利用表面電漿共振生物感測器及單分子模型槽研究蛋白質在固/液及氣/液界面上之結構

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吳旻珈(Ming-Chia Wu) 查詢紙本館藏

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化學工程與材料工程學系

論文名稱

利用表面電漿共振生物感測器及單分子模型槽研究蛋白質在固/液及氣/液界面上之結構
(Studies of Protein Conformation at Solid/Liquid and Air/Liquid Interfaces by Surface Plasmon Resonance and Langmuir-Blodgett Trough)

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摘要(中)

摘要
本研究利用表面電漿共振生物感測器(SPR)測出角度的變化量，進而得到金膜上蛋白質構型的改變，再利用單分子模型槽(L-B Trough)、圓二色光譜儀(CD)與螢光光譜儀(Fluorescence)得到蛋白質更精確的結構藉以輔佐SPR的結果；實驗上利用溶菌酶(Lysozyme)與核醣核酸酶(Ribonuclease A)這兩種蛋白質，利用有無添加還原劑(i.e. DTT)與不同濃度變性劑(i.e. Urea與GuHCl)的環境下看蛋白質構形的改變。
SPR實驗利用Self-Assembly Monolayer(SAM)及表面活化的方法把蛋白質固定在金膜上，再通入還原劑與不同濃度的變性劑；在沒有添加還原劑的環境下，SPR角度變化量有一個正的趨勢，認為在只有變性劑下的蛋白質結構並沒有完全被破壞，變性劑只是吸附在蛋白質的表面，因變性劑的折射係數(refractive index)較緩衝溶液來的大，因此較高濃度的變性劑下得到較高的角度變化量；在有還原劑的環境下，SPR則是一個負的趨勢，因為雙硫鍵被打斷後，加入變性劑能穩定不穩定的去摺疊狀態，造成蛋白質結構變較鬆散，使得折射係數降低，進而得到一個負的趨勢。而在L-B trough的實驗中，所得到在氣/液界面上每分子所佔據的面積與平衡的表面壓，也可說明以上的現象。最後在輔以CD及Fluorescence能更清楚的知道影響SPR訊號主要是以蛋白質三級結構為主。

摘要(英)

Abstract
Behaviors of proteins immobilized on a gold surface were investigated using a home-made biosensor utilizing surface plasmon resonance(SPR). In order to examine the possibility of the use of SPR for high sensitive, real-time and label-free monitoring of the protein conformation of unfolding and refolding process, the protein immobilized on a self-assembled monolayer (SAM) layer was analyzed. Specific structure was assigned to the changing surface plasmon resonance(SPR) signals of the immobilized proteins using Langmuir-Blodgett Trough(L-B Trough), Circular Dichroism(CD) and Fluorescence spectroscopies, which are established techniques for the conformational analysis of proteins.
For the oxidized proteins, from L-B trough, CD and fluorescence infer that the hydrophobic region was not exposed and retain most of the ordered secondary and tertiary structure. The denaturants(i.e. urea and guanidine hydrochloride) were bound to the protein at specifically hydrophobic sites, therefore SPR angle shift was increasing with concentration of denaturants.
The reducing agent affect the conformational changes of proteins in SPR signal, make a positive SPR angle shift. From L-B truogh experiments reveal a compact conformation and hydrophobic region exposed unobviously, therefore, protein film became compactly and increase the refractive index of protein layers. For the reduced proteins, the denaturants not only destroy the ordered secondary and tertiary structure but also stabilize the unfolded conformation, that would increase the thickness of the protein layers and decrease the refractive index of the protein layers, and therefore SPR angle shift was decreasing with the concentration of denaturants.

關鍵字(中)

★ 蛋白質摺疊與去摺疊
★ 單分子模型槽
★ 表面電漿共振
★ 蛋白質構型

關鍵字(英)

★ protein unfoldimg and refolding
★ Langmuir-Blodgett trough
★ surface plasmon resonance
★ protein conformation

論文目次

目錄
摘要 ……………………………………………………………………Ⅰ
Abstract ……………………………………………………………… Ⅱ
誌謝 ……………………………………………………………………Ⅲ
目錄 ……………………………………………………………………Ⅳ
第一章緒論 ………………………………………………………… 1
第二章文獻回顧
2-1 蛋白質介紹 …………………………………………………… 3
2-1-1　蛋白質的組成及結構…………………………………… 3
2-1-2　穩定蛋白質結構的作用力……………………………… 8
2-2 蛋白質的變性 ………………………………………………… 10
2-3 蛋白質介紹 …………………………………………………… 12
2-3-1 核醣核酸酶(Ribonuclease A；RNase A)介紹 ……… 12
2-3-2 溶菌酶(Lysozyme)介紹………………………………… 14
2-4 表面電漿共振生物感測器 …………………………………… 17
2-4-1 表面電漿共振生物感測器之光學系統………………… 17
2-4-2 表面電漿共振生物感測器應用在蛋白質構形之探討… 20
2-5 單分子模型槽 ………………………………………………… 22
2-5-1 蛋白質於氣/液界面上的吸附行為 …………………… 22
2-5-2 表面張力的定義與量測 ……………………………… 23
2-5-3 單分子層(monolayer) ………………………………… 26
2-5-3-1 氣/液界面之單分子層 ……………………………… 26
2-5-3-2 蛋白質單分子層 …………………………………… 27
2-5-3-3 氣/液界面單分子層行為 …………………………… 28
2-6 圓二色光譜儀 ………………………………………………… 31
2-6-1 圓二色光譜儀測量原理………………………………… 31
2-6-2 蛋白質或多