請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/67857
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 楊台鴻(Tai-Horng Young) | |
dc.contributor.author | Yi-Chia Chen | en |
dc.contributor.author | 陳邑佳 | zh_TW |
dc.date.accessioned | 2021-06-17T01:54:08Z | - |
dc.date.available | 2022-08-01 | |
dc.date.copyright | 2017-08-01 | |
dc.date.issued | 2017 | |
dc.date.submitted | 2017-07-23 | |
dc.identifier.citation | 1. Rabinowitz, Y.S., Keratoconus. Survey of Ophthalmology, 1998. 42(4): p. 297-319.
2. Gokhale, N.S., Epidemiology of keratoconus. Indian Journal of Ophthalmology, 2013. 61(8): p. 382-383. 3. Mikami, T., et al., Interleukin 1 beta promoter polymorphism is associated with keratoconus in a Japanese population. Molecular Vision, 2013. 19: p. 845-851. 4. Meek, K.M. and C. Knupp, Corneal structure and transparency. Progress in Retinal and Eye Research, 2015. 49: p. 1-16. 5. Ruberti, J.W., A.S. Roy, and C.J. Roberts, Corneal structure and function. Annu Rev Biomed Eng, 2011. 13: p. 269-295. 6. DelMonte, D.W. and T. Kim, Anatomy and physiology of the cornea. Journal of Cataract & Refractive Surgery, 2011. 37(3): p. 588-598. 7. Seiler, T., et al., Does Bowman's layer determine the biomechanical properties of the cornea? (1042-962X (Print)). 8. Eghrari, A.O., S.A. Riazuddin, and J.D. Gottsch, Chapter Two - Overview of the Cornea: Structure, Function, and Development, in Progress in Molecular Biology and Translational Science, J.F. Hejtmancik and M.N. John, Editors. 2015, Academic Press. p. 7-23. 9. Anderson, K., A. El-Sheikh, and T. Newson, Application of structural analysis to the mechanical behaviour of the cornea. Journal of the Royal Society Interface, 2004. 1(1): p. 3-15. 10. Snedeker, J.G. and A. Gautieri, The role of collagen crosslinks in ageing and diabetes - the good, the bad, and the ugly. Muscles, Ligaments and Tendons Journal, 2014. 4(3): p. 303-308. 11. Shetty, R., et al., Attenuation of lysyl oxidase and collagen gene expression in keratoconus patient corneal epithelium corresponds to disease severity. Molecular Vision, 2015. 21: p. 12-25. 12. Takaoka, A., et al., An Evaluation of Lysyl Oxidase–Derived Cross-Linking in Keratoconus by Liquid Chromatography/Mass SpectrometryCross-Linking Evaluation in Keratoconus by LC/MS. Investigative Ophthalmology & Visual Science, 2016. 57(1): p. 126-136. 13. Riley, G.P., et al., Collagenase (MMP-1) and TIMP-1 in destructive corneal disease associated with rheumatoid arthritis. Eye, 1995. 9(6): p. 703-718. 14. Collier, S.A., Is the corneal degradation in keratoconus caused by matrix-metalloproteinases? Clinical & Experimental Ophthalmology, 2001. 29(6): p. 340-344. 15. Balasubramanian, S.A., et al., Proteases, proteolysis and inflammatory molecules in the tears of people with keratoconus. Acta Ophthalmologica, 2012. 90(4): p. e303-e309. 16. Dudakova, L. and K. Jirsova, The impairment of lysyl oxidase in keratoconus and in keratoconus-associated disorders. Journal of Neural Transmission, 2013. 120(6): p. 977-982. 17. Coskunseven, E., F. Jankov Mr 2nd Fau - Hafezi, and F. Hafezi, Contralateral eye study of corneal collagen cross-linking with riboflavin and UVA irradiation in patients with keratoconus. Journal of Refractive Surgery, 2009. 