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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 董成淵(Chen-Yuan Dong) | |
| dc.contributor.author | Ping-Jung Su | en |
| dc.contributor.author | 蘇秉榮 | zh_TW |
| dc.date.accessioned | 2021-06-15T06:53:28Z | - |
| dc.date.available | 2016-02-20 | |
| dc.date.copyright | 2011-02-20 | |
| dc.date.issued | 2011 | |
| dc.date.submitted | 2011-02-12 | |
| dc.identifier.citation | 1. Shoulders, M. D., and R. T. Raines. 2009. Collagen structure and stability. Annu Rev Biochem 78:929-958.
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Monitoring the thermally induced structural transitions of collagen by use of second-harmonic generation microscopy. Optics Letters 30:622-624. 41. Sun, Y., W. L. Chen, S. J. Lin, S. H. Jee, Y. F. Chen, L. C. Lin, P. T. C. So, and C. Y. Dong. 2006. Investigating mechanisms of collagen thermal denaturation by high resolution second-harmonic generation imaging. Biophysical Journal 91:2620-2625. 42. Kim, B. M., J. Eichler, K. M. Reiser, A. M. Rubenchik, and L. B. Da Silva. 2000. Collagen structure and nonlinear susceptibility: Effects of heat, glycation, and enzymatic cleavage on second harmonic signal intensity. Lasers in Surgery and Medicine 27:329-335. 43. Koehler, M. J., K. Konig, P. Elsner, R. Buckle, and M. Kaatz. 2006. In vivo assessment of human skin aging by multiphoton laser scanning tomography. Optics Letters 31:2879-2881. 44. Lee, H. S., S. W. Teng, H. C. Chen, W. Lo, Y. Sun, T. Y. Lin, L. L. Chiou, C. C. Jiang, and C. Y. Dong. 2006. Imaging human bone marrow stem cell morphogenesis in polyglycolic acid scaffold by multiphoton microscopy. Tissue Engineering 12:2835-2841. 45. Williams, R. M., W. R. Zipfel, and W. W. Webb. 2005. Interpreting second-harmonic generation images of collagen I fibrils. Biophysical Journal 88:1377-1386. 46. Lee, H. S., G. T. Huang, H. S. Chiang, L. L. Chiou, M. H. Chen, C. H. Hsieh, and C. C. Jiang. 2003. Multipotential mesenchymal stem cells from femoral bone marrow near the site of osteonecrosis. Stem Cells 21:190-199. 47. Chen, W. L., C. H. Huang, L. L. Chiou, T. H. Chen, Y. Y. Huang, C. C. Jiang, H. S. Lee, and C. Y. Dong. 2010. Multiphoton Imaging and Quantitative Analysis of Collagen Production by Chondrogenic Human Mesenchymal Stem Cells Cultured in Chitosan Scaffold. Tissue Eng Part C Methods. 48. Cox, G., E. Kable, A. Jones, I. K. Fraser, F. Manconi, and M. D. Gorrell. 2003. 3-dimensional imaging of collagen using second harmonic generation. 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Physical Review Letters 92:207401. 54. Mitchell, S. A., R. A. McAloney, D. Moffatt, N. Mora-Diez, and M. Z. Zgierski. 2005. Second-harmonic generation optical activity of a polypeptide alpha-helix at the air/water interface. Journal of Chemical Physics 122:114707. 55. Deniset-Besseau, A., J. Duboisset, E. Benichou, F. Hache, P. F. Brevet, and M. C. Schanne-Klein. 2009. Measurement of the Second-Order Hyperpolarizability of the Collagen Triple Helix and Determination of Its Physical Origin. Journal of Physical Chemistry B 113:13437-13445. 56. Pena, A. M., T. Boulesteix, T. Dartigalongue, and M. C. Schanne-Klein. 2005. Chiroptical effects in the second harmonic signal of collagens I and IV. Journal of the American Chemical Society 127:10314-10322. 57. Psilodimitrakopoulos, S., S. Santos, I. Amat-Roldan, A. K. N. Thayil, D. Artigas, and P. Loza-Alvarez. 2009. 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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/48349 | - |
| dc.description.abstract | 本論文使用二階電化率顯微術來研究膠原蛋白的結構。利用旋轉線性飛秒脈衝激發光，研究病理皮膚，軟骨組織工程與眼角膜。藉由測量影像中每一個點的二階電化率張量，並轉換成影像圖，發現此張量可以用來鑑別病理皮膚，第一型與第二型的膠原纖維。更進一步，建立分子模型，來描述所觀測到的張量變異，並且此模型和已知的高解析x-ray的數據吻合。除此之外，將這顯微術更進一步推廣，測量透明材料的折射率、膠原纖維的相關聯常數和纖維走向的亂度。最後，本研究發現，在眼角膜的正向與背向背頻訊號裡，隱藏著纖維走向有強相關聯的特質。 | zh_TW |
| dc.description.abstract | In the thesis, excitation polarization-resolved second harmonic generation (PSHG) microscopy is utilized to study the most rich mammal protein: collagen. Using PSHG microscopy, second harmonic generation (SHG) signal as a function of the excitation polarization angle was measured for normal and pathological human dermis, engineered cartilage tissue, and cornea. Second-order susceptibility (SOS,χ (2) ) tensor ratios of different collagen types were determined to single-pixel resolution and the results were displayed as images.
