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http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/30524完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 張正憲(Jeng-Shian Chang) | |
| dc.contributor.author | Chih-Kai Yang | en |
| dc.contributor.author | 楊智凱 | zh_TW |
| dc.date.accessioned | 2021-06-13T02:06:58Z | - |
| dc.date.available | 2007-07-16 | |
| dc.date.copyright | 2007-07-16 | |
| dc.date.issued | 2007 | |
| dc.date.submitted | 2007-06-29 | |
| dc.identifier.citation | [1] W. S. Tillet and T. Francis, Serological reactions in pneumonia with a non-protein somatic fraction of pneumococcus, J. Exp. Med., vol. 52 (1930), pp. 561–571.
[2] N. Camillone, Diffusion-limited thiol adsorption on the gold (111) surface, Langmuir, vol. 20 (2004), pp. 1199-1206. [3] D. B. Hibbert, and J. J. Gooding, Kinetics of irreversible adsorption with diffusion: Application to biomolecule immobilization, Langmuir, vol. 18 (2002), pp. 1770-1776. [4] W. M. Deen, Analysis of Transport Phenomena, Oxford University Press, New York, 1998. [5] M. Sigurdson, D. Wang, and C. D. Meinhart, Electro-thermal stirring for heterogeneous immunoassays, Lab on a chip, vol. 5 (2005), pp. 1366-1373. [6] R. Pethig, Dieletrophoresis: using inhomogeneous AC electrical fields to separate and manipulate cells, Crit. Revs. Biotechnol., vol. 16 (1996), pp. 331-348. [7] X.-B. Wang, Y. Huang, P.R.C. Gascoyne, and F.F. Becker, Dielectrophoretic manipulation of particles, IEEE Trans. Ind. Appl., vol. 33 (1997), pp. 660-669. [8] H. Morgan, M.P. Hughes, and N.G. Green, Separation of submicron bioparticles by dielectrophoresis, Biophysical J., vol. 77 (1999), pp. 516-525. [9] A. Ramos, H. Morgan, and A. Castellanos, AC Electrokinetics: a review of forces in microelectrode structures, J.Phys.D:Appl.Phys., vol. 31 (1998), pp. 2338-2353. [10] A. Ramos, A. Gonzalez, N. Green, A. Castellanos, and H. Morgan, Fluid flow induced by nonuniform ac electric fields in electrolytes on microelectrodes, II. A linear double-layer analysis, Phys Rev., vol. 61-4 (2000), pp. 4019-4028. [11] N. Green, A. Ramos, A. Gonzalez, H. Morgan, and A. Castellanos, Fluid flow induced by nonuniform ac electric fields in electrolytes on microelectrodes, I. Experimental measurements, Phys Rev., vol. 61-4 (2000), pp. 4011-4018. [12] C. Meinhart, D. Wang, and K. Turner, Measurement of ac electrokinetic flows, Biomed Microdevices, vol. 5-2 (2003), pp. 139-145. [13] M. Washizu, and S. Suzuki, Molecular dielectrophoresis of biopolymers, IEEE Transaction on Industry Application, vol. 30 (1994), pp. 835-843. [14] D. Wang, M. Sigurdson, and C. D. Meinhart, Experimental analysis of particle and fluid motion in ac electrokinetics, Experiments in Fluid, vol. 38 (2005), pp. 1-10. [15] D.R. Lide, CRC Handbook of Chemistry and Physics, CRC Press, New York, 81st edition, 2000. [16] J. A. Stratton, Electromagnetic Theory, McGraw Hill, New York, 1941. [17] L. D. Landau and E. M. Lifshitz, Fluid Mechanics, Pergamon, Oxford, 1959. [18] I. Langmuir, The adsorption of gases on plane surfaces of glass, mica and platinum, J. Am. Chem. Soc., vol. 40 (1918), pp. 1361-1403. [19] Y. Hokama, M. K. Coleman, and R. F. Riley, An agar interaction in immunodiffusion, J. Immunology, vol. 95 (1965), pp. 156-161. [20] H. A. Leddy and F. Guilak, Site-specific molecular diffusion in articular cartilage measured using fluorescence recovery after photobleaching, Annals of biomedical engineering, vol. 31 (2003), pp. 753-760. [21] E. Behravesh, V. I. Sikavitsas, and A. G. Mikos, Quantification of ligand surface concentration of bulk-modified biomimetic hydrogels, Biomaterials, vol. 24 (2003), pp. 4365-4374. [22] C. Chou, H.-Y. Hsu, H.-T. Wu, K.-Y. Tseng, A. C. C.-J. Yu, Z.-Y. Lee, and T.-S. Chan, Fiber optic biosensor for the detection of C-reactive protein and the study of protein binding kinetics, J. Biomedical Optics, vol. 12 (2007), pp. 024025-1 - 024025-9. [23] Comsol Multiphysics, Version 3.3, COMSOL Ltd., Stokhelm, Sweden. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/30524 | - |
| dc.description.abstract | Specific binding reaction of an analyte-ligand protein pair is a natural characteristic which is applied to design biosensors, such as micro-cantilever beam based biosensor, the Surface Plasmon Resonance (SPR) sensor, and the Quartz Crystal Microbalance (QCM) sensor.