25(1081-597X (Print)): p. 371-376. 18. Wollensak, G., E. Spoerl, and T. Seiler, Riboflavin/ultraviolet-a–induced collagen crosslinking for the treatment of keratoconus. American Journal of Ophthalmology, 2003. 135(5): p. 620-627. 19. Brart, D.P.S., et al., A randomised, prospective study to investigate the efficacy of riboflavin/ultraviolet A (370 nm) corneal collagen cross-linkage to halt the progression of keratoconus. British Journal of Ophthalmology, 2011. 95(11): p. 1519. 20. Hersh, P.S., S.A. Greenstein, and K.L. Fry, Corneal collagen crosslinking for keratoconus and corneal ectasia: One-year results. Journal of Cataract & Refractive Surgery, 2011. 37(1): p. 149-160. 21. Kohlhaas, M., et al., Biomechanical evidence of the distribution of cross-links in corneastreated with riboflavin and ultraviolet A light. Journal of Cataract & Refractive Surgery, 2006. 32(2): p. 279-283. 22. Wollensak, G., et al., Corneal Endothelial Cytotoxicity of Riboflavin/UVA Treatment in vitro. Ophthalmic Research, 2003. 35(6): p. 324-328. 23. Mazzotta, C., et al., Treatment of progressive keratoconus by riboflavin-UVA-induced cross-linking of corneal collagen: ultrastructural analysis by Heidelberg Retinal Tomograph II in vivo confocal microscopy in humans. Cornea, 2007. 26(0277-3740 (Print)). 24. Wollensak, G., et al., Keratocyte cytotoxicity of riboflavin//UVA-treatment in vitro. Eye, 2004. 18(7): p. 718-722. 25. Kymionis, G.D., et al., Corneal stroma demarcation line after standard and high-intensity collagen crosslinking determined with anterior segment optical coherence tomography. Journal of Cataract & Refractive Surgery, 2014. 40(5): p. 736-740. 26. Brindley, G.S., The Bunsen-Roscoe law for the human eye at very short durations. The Journal of Physiology, 1952. 118(1): p. 135-139. 27. Raiskup-Wolf, F., et al., Collagen crosslinking with riboflavin and ultraviolet-A light in keratoconus: Long-term results. Journal of Cataract & Refractive Surgery, 2008. 34(5): p. 796-801. 28. Krueger RR, Spoerl E, and H. S., Rapid vs standard collagen CXL with equivalent energy dosing., in Proceedings of the Third International Congress of Corneal Collagen Crosslinking. 2007: Zurich, Switzerland. 29. Wollensak, G., et al., Endothelial cell damage after riboflavin–ultraviolet-A treatment in the rabbit. Journal of Cataract & Refractive Surgery, 2003. 29(9): p. 1786-1790. 30. O’Brart, D.P.S., Corneal collagen cross-linking: A review. Journal of Optometry, 2014. 7(3): p. 113-124. 31. Zhang, Z.-Y. and X.-R. Zhang, Efficacy and safety of transepithelial corneal collagen crosslinking. Journal of Cataract & Refractive Surgery, 2012. 38(7): p. 1304. 32. Kolli, S. and I.M. Aslanides, Safety and efficacy of collagen crosslinking for the treatment of keratoconus. Expert Opinion on Drug Safety, 2010. 9(6): p. 949-957. 33. Kozobolis V.Labiris G and Gkika M, Corneal collagen cross-linking using riboflavin and ultraviolet-A : a review of clinical and experimental studies International Ophthalmol, 2011. 31(4): p. 309-957. 34. Na Li and Z.F. Xiujun Peng, Research Progress in corneal cross-linking agents. Eye Science, 2014. 29: p. 125-128. 