It was found that χ (2) tensor ratios can be used in the discrimination of normal and pathological skin dermis which normal dermis contain approximately 80% type I collagen and 20% type III collagen. SOS microscopy was found to be useful in distinguish the type I and type II collagen. In particular, χzzz|χzxx = 1.40 ± 0.04 and χxzx|χzxx = 0.53 ± 0.10 are obtained for type I collagen from rat tail tendon, and χzzz|χzxx = 1.14 ± 0.09 and χxzx|χzxx = 0.29 ± 0.11 for type II collagen from rat trachea cartilage. We also extended this methodology to the label-free SOS imaging of engineered cartilage tissue and we found that the presence of type I and II collagen in the tissue can be identified. Next, in an attempt to better explain the SOS results for collagen, we developed a new molecular model which incorporated the SOS contributions of peptide and methylene groups and it was found that the model is consistent with high resolution x-ray diffraction data in collagen-like model peptides. As extensions to the work described above, the methodology described in this thesis was also found to be able to determine fibril orientation. Strong correlation of fibril orientation between forward and backward scattering SHG was found and the described approach has great potential in the application of clinical ophthalmology. Finally, localized birefringence of a material was found to be determinable through depth-resolved SOS microscopy. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-15T06:53:28Z (GMT). No. of bitstreams: 1 ntu-100-D94222010-1.pdf: 9233881 bytes, checksum: 03dba2dc5ce2544ff60c904bfc75e02b (MD5) Previous issue date: 2011 | en |
| dc.description.tableofcontents | 1. Introduction..............................................................................................................8
1.1 Collagen ..........................................................................................................8 1.2 Second harmonic generation (SHG) microscopy......................................12 1.2.1 Requirement of non-centrosymmetry.............................................12 1.2.2 SHG from a nonlinear dipole radiator............................................13 1.2.3 χ (2) tensor components in cylindrical symmetry ........................14 1.2.4 Relationship of SHG intensity and excitation linear polarizations ......................................................................................................................14 2. Label-free imaging of pathological skin dermis..................................................16 2.1 Introduction..................................................................................................16 2.2 Materials and methods ................................................................................17 2.2.1 Second order susceptibility image analysis.....................................17 2.2.2 Excitation polarization resolved second harmonic generation microscope ..................................................................................................20 2.2.3 Specimen preparation.......................................................................22 2.3 Results and discussions................................................................................23 3. Discrimination of type I/II collagen......................................................................31 3.1 Introduction..................................................................................................31 3.2 Materials and Methods................................................................................33 3.2.1 Excitation polarization-resolved SHG microscope ........................33 3.2.2 Sample preparation ..........................................................................33 3.3 Results and Discussion.................................................................................37 3.4 Summary.......................................................................................................45 4. Determination of collagen nanostructure ............................................................47 4.1 Introduction..................................................................................................47 4.2 Theoretical Background..............................................................................49 4.2.1 Cylindrical symmetry of collagen molecules ..................................49 4.2.2 Molecular origins of second order susceptibility: peptide groups50 4.2.3 Molecular origins of second order susceptibility: methylene groups..........................................................................................................51 4.2.4 Molecular origins of second order susceptibility: peptide and methylene groups combined......................................................................52 4.3 Materials and Methods................................................................................56 4.3.1 Excitation polarization-resolved SHG microscope ........................56 4.3.2 Sample preparation: pure type I and II collagens in tissues and mixed types of collagen..............................................................................56 4.3.3 Data analysis......................................................................................58 4.4 Results and Discussion.................................................................................59 5. Measurement of birefringence and attenuation..................................................72 5.1 Motivation.....................................................................................................72 5.2 Measurement of birefringence....................................................................72 5.3 Attenuation of light......................................................................................73 5.4 Measurement of corneal birefringence ......................................................74 6. Orientation correlation length..............................................................................75 6.1 Introduction..................................................................................................75 6.2 Methods.........................................................................................................76 6.3 Results ...........................................................................................................77 7. Analysis of orienation angles.................................................................................79 7.1 Introduction..................................................................................................79 7.2 Results ...........................................................................................................79 8. Conclusions and perspectives................................................................................81 9. References...............................................................................................................82 10. Publication lists ....................................................................................................89 | |
| dc.language.iso | en | |
| dc.subject | 二階電化率 | zh_TW |
| dc.subject | 膠原蛋白 | zh_TW |
| dc.subject | second order susceptibility | en |
| dc.subject | collagen | en |
| dc.title | 二階電化率顯微術於膠原蛋白結構的研究 | zh_TW |
| dc.title | Investigation of collagen structure through second order susceptibility microscopy | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 99-1 | |
| dc.description.degree | 博士 | |
| dc.contributor.oralexamcommittee | 朱士維(Shi-Wei Chu),李宣書(Hsuan-Shu Lee),楊台鴻(Tai-Hong Young),黃義侑(Yi-You Huang),陳永芳(Yang-Fang Chen),章為皓(Wei-Hau Chang),楊維元(Wei-Yuan Young) | |
| dc.subject.keyword | 膠原蛋白,二階電化率, | zh_TW |
| dc.subject.keyword | collagen,second order susceptibility, | en |
| dc.relation.page | 89 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2011-02-12 | |
| dc.contributor.author-college | 理學院 | zh_TW |
| dc.contributor.author-dept | 物理研究所 | zh_TW |
| 顯示於系所單位： | 物理學系 | |
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