
5.2.4.1.1;Cell Surface Mucilage;76
5.2.4.1.2;Raphe Adhesives;77
5.2.4.2;3.2.4.2 QCM-D;78
5.2.5;3.2.5 Molecular Composition;79
5.2.5.1;3.2.5.1 Craspedostauros australis;79
5.2.5.2;3.2.5.2 Pinnularia viridis;80
5.2.5.3;3.2.5.3 Amphora coffeaeformis;81
5.2.5.4;3.2.5.4 Phaeodactylum tricornutum;82
5.3;3.3 Sessile Adhesion;83
5.3.1;3.3.1 Physical Properties of Adhesive Pads with AFM;83
5.3.1.1;3.3.1.1 Toxarium undulatum;83
5.3.1.2;3.3.1.2 Eunotia sudetica;85
5.3.2;3.3.2 Molecular Composition and Chemical Properties of Stalks: Achnanthes longipes;85
5.3.2.1;3.3.2.1 Stalk Formation;85
5.3.2.2;3.3.2.2 Composition and Properties;86
5.4;3.4 Concluding Remarks;88
5.5;References;89
6;Chapter 4: Progress in the Study of Adhesion by Marine Invertebrate Larvae;94
6.1;4.1 Introduction;95
6.2;4.2 In Situ Imaging for Morphological and Compositional Studies of Larval Adhesives;96
6.3;4.3 In Situ Spectroscopic Investigations of Larval Adhesive Secretions;100
6.4;4.4 Quantifying the Interaction of Naturally Secreted Adhesives with Surfaces;103
6.5;4.5 Measuring Surface Adsorption of Purified Larval Adhesive Proteins;105
6.6;4.6 Micromechanical Measurement of Adhesion Force in Larval Adhesives;107
6.7;4.7 Conclusions;108
6.8;References;109
7;Chapter 5: The Adhesive Tape-Like Silk of Aquatic Caddisworms;113
7.1;5.1 Introduction;113
7.2;5.2 Multi-scale Structure of Casemaker Caddisworm Silk;115
7.3;5.3 The Peripheral Adhesive Coating;117
7.3.1;5.3.1 Composition of the Silk Coating;117
7.3.2;5.3.2 Enzyme-Catalyzed Cross-Linking in the Peripheral Coating;117
7.3.3;5.3.3 Interfacial Adhesion Mechanisms;118
7.4;5.4 The Tough Fibrous Silk Core;120
7.4.1;5.4.1 Composition of the Silk Core;120
7.4.2;5.4.2 H-Fibroin Structure;120
7.5;5.5 Mechanical Properties of Caddisworm Silk;124
7.5.1;5.5.1 Mechanically Probing Caddisworm Silk Structure;124
7.5.2;5.5.2 A Mechanical Model of Caddisworm Silk;126
7.6;5.6 The Silk Spinning System;129
7.6.1;5.6.1 Silk Gland Anatomy;129
7.6.2;5.6.2 Fiber Formation in the Anterior Silk Gland;131
7.7;References;132
8;Chapter 6: Interfacial Phenomena in Marine and Freshwater Mussel Adhesion;135
8.1;6.1 Introduction;136
8.2;6.2 Recent Advances in Understanding Freshwater Mussel Adhesion;139
8.2.1;6.2.1 Structure and Composition of the Adhesive Interface;139
8.2.2;6.2.2 Characterization of Zebra and Quagga Mussel Byssal Proteins;143
8.3;6.3 Redox Chemistry at the Adhesive Interface;145
8.3.1;6.3.1 Control of pH During Protein Secretion;146
8.3.2;6.3.2 Antioxidant Proteins at the Plaque-Substratum Interface;148
8.3.3;6.3.3 Dopaquinone Tautomers;148
8.4;6.4 The Effect of Surface Chemistry and Mode of Dopa Interaction;150
8.5;6.5 The Role of Amino Acids Other than Dopa in Adhesion;152
8.6;6.6 Concluding Remarks;153
8.7;References;154
9;Chapter 7: Barnacle Underwater Attachment;158
9.1;7.1 Introduction;158
9.2;7.2 Barnacle Attachment;159
9.2.1;7.2.1 A Unique Sessile Crustacean;159
9.2.2;7.2.2 Attachment in the Life Cycle and Biosynthesis/Secretion of the Cement;160
9.3;7.3 Barnacle Underwater Cement;163
9.3.1;7.3.1 Adhesive Layer of the Cement;163
9.3.2;7.3.2 Authentic Sample of the Cement;164
9.3.3;7.3.3 Cement Nature;165
9.3.4;7.3.4 Multifunctionality in Underwater Attachment;166
9.3.5;7.3.5 Cement Proteins and Possible Functions;167
9.3.5.1;7.3.5.1 CP-100k and CP-52k;167
9.3.5.2;7.3.5.2 CP-68k;168
9.3.5.3;7.3.5.3 CP-20k;169
9.3.5.4;7.3.5.4 CP-19k;171
9.3.5.5;7.3.5.5 CP-16k;171
9.3.6;7.3.6 Possible Molecular Model for Barnacle Underwater Attachment;172
9.4;7.4 Comparison with Other Holdfasts and Proteins;173
9.5;7.5 Impacts to Material Science;176
9.6;7.6 Concluding Remarks;177