35. Jorge-Herrero, E., et al., Influence of different chemical cross-linking treatments on the properties of bovine pericardium and collagen. Biomaterials, 1999. 20(6): p. 539-545. 36. Dunn, R.M., Cross-linking in biomaterials: a primer for clinicians. Plastic and Reconstructive Surgery, 2012. 130(1529-4242 (Electronic)): p. 18S-26S. 37. Ma, B., et al., Crosslinking strategies for preparation of extracellular matrix-derived cardiovascular scaffolds. Regenerative Biomaterials, 2014. 1(1): p. 81-89. 38. Avila, M.Y. and J.L. Navia, Effect of genipin collagen crosslinking on porcine corneas. J Cataract Refract Surg, 2010. 36(4): p. 659-64. 39. Avila, M.Y., V.A. Gerena, and J.L. Navia, Corneal crosslinking with genipin, comparison with UV-Riboflavin in ex-vivo model. Molecular Vision, 2012. 18: p. 1068-1073. 40. Avila, M.Y., M. Narvaez, and J.P. Castañeda, Effects of genipin corneal crosslinking in rabbit corneas. Journal of Cataract & Refractive Surgery, 2016. 42(7): p. 1073-1077. 41. Spoerl, E., M. Huhle, and T. Seiler, Induction of Cross-links in Corneal Tissue. Experimental Eye Research, 1998. 66(1): p. 97-103. 42. Spoerl, E. and T. Seiler, Techniques for stiffening the cornea. J Refract Surg, 1999. 15(1081-597X (Print)). 43. Liu, Y., et al., A Simple, Cross-linked Collagen Tissue Substitute for Corneal Implantation. Investigative Ophthalmology & Visual Science, 2006. 47(5): p. 1869-1875. 44. Koh, B.L., et al., Epoxy Cross-Linked Collagen and Collagen-Laminin Peptide Hydrogels as Corneal Substitutes. Journal of Functional Biomaterials, 2013. 4(3). 45. Kim, M., et al., Pharmacologic Alternatives to Riboflavin Photochemical Corneal Cross-Linking: A Comparison Study of Cell Toxicity Thresholds. Investigative Ophthalmology & Visual Science, 2014. 55(5): p. 3247-3257. 46. Babar, N., et al., Cosmetic Preservatives as Therapeutic Corneal and Scleral Tissue Cross-Linking AgentsCosmetic Preservatives for Tissue Cross-Linking. Investigative Ophthalmology & Visual Science, 2015. 56(2): p. 1274-1282. 47. Nyquist, G.W., Rheology of the cornea: Experimental techniques and results. Experimental Eye Research, 1968. 7(2): p. 183-IN2. 48. Elsheikh, A., et al., Numerical Study of the Effect of Corneal Layered Structure on Ocular Biomechanics. Current Eye Research, 2009. 34(1): p. 26-35. 49. Greene, P.R. and T.A. McMahon, Scleral creep vs. temperature and pressure in vitro. Experimental Eye Research, 1979. 29(5): p. 527-537. 50. Boyce, B.L., et al., Stress-controlled viscoelastic tensile response of bovine cornea. Journal of Biomechanics, 2007. 40(11): p. 2367-2376. 51. Wollensak, G., E. Spoerl, and T. Seiler, Stress-strain measurements of human and porcine corneas after riboflavin–ultraviolet-A-induced cross-linking. Journal of Cataract & Refractive Surgery, 2003. 29(9): p. 1780-1785. 52. Parfitt, G.J., et al., Three-dimensional reconstruction of collagen–proteoglycan interactions in the mouse corneal stroma by electron tomography. Journal of Structural Biology, 2010. 170(2): p. 392-397. 53. Parry, D.A.D., G.R.G. Barnes, and A.S. Craig, A Comparison of the Size Distribution of Collagen Fibrils in Connective Tissues as a Function of Age and a Possible Relation between Fibril Size Distribution and Mechanical Properties. Proceedings of the Royal Society of London. Series B. Biological Sciences, 1978. 