Biophysical and Chemical Properties of Collagen: Biomedical Applications in Tissue Engineering

PRELIMS.pdf
Preface
Acknowledgments
Author biographies
John A M Ramshaw
Veronica Glattauer
Abbreviations
Disclaimer
CH001.pdf
Chapter 1 Introduction
1.1 Overview
References
CH002.pdf
Chapter 2 The structure of collagen
2.1 Composition
2.2 X-ray diffraction studies
2.2.1 Fibre diffraction
2.2.2 Peptide diffraction
2.2.3 Hydrogen bonding
2.2.4 Hydration
2.2.5 The role of hydroxyproline
2.3 Different collagen types
2.4 Other proteins with a triple-helix
2.4.1 Animal proteins
2.4.2 Bacterial collagens
2.5 Protein sequences
References
CH003.pdf
Chapter 3 Biosynthesis and biodegradation of collagen
3.1 Biosynthetic pathway
3.2 Selected secondary modification enzymes in collagen biosynthesis
3.2.1 Prolyl hydroxylase
3.2.2 Lysyl hydroxylase
3.2.3 Lysyl oxidase
3.3 Degradation of collagen in tissues
References
CH004.pdf
Chapter 4 Collagen assemblies
4.1 Ordered collagen structures
4.1.1 Interstitial collagen fibrils
4.1.2 Other ordered structures for interstitial collagens
4.1.3 Ordered structures for other collagen types
4.2 Fibrillogenesis
4.2.1 Interstitial collagen fibril formation
4.2.2 Regulation of collagen fibril formation
4.2.3 Heterotypic collagen fibrils
4.2.4 Interstitial collagen fibril growth
4.2.5 Crimp in collagen fibrils
References
CH005.pdf
Chapter 5 Tissue arrangement
5.1 Formation of new tissue
5.2 Native crosslinking
5.2.1 Enzyme-initiated crosslinking
5.2.2 Non-enzymatic crosslinking
5.3 Examples of tissue structure
5.3.1 Tissue organisation in tendon and ligament
5.3.2 Tissue organisation in cornea
5.3.3 Tissue organisation in skin
5.3.4 Tissue organisation in other tissues
5.4 Mineralisation
5.5 Mechanical properties
5.5.1 Soft tissues
5.5.2 The effect of mineralisation
References
CH006.pdf
Chapter 6 Collagen stability
6.1 Molecular stability
6.1.1 Individual soluble collagen molecule stability
6.1.2 Tissue collagen stability
6.2 Solvent effects on stability
6.3 Peptide models to study stability
6.3.1 Polypeptide models
6.3.2 Defined peptide models
6.3.3 Effects of solvents on peptide models
6.4 Other uses for peptide models
6.4.1 Synthetic peptide model designs
References
CH007.pdf
Chapter 7 Interactions
7.1 Describing interactions with other molecules
7.1.1 Collagen network plots
7.1.2 Collagen interactome maps
7.2 Interactions with other collagens
7.3 Interactions with proteoglycans
7.3.1 Heparin and heparan sulfate glycan chains
7.3.2 Interactions with other proteoglycans
7.4 Interaction with globular proteins
7.4.1 Signalling molecules
7.4.2 Protease sites
7.4.3 Other interaction sites
7.5 Interactions with the immune system
7.5.1 Responses to collagen-based products
7.6 Antibodies to collagens as biochemical reagents
7.6.1 Polyclonal antibodies
7.6.2 Monoclonal antibodies
7.6.3 Defining epitopes
References
CH008.pdf
Chapter 8 Production of tissue-derived collagens
8.1 Tissue and fibrous collagen
8.2 Acellular matrix
8.3 Soluble collagens
8.3.1 Extraction of soluble collagen
8.3.2 Extraction of acid soluble collagen
8.3.3 Neutral salt soluble collagen
8.3.4 Increasing soluble collagen yield
8.3.5 Extraction of soluble collagen by tissue digestion
8.3.6 Sources for specific collagen types
8.4 Production of collagen in cell culture
8.5 Fractionation of soluble collagens
8.6 Further purification of soluble collagens
8.6.1 Ion exchange chromatography
8.6.2 Gel permeation chromatography
8.6.3 Affinity chromatography
8.6.4 Other approaches
References
CH009.pdf
Chapter 9 Production of recombinant collagens
9.1 Recombinant animal collagen production
9.1.1 Bacterial expression
9.1.2 Animal cell expression
9.1.3 Yeast expression
9.1.4 Transgenic expression
9.1.5 Purification and quality
9.2 Recombinant bacterial collagen production
9.3 Recombinant ‘bioengineered’ adaptations to collagen structures
9.3.1 Adaptations to animal collagens
9.3.2 Adaptations to bacterial collagens