By applying a non-uniform AC electric field to the flow micro-channel of the biosensor, the electro-thermal force can be generated, a pair of stirring vortices can be formed to stir the flow field and the diffusion boundary layer on the reaction surface, and hence increase the transport of the analytes to the reaction surface to enhance the association or dissociation of analyte-ligand complex. This work simulates the binding reaction kinetics of two common-used proteins, CRP and IgG, in a reaction chamber (micro-channel) of a biosensor. For a diffusion-limited protein, whose Damköhler number is greater than unity, the diffusion boundary layer on the reaction surface would hinder the binding reaction from association and dissociation. Several crucial factors which influence the binding reaction curves in the simulation are discussed, including concentration of analyte, position of reaction surface, channel height, and width of reaction surface. A higher channel causes the diffusive transport of the analyte to take longer time to reach the reaction surface, which in term decreases the reaction rate of the protein pairs. The width of the reaction surface plays an important role in the formation of the boundary layer. The wider reaction surface takes more time to allow diffusion to overcome the wider diffusion boundary layer, resulting in a slower binding rate and a longer time to reach saturation. The blocking effect of the flow field by the existence of the reaction surface at the different position of the micro-channel could cause different degrees of enhancement to the association and the dissociation. It is found that by changing the position of the reaction surface the largest enhancement is found at the position near the negative electrode. For the configuration of the micro-channel we studied, the initial slope of the curve of the analyte-ligand complex versus time can be raised up to 5.166 for CRP and 1.934 for IgG in association, and 3.744 for CRP and 1.277 for IgG in dissociation, respectively, under the applied AC field 15 Vrms peak-to-peak and operating frequency 100 kHz. An improved design with neck region near the reaction surface is demonstrated. The reaction surface is fixed to locate at the middle of the bottom side. With the existence of the stirring flow field, the association rate of the 30 μm-neck is 2.733 times to that of the original channel (no neck). The results of 3-D simulation demonstrate the lateral diffusion effect. Furthermore, the design of the U-shape reaction surface enhances the reaction velocity due to its hollow region. The presented data of simulation are useful in designing the biosensors. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-13T02:06:58Z (GMT). No. of bitstreams: 1 ntu-96-R94543048-1.pdf: 3060773 bytes, checksum: a057797836e0ac37901ffe87e4ace786 (MD5) Previous issue date: 2007 | en |
| dc.description.tableofcontents | Acknowledgements i
摘要 ii Abstract iv List of Figures ix List of Tables xii Chapter 1 Introduction 1 Chapter 2 Theory 6 2.1 Electro-thermal force 7 2.2 The electric field 8 2.3 The temperature field 9 2.4 The flow field 9 2.5 The concentration field 10 2.6 The reaction surface 11 Chapter 3 Simulation details 12 3.1 The electric field configuration 13 3.2 The temperature field configuration 14 3.3 The flow field configuration 14 3.4 The concentration field configuration and kinetics of the specific binding 15 3.5 Summary of parameters in simulation 17 Chapter 4 Results in 2-D simulation and discussion 18 4.1 The binding kinetics of CRP and IgG without applying voltage 18 4.2 Effect of inlet flow velocity 21 4.3 The binding kinetics of CRP and IgG in stirring flow field 22 4.4 The diffusion boundary layer 26 4.5 The initial slope of the binding reaction curve 33 4.6 The enhancement factor of the binding kinetics 34 4.7 Damköhler number 36 4.8 The extension of the boundary layer 38 4.9 The design of the micro-channel 40 4.10 Determination of , , and from the experimental data curve 41 4.11 Prediction of bulk concentration of analyte from the experimental data curves 42 Chapter 5 Results in –D simulation and discussion 44 5.1 The binding kinetics of CRP in 3-D simulation 44 5.2 The cavity under the reaction surface 47 5.3 The U-shape reaction surface 49 Chapter 6 Conclusion and future work 51 References 53 | |
| dc.language.iso | en | |
| dc.subject | 結合反應 | zh_TW |
| dc.subject | 解離反應 | zh_TW |
| dc.subject | C-反應蛋白質 | zh_TW |
| dc.subject | 有限元素分析 | zh_TW |
| dc.subject | 生物感測器 | zh_TW |
| dc.subject | 免疫球蛋白-G | zh_TW |
| dc.subject | biosensor | en |
| dc.subject | CRP | en |
| dc.subject | finite element analysis | en |
| dc.subject | IgG | en |
| dc.subject | dissociation | en |
| dc.subject | association | en |
| dc.title | 電熱力的流場攪拌效應對生物感測器吸附受體效益之數值研究 | zh_TW |
| dc.title | Analysis of Enhancement of Analytes Adsorption Due to Flow Stirring by Electro-thermal Force in a biosensor | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 95-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.coadvisor | 趙聖德(Sheng-Der Chao) | |
| dc.contributor.oralexamcommittee | 吳光鐘(Kuang-Chong Wu),黃榮山(Long-Sun Huang),林世明(Shi-Ming Lin),林啟萬 | |
| dc.subject.keyword | 結合反應,解離反應,生物感測器,有限元素分析,C-反應蛋白質,免疫球蛋白-G, | zh_TW |
| dc.subject.keyword | association,dissociation,biosensor,finite element analysis,CRP,IgG, | en |
| dc.relation.page | 55 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2007-07-03 | |
| dc.contributor.author-college | 工學院 | zh_TW |
| dc.contributor.author-dept | 應用力學研究所 | zh_TW |
| 顯示於系所單位: | 應用力學研究所 | |
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