203(1152): p. 305. 54. Parry, D.A., The molecular and fibrillar structure of collagen and its relationship to the mechanical properties of connective tissue. Biophys Chem., 1988. 29(0301-4622 (Print)): p. 195-209. 55. Dale, W.C. and E. Baer, Fibre-buckling in composite systems: a model for the ultrastructure of uncalcified collagen tissues. Journal of Materials Science, 1974. 9(3): p. 369-382. 56. Fratzl, P., et al., Fibrillar Structure and Mechanical Properties of Collagen. Journal of Structural Biology, 1998. 122(1): p. 119-122. 57. Garcia-Porta, N., et al., Corneal Biomechanical Properties in Different Ocular Conditions and New Measurement Techniques. ISRN Ophthalmology, 2014. 2014: p. 19. 58. Girard, M.J.A., et al., Scleral Biomechanics in the Aging Monkey Eye. Investigative ophthalmology & visual science, 2009. 50(11): p. 5226-5237. 59. Avila, M.Y. and J.L. Navia, Effect of genipin collagen crosslinking on porcine corneas. Journal of Cataract & Refractive Surgery, 2010. 36(1873-4502 (Electronic)): p. 659-664. 60. Tao, X., et al., Role of Corneal Epithelium in Riboflavin/Ultraviolet-A Mediated Corneal Cross-linking Treatment in Rabbit Eyes. BioMed Research International, 2013. 2013: p. 624563. 61. Hayes, S., et al., The effect of riboflavin/UVA collagen cross-linking therapy on the structure and hydrodynamic behaviour of the ungulate and rabbit corneal stroma. PLoS ONE, 2013. 8(1932-6203 (Electronic)). 62. Hedbys, B.O., The role of polysaccharides in corneal swelling. Experimental Eye Research, 1961. 1(1): p. 81-91. 63. Xi Cheng, H.H.-M., Peter M. Pinsky, Modeling Collagen-Proteoglycan Structural Interactions in the Human Cornea, in Protein and Cell Mechanics. 2013, Springer: Dordrecht. p. 11-24. 64. Bettelheim, F.A. and B. Plessy, The hydration of proteoglycans of bovine cornea. Biochimica et Biophysica Acta (BBA) - General Subjects, 1975. 381(1): p. 203-214. 65. François, J., M. Rabaey, and G. Vandermeerssche, L'ultrastructure des tissus oculaires au microscope électronique. Ophthalmologica, 1954. 127(2): p. 74-85. 66. Maurice, D.M., The structure and transparency of the cornea. The Journal of Physiology, 1957. 136(2): p. 263-286.1. 67. Wollensak, G., et al., Hydration behavior of porcine cornea crosslinked with riboflavin and ultraviolet A. Journal of Cataract & Refractive Surgery, 2007. 33(3): p. 516-521. 68. Scott, J.E., Morphometry of cupromeronic blue-stained proteoglycan molecules in animal corneas, versus that of purified proteoglycans stained in vitro, implies that tertiary structures contribute to corneal ultrastructure. Journal of Anatomy, 1992. 180(Pt 1): p. 155-164. 69. Xu, Y., Chapter 9 - Thermal Stability of Collagen Triple Helix, in Methods in Enzymology. 2009, Academic Press. p. 211-232. 70. Spoerl, E., et al., Thermomechanical Behavior of Collagen-Cross-Linked Porcine Cornea. Ophthalmologica, 2004. 218(2): p. 136-140. 71. Paik, D.C., et al., Aliphatic β-nitro alcohols for non-enzymatic collagen cross-linking of scleral tissue. Experimental Eye Research, 2008. 87(3): p. 279-285. 72. Paik, D.C., et al., Initial studies using aliphatic beta-nitro alcohols for therapeutic corneal cross-linking. Investigative ophthalmology & visual science, 2009. 