9.4 Recombinant chimeric fusion proteins
9.5 De novo designed structures
References
CH010.pdf
Chapter 10 Evaluation of the quality of collagen preparations
10.1 Collagen quantitation
10.2 Solution properties
10.3 Electrophoretic methods
10.4 Optical methods
10.4.1 UV and visible spectroscopy
10.4.2 IR spectroscopy
10.4.3 CD and ORD spectroscopy
10.4.4 Microscopy
10.4.5 Refractive index
10.5 Biophysical methods
10.5.1 Calorimetry
10.5.2 Other methods
References
CH011.pdf
Chapter 11 Fabrication of biomedical products
11.1 Gels and hydrogels
11.2 Foams and sponges
11.2.1 Foams
11.2.2 Sponges
11.2.3 Measurement of pore size and porosity
11.3 Reconstituted fibres
11.3.1 Wet spinning
11.3.2 Electrospinning
11.3.3 Printing
11.4 Films and membranes
11.5 Beads and particles
11.5.1 Using purified, soluble collagen
11.5.2 Using collagen fibre dispersions
11.5.3 Using collagen tissue
11.6 Fibrous capsule materials
11.6.1 Biosynthetic materials
11.7 Other technologies
11.7.1 Ionic liquids
11.7.2 Alignment technologies
11.8 Sterilisation
11.8.1 Physical approaches including irradiation
11.8.2 Chemical and other approaches
11.8.3 Bovine spongiform encephalopathy
References
CH012.pdf
Chapter 12 Chemical modifications
12.1 Chemical crosslinking methods
12.1.1 Aldehyde-based crosslinks
12.1.2 Other crosslink approaches
12.1.3 Introducing zero-length crosslinks
12.2 Physical crosslinking
12.2.1 Direct, non-catalysed reactions
12.2.2 Catalysed reactions
12.3 Assessing the effectiveness of crosslinking
12.3.1 Physical methods
12.3.2 Chemical and biological methods
12.4 Site-specific chemical modifications
12.4.1 Additional reactions with amino groups
12.4.2 Reactions with other functional groups
References
CH013.pdf
Chapter 13 Applications for intact tissue collagen
13.1 Stabilised tissues
13.1.1 Intestine
13.1.2 Amnion
13.1.3 Pericardium
13.1.4 Heart valve
13.1.5 Issues with calcification of tissue-based devices
13.1.6 Other tissues
13.2 Acellular matrix
References
CH014.pdf
Chapter 14 Applications for purified collagen
14.1 Gels and hydrogels
14.1.1 Tissue augmentation
14.1.2 Dermal repair
14.1.3 Ophthalmic uses
14.1.4 Other uses of gels
14.1.5 Hydrogels
14.2 Foams and sponges
14.2.1 Dermal wound repair
14.2.2 Haemostats
14.2.3 Orthopaedic applications
14.2.4 Other applications
14.3 Films and membranes
14.3.1 Periodontal treatment
14.3.2 Adhesion control
14.3.3 Nerve repair
14.3.4 Other examples
14.4 Beads and particles
14.5 Reconstituted fibres
References
CH015.pdf
Chapter 15 Applications of biosynthetic materials
15.1 Vascular devices
15.1.1 Background technologies
15.1.2 Biosynthetic vascular device
15.1.3 Explant analyses
15.2 Hernia, ligament and other options
References
CH016.pdf
Chapter 16 Collagen applications in tissue engineering and regenerative medicine
16.1 Fabricated collagen as a supporting structure
16.1.1 Musculoskeletal and associated tissues
16.1.2 Cardiovascular tissues
16.1.3 Other tissues
16.2 ACM as a supporting structure
16.2.1 Bladder and urologic tissues
16.2.2 Other tissues
16.2.3 Organ replacements
References
CH017.pdf
Chapter 17 Coating of biomedical materials with collagen
17.1 Coating of synthetic polymers
17.1.1 Plasma modification prior to collagen coating
17.1.2 Chemical modification of surfaces
17.1.3 Layer-by-layer coating
17.2 Collagen on metals and inorganic materials
17.2.1 Metallic surfaces
17.2.2 Ceramic surfaces
References
CH018.pdf
Chapter 18 Composites of collagen with other materials
18.1 Composites with other biopolymers
18.1.1 Proteins
18.1.2 Carbohydrates
18.2 Composites with synthetic polymers
18.2.1 Hydrogel and related composites
18.2.2 Two phase systems
18.3 Composites with inorganic materials
18.3.1 Hydroxyapatite and calcium phosphate phases
18.3.2 Other inorganic materials
18.4 Composites with bioactive entities
18.4.1 Growth factors
18.4.2 Delivery of drugs, including antibiotics
References
CH019.pdf
Chapter 19 Concluding remarks
References