9.7;References;178
10;Chapter 8: The Biochemistry and Mechanics of Gastropod Adhesive Gels;182
10.1;8.1 Introduction;182
10.2;8.2 Adhesive Gels Used by Different Animals;183
10.3;8.3 Principles of Gel Mechanics;186
10.4;8.4 Adhesive Gel Structure;189
10.5;8.5 Cross-Linking and the Mechanics of Adhesive Gels: Stiffness and Double Networks;191
10.6;8.6 Protein Functions in the Glue;193
10.7;8.7 Comparison of Gel Structure Among Gastropods;194
10.8;8.8 Conclusion;195
10.9;References;196
11;Chapter 9: Adhesive Secretions in Echinoderms: A Review;198
11.1;9.1 Introduction;199
11.2;9.2 Tube Feet;199
11.2.1;9.2.1 Morphology and Adhesion Strength;199
11.2.2;9.2.2 Histology and Ultrastructure;201
11.2.3;9.2.3 Fine Structure and Composition of the Adhesive Material;205
11.2.3.1;9.2.3.1 Protein Fraction;207
11.2.3.1.1;Adhesive Proteins;208
11.2.3.1.2;De-adhesive Proteins;211
11.2.3.2;9.2.3.2 Carbohydrate Fraction;212
11.3;9.3 Cuvierian Tubules;212
11.3.1;9.3.1 Fine Structure and Adhesion Strength;213
11.3.2;9.3.2 Ultrastructure and Composition of the Adhesive Material;214
11.4;9.4 Comparisons Between Echinoderm Adhesives and with Other Marine Bioadhesives;219
11.5;References;224
12;Chapter 10: An Adhesive Secreted by Australian Frogs of the Genus Notaden;228
12.1;10.1 Introduction;229
12.2;10.2 Preliminary Field and Laboratory Data;230
12.3;10.3 Adhesive Collection;231
12.4;10.4 Solubilisation and Solidification;232
12.5;10.5 Mechanical Properties;233
12.6;10.6 Biocompatibility;234
12.7;10.7 Biochemical Studies;236
12.7.1;10.7.1 Colour;237
12.7.2;10.7.2 CD Spectra;237
12.7.3;10.7.3 Amino Acid Analysis;238
12.7.4;10.7.4 Protein Fractionation;239
12.8;10.8 Comparative Studies;240
12.9;10.9 Applications;242
12.10;10.10 Conclusions;245
12.11;References;246
13;Chapter 11: Properties, Principles, and Parameters of the Gecko Adhesive System;249
13.1;11.1 Introduction;249
13.2;11.2 Adhesive Properties of Gecko Setae;251
13.2.1;11.2.1 Properties (1) and (2): Anisotropic Attachment and High Adhesion Coefficient (mu);252
13.2.1.1;11.2.1.1 Large Safety Factor for Adhesion and Friction?;252
13.2.2;11.2.2 Property (3): Low Detachment Force;254
13.2.3;11.2.3 Integration of Body and Leg Dynamics with Setal Attachment and Detachment;255
13.2.4;11.2.4 Molecular Mechanism of Gecko Adhesion;256
13.2.4.1;11.2.4.1 Unsupported Mechanisms: Glue, Suction, Electrostatics, Microinterlocking, and Friction;256
13.2.4.2;11.2.4.2 Potential Intermolecular Mechanisms: Van der Waals and Capillary Forces;257
13.2.4.3;11.2.4.3 Contact Angle Estimates of Surface Energy;258
13.2.5;11.2.5 Property (4): Material-Independent Adhesion;258
13.2.5.1;11.2.5.1 Testing the van der Waals and Capillary Adhesion Hypotheses;258
13.2.5.2;11.2.5.2 The Role of Water in Gecko Adhesion;259
13.2.5.3;11.2.5.3 Dominance of Geometry in VdW Interactions;260
13.2.5.4;11.2.5.4 JKR Model of Spatulae;261
13.2.5.5;11.2.5.5 Kendall Peel Model of Spatulae;262
13.2.6;11.2.6 Property (5): Rate-Dependent Adhesion;263
13.3;11.3 Antiadhesive Properties of Gecko Setae;263
13.3.1;11.3.1 Properties (6) and (7): Self-Cleaning and Anti-Self-Adhesion;264
13.3.2;11.3.2 Property (8): Nonsticky Default State;266
13.4;11.4 Modeling Adhesive Nanostructures;267
13.4.1;11.4.1 Effective Modulus of a Setal Array;267
13.4.2;11.4.2 Rough Surface and Antimatting Conditions;269
13.5;11.5 Scaling;270
13.5.1;11.5.1 Scaling of Pad Area and Spatular Size;270
13.5.2;11.5.2 Scaling of Stress;271
13.6;11.6 Comparison of Conventional and Gecko Adhesives;271
13.7;11.7 Gecko-Inspired Synthetic Adhesive Nanostructures;274
13.8;11.8 Future Directions in the Study of the Gecko Adhesive System;275