50(1552-5783 (Electronic)): p. 1098-1105. 73. Zhou, L., et al., Expression of degradative enzymes and protease inhibitors in corneas with keratoconus. Investigative Ophthalmology & Visual Science, 1998. 39(7): p. 1117-1124. 74. Davidson, A.E., et al., The pathogenesis of keratoconus. Eye, 2014. 28(2): p. 189-195. 75. Spoerl, E., T. Wollensak G Fau - Seiler, and T. Seiler, Increased resistance of crosslinked cornea against enzymatic digestion. Current Eye Research, 2009. 29(0271-3683 (Print)). 76. Aldahlawi, N.H., et al., Enzymatic Resistance of Corneas Crosslinked Using Riboflavin in Conjunction With Low Energy, High Energy, and Pulsed UVA Irradiation ModesCorneal Enzymatic Resistance Following Crosslinking. Investigative Ophthalmology & Visual Science, 2016. 57(4): p. 1547-1552. 77. Aldahlawi, N.H., et al., An investigation into corneal enzymatic resistance following epithelium-off and epithelium-on corneal cross-linking protocols. Experimental Eye Research, 2016. 153: p. 141-151. 78. Zhang, Y., A.H. Conrad, and G.W. Conrad, Effects of Ultraviolet-A and Riboflavin on the Interaction of Collagen and Proteoglycans during Corneal Cross-linking. The Journal of Biological Chemistry, 2011. 286(15): p. 13011-13022. 79. Zhang, Y., et al., Resistance of Corneal RFUVA–Cross-Linked Collagens and Small Leucine-Rich Proteoglycans to Degradation by Matrix Metalloproteinases. Investigative Ophthalmology & Visual Science, 2013. 54(2): p. 1014-1025. 80. Williams, V.Z., Infrared and Raman Spectra of Polyatomic Molecules (Herzberg, Gerhard). Journal of Chemical Education, 1945. 22(11): p. 572. 81. Fini, M.E., Keratocyte and fibroblast phenotypes in the repairing cornea. Progress in Retinal and Eye Research, 1999. 18(1350-9462 (Print)). 82. Spoerl, E., et al., Safety of UVA-Riboflavin Cross-Linking of the Cornea. Cornea, 2007. 26(4). 83. Englert, C., et al., Bonding of articular cartilage using a combination of biochemical degradation and surface cross-linking. Arthritis Research & Therapy, 2007. 9(3): p. R47-R47. 84. Sung, H.W., et al., In vitro evaluation of cytotoxicity of a naturally occurring cross-linking reagent for biological tissue fixation. J Biomater Sci Polym Ed., 1999. 10(0920-5063 (Print)): p. 63-78. 85. Lai, J.-Y., Biocompatibility of Genipin and Glutaraldehyde Cross-Linked Chitosan Materials in the Anterior Chamber of the Eye. International Journal of Molecular Sciences, 2012. 13(9): p. 10970-10985. 86. De Boulle, K., et al., A Review of the Metabolism of 1,4-Butanediol Diglycidyl Ether–Crosslinked Hyaluronic Acid Dermal Fillers. Dermatologic Surgery, 2013. 39(12): p. 1758-1766. 87. Li, X., et al., Novel hydrogels based on carboxyl pullulan and collagen crosslinking with 1, 4-butanediol diglycidylether for use as a dermal filler: initial in vitro and in vivo investigations. Materials Science and Engineering: C, 2015. 57: p. 189-196. 88. Rafat, M., et al., Highly elastic epoxy cross-linked collagen hydrogels for corneal tissue engineering. Acta Ophthalmologica, 2012. 90: p. 0-0. 89. Lan, S.-M., et al., Investigation into the safety of perineural application of 1,4-butanediol diglycidyl ether-crosslinked hyaluronan in a rat model. Journal of Biomedical Materials Research Part B: Applied Biomaterials, 2015. 