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| 050 | 4 | _aR857.M3 R367 2019 | |
| 082 | 0 | _a610.28 | |
| 100 | 1 | _aRamshaw, John A. M. | |
| 245 | 1 | 0 |
_aBiophysical and Chemical Properties of Collagen : _bBiomedical Applications. |
| 250 | _a1st ed. | ||
| 264 | 1 |
_aBristol : _bInstitute of Physics Publishing, _c2019. |
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| 264 | 4 | _c©2020. | |
| 300 | _a1 online resource (346 pages) | ||
| 336 |
_atext _btxt _2rdacontent |
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| 337 |
_acomputer _bc _2rdamedia |
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| 338 |
_aonline resource _bcr _2rdacarrier |
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| 490 | 1 | _aBiophysical Society-IOP Series | |
| 505 | 0 | _aIntro -- Preface -- Acknowledgments -- Author biographies -- John A M Ramshaw -- Veronica Glattauer -- Abbreviations -- Disclaimer -- Chapter 1 Introduction -- 1.1 Overview -- References -- 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 -- 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 -- 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 -- 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 -- Chapter 6 Collagen stability. | |
| 505 | 8 | _a6.1 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 -- 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 -- 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 -- Chapter 9 Production of recombinant collagens -- 9.1 Recombinant animal collagen production. | |
| 505 | 8 | _a9.1.1 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 -- 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 -- 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 -- 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. | |
| 505 | 8 | _a12.2.1 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 -- 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 -- 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 -- 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 -- 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 -- Chapter 17 Coating of biomedical materials with collagen. | |
| 505 | 8 | _a17.1 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 -- 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 -- Chapter 19 Concluding remarks -- References. | |
| 520 | _aBiophysical and Chemical Properties of Collagen: Biomedical Applications provides an introduction to the biophysics and chemistry of collagen and its use as a biomedical material in the rapidly changing fields of biomedical device production, tissue engineering and regenerative medicine. Written by experts in the field, this text will be of interest for researchers as well as lecturers and students. | ||
| 588 | _aDescription based on publisher supplied metadata and other sources. | ||
| 590 | _aElectronic reproduction. Ann Arbor, Michigan : ProQuest Ebook Central, 2024. Available via World Wide Web. Access may be limited to ProQuest Ebook Central affiliated libraries. | ||
| 650 | 0 | _aBiomedical materials. | |
| 655 | 4 | _aElectronic books. | |
| 700 | 1 | _aGlattauer, Veronica. | |
| 776 | 0 | 8 |
_iPrint version: _aRamshaw, John A. M. _tBiophysical and Chemical Properties of Collagen: Biomedical Applications _dBristol : Institute of Physics Publishing,c2019 _z9780750320979 |
| 797 | 2 | _aProQuest (Firm) | |
| 830 | 0 | _aBiophysical Society-IOP Series | |
| 856 | 4 | 0 |
_uhttps://ebookcentral.proquest.com/lib/orpp/detail.action?docID=31252900 _zClick to View |
| 999 |
_c36755 _d36755 |
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