13.9;References;277
14;Chapter 12: Adhesive Secretions in Harvestmen (Arachnida: Opiliones);285
14.1;12.1 Introduction;285
14.2;12.2 Types of Adhesive Secretions and Their Distribution Among Harvestmen;286
14.3;12.3 Glandular Setae in Palpatores;288
14.4;12.4 Pedipalpal Adhesives in Laniatores Nymphs;295
14.5;12.5 Soil Camouflage;297
14.6;12.6 Egg Coatings and Spermatophores;299
14.7;12.7 Conclusion;301
14.8;References;302
15;Chapter 13: Unraveling the Design Principles of Black Widow´s Gumfoot Glue;306
15.1;13.1 Introduction;306
15.2;13.2 Gumfoot Glue;309
15.2.1;13.2.1 Secretion Mechanism;309
15.2.2;13.2.2 Material Properties;309
15.2.2.1;13.2.2.1 Viscoelasticity;309
15.2.2.2;13.2.2.2 Chemical Composition;310
15.2.2.2.1;Hygroscopic Salts;310
15.2.2.2.2;Water-Soluble Peptides;311
15.2.2.2.3;Glycoproteins;312
15.2.2.2.4;Lipids;312
15.2.3;13.2.3 Humidity-Mediated Adhesion;313
15.2.4;13.2.4 Molecular Mechanism of Adhesion;315
15.2.4.1;13.2.4.1 Detecting Gumfoot Glue Peaks;315
15.2.4.2;13.2.4.2 Effect of Salts on the Humidification of Glue Proteins;316
15.2.4.3;13.2.4.3 Effect of Humidity on Salt Mobility;317
15.2.4.4;13.2.4.4 Implications of Molecular-Level Findings Toward Macro-Level Adhesion;318
15.2.5;13.2.5 Summary;319
15.3;References;319
16;Chapter 14: High-Strength Adhesive Exuded from the Adventitious Roots of English Ivy;323
16.1;14.1 Introduction;323
16.2;14.2 Uniqueness and Importance of the Bioadhesive Derived from English Ivy;325
16.2.1;14.2.1 Hierarchical Attachment Strategies of English Ivy;326
16.2.2;14.2.2 Spherical Nanoparticles Observed in the Ivy-Derived Adhesive;326
16.2.3;14.2.3 Monitoring the Secretion of the Nanocomposite-Rich Adhesive in Real Time;328
16.3;14.3 Identification of the Chemical Constituents of the Spheroidal Nanoparticles;329
16.3.1;14.3.1 Massive Harvest of the Purified Ivy Nanoparticles;329
16.3.2;14.3.2 Physicochemical Characterization;330
16.3.3;14.3.3 Glycoprotein Nature of the Ivy Nanoparticles;331
16.4;14.4 Molecular Basis for the Ivy-Derived Adhesive;335
16.4.1;14.4.1 Preferable Surface Wetting Favored by the Ivy Nanoparticles;335
16.4.2;14.4.2 Chemical Components Within the Ivy-Derived Adhesive;336
16.4.3;14.4.3 Calcium-Driven Cross-Linking;338
16.4.4;14.4.4 Putative Model of the Ivy-Derived Bioadhesive;339
16.5;14.5 Adhesion Strength;340
16.5.1;14.5.1 Adhesion Force of the Ivy-derived Adhesive Characterized by AFM;340
16.5.2;14.5.2 Adhesion Strength of the Ivy-Mimetic Adhesive Composites;340
16.6;14.6 Conclusions and Future Prospects;341
16.7;References;342
17;Chapter 15: Biomimetic Adhesives and Coatings Based on Mussel Adhesive Proteins;347
17.1;15.1 Introduction;347
17.2;15.2 Mussel Adhesive Proteins and DOPA;348
17.3;15.3 Catechol Chemistry;349
17.3.1;15.3.1 Reversible Interactions;350
17.3.2;15.3.2 Oxidization-Induced Covalent Interactions;351
17.3.3;15.3.3 ROS Generation During Catechol Oxidization;352
17.3.4;15.3.4 Chemical Modification to Catechol;352
17.4;15.4 Mussel-Inspired Adhesive Polymers;353
17.4.1;15.4.1 Extraction and Expression of MAPs;353
17.4.2;15.4.2 Synthetic Mussel-Inspired Polymer Adhesive;355
17.5;15.5 Mussel-Inspired Material Surface Functionalization;358
17.5.1;15.5.1 Antifouling Coating Mediated by Catechol-Interface Interactions;358
17.5.2;15.5.2 Polydopamine Coating;361
17.6;15.6 Advanced Material Design Based on Catechol Chemistry;363
17.6.1;15.6.1 Gecko- and Mussel-Inspired Hybrid Adhesive;363
17.6.2;15.6.2 Nanocomposite Adhesive Hydrogel;364
17.6.3;15.6.3 Drug Delivery;365
17.6.4;15.6.4 Hydrogel Actuator;366
17.6.5;15.6.5 Self-Healing Hydrogel;367
17.7;15.7 Summary and Future Outlook;369
17.8;References;369