103(3): p. 718-726. 90. Eddington, W.A., et al., Evaluation of Cytotoxicity of Riboflavin/UVA Cross-Linking Applied to Human Corneal Endothelium Cells. Investigative Ophthalmology & Visual Science, 2014. 55(13): p. 2022-2022. 91. Sato, K., et al., The Primary Cytotoxicity in Ultraviolet-A-Irradiated Riboflavin Solution Is Derived from Hydrogen Peroxide. Journal of Investigative Dermatology, 1995. 105(4): p. 608-612. 92. Minami, H., et al., Hypoxia Potentiates Ultraviolet A-Induced Riboflavin Cytotoxicity. Journal of Investigative Dermatology, 1999. 113(1): p. 77-81. 93. Kohlhaas, M., et al., Biomechanical evidence of the distribution of cross-links in corneas treated with riboflavin and ultraviolet A light. 2006(0886-3350 (Print)). 94. Hayes, S., et al., Riboflavin/UVA Collagen Cross-Linking-Induced Changes in Normal and Keratoconus Corneal Stroma. PLoS ONE, 2011. 6(8): p. e22405. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/67857 | - |
dc.description.abstract | 核黃素/紫外線膠原蛋白交聯術已普遍得到認可是治療圓錐角膜及其他角膜異位症安全又有效的療法。核黃素於其中扮演光敏劑的角色,對於波長370nm的光能具最大吸收峰值,當其受到波長370nm的紫外光照射、激發時,核黃素會因而產生自由基導致組織中的膠原纖維進行物理交聯,因而使逐漸變薄和弱化的角膜基質被硬化。然而,有鑑於紫外線照射的傷害力,此種光交聯法仍有許多潛在風險。因此,許多研究團隊開始改用化學交聯劑,作為光交聯的替代方案,以提高角膜的機械性質及硬度。在本研究中,我們選擇了三種不同的化學交聯劑,旨在比較這些化學交聯法和核黃素/紫外線交聯法對牛角膜的生物物理、生物化學、生物力學和光譜學性質的影響。研究結果顯示,無論我們使用哪種交聯方法,牛角膜的機械強度都有顯著的變化,對於酵素酶的消化抵抗力也有增加,但是對於角膜的含水行為來講並無太大的改變,此外,從傅立葉轉換紅外光譜的分析結果看來,角膜交聯後力學強度的提升及對酵素酶消化抵抗力的提升很有可能是因為多了碳氫鍵的生成。 | zh_TW |
dc.description.abstract | Riboflavin/UVA collagen cross-linking has already been recognized as a safe and effective therapy for the progressive keratoconus and other corneal ectatic disorders. The thinning and weakening corneal stroma can be stiffened when the photosensitizer riboflavin excited by UVA at its absorption peak of 370 nm creates free radicals resulting in cross-linking of collagen fibers. However, there are still some potential risks for the corneal and the ocular tissues with UVA irradiation. Therefore, searching other chemical cross-linking alternatives have become emergent to enhance biomechanical properties and stiffness of cornea in addition to riboflavin/UVA collagen cross-linking. In this research, we chose three different chemical cross-linkers and aimed to compare their safety and effectiveness caused by these chemical cross-linking and riboflavin/UVA collagen cross-linking on the biophysical, biochemical, biomechanical and spectroscopy properties of bovine cornea. Our results suggest that there are significant change in the mechanical strength of bovine cornea and its resistance against enzyme digestion in all of the cross-linking methods. However, there is no difference of the hydration behavior of cornea after cross-linking treated among them except the group cross-linked by BDDE. In addition, from the FT-IR spectrum that the enhancement of biomechanical property of cornea and the resistance to enzyme digestion are possibly due to the formation of carbon-oxygen linkage between collagen and cross-linker. | en |
dc.description.provenance | Made available in DSpace on 2021-06-17T01:54:08Z (GMT). No. of bitstreams: 1 ntu-106-R04548006-1.pdf: 2158730 bytes, checksum: 7b2f68dc34b4bd665b608dc920da4669 (MD5) Previous issue date: 2017 | en |
dc.description.tableofcontents | 誌謝 i
中文摘要 ii ABSTRACT iii CONTENTS iv LIST OF FIGURES vi LIST OF TABLES vii Chapter 1 Introduction 1 1.1 Keratoconus 1 1.2 Corneal structures 1 1.3 Corneal collagen cross-linking 3 1.3.1 Collagen structure maturation and degradation 3 1.3.2 Collagen Cross-linking protocols in clinical practice 4 1.4 Chemical cross-links and potential applications in ophthalmology 6 1.5 Evaluating corneal properties using cross-linking strategies 8 1.5.1 Biomechanical properties 8 1.5.2 Biophysical properties 9 1.5.3 Biochemistry properties 11 1.6 The Aim 13 Chapter 2 Materials and methods 14 2.1 Materials 14 2.2 Methods 14 2.2.1 Human corneal epithelial cell (HCEC) culture 14 2.2.2 Isolation of bovine corneal fibroblasts (BCfb) and bovine corneal endothelium cell (BCED) 15 2.2.3 Cell viability 16 2.2.4 Crosslinking procedures 16 .2.2.4.1 Photo-induced cross-linking 17 .2.2.4.2 Chemical cross-linking 17 2.2.5 Hydration behavior 18 2.2.6 Enzymatic digestion 18 2.2.7 Biomechanical measurements 18 2.2.8 Fourier-transformed infrared spectroscopy(FT-IR) 19 2.2.9 Statistical analysis 19 Chapter 3 Results 20 3.1 Cell viability 20 3.2 Hydration behavior 21 3.3 Enzymatic digestion 21 3.4 Biomechanical measurements 22 3.5 Fourier-transformed infrared spectroscopy 23 Chapter 4 Discussion 25 Chapter 5 Conclusion and perspective 30 FIGURES 31 Tables 36 REFERENCES 38 LIST OF FIGURES Figure 1 Cross section through the cornea 3 Figure 2 Collagen lamellae in the corneal stroma 3 Figure 3 Hyperelastic behaviour of sclera tissue governed by the un-crimpling of buckled collagen fibres 9 Figure 4 Collagen-Proteoglycan arrangement in the corneal stroma 10 Figure 5 Experiment framework 13 Figure 6 Cross-linkers 26 Figure 7 The possible locations where cross-links occur after cross-linking 27 Figure 8 Cell Viability 31 Figure 9 Bovine Corneal Hydration Behavior 32 Figure 10 Bovine Cornea Enzyme Digestion 33 Figure 11 Bovine Cornea Young’s Modulus 34 Figure 12 FT-IR Spectrum of Bovine Cornea 35 LIST OF TABLES Table 1 Weight of Bovine Cornea before/after immersion (n = 3) 36 Table 2 Young’s Modulus of Bovine cornea after cross-linking (control group:n=12; experiment groups: n = 6) 36 Table 3 Under curve area of cross-linked cornea FT-IR spectrum (n=4, p value : compare to control group) 37 | |
dc.language.iso | en | |
dc.title | 利用交聯反應治療角膜病變之研究 | zh_TW |
dc.title | The Research of Healing Cornea Lesion with Cross-linking Reaction | en |
dc.type | Thesis | |
dc.date.schoolyear | 105-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 王一中(I-Jong Wang),林宏殷(Hung-Yin Lin),李玫樺(Mei-Hwa Lee) | |
dc.subject.keyword | 圓錐角膜,核黃素/紫外線交聯術,化學交聯劑,生物機械性質,酵素消化,紅外線光譜, | zh_TW |
dc.subject.keyword | Keratoconus,riboflavin/UVA crosslinking,chemical cross-linker,biomechanical strength,enzyme digestion,infrared spectroscopy, | en |
dc.relation.page | 43 | |
dc.identifier.doi | 10.6342/NTU201701870 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2017-07-24 | |
dc.contributor.author-college | 工學院 | zh_TW |
dc.contributor.author-dept | 醫學工程學研究所 | zh_TW |
顯示於系所單位: | 醫學工程學研究所 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-106-1.pdf 目前未授權公開取用 | 2.11 MB | Adobe PDF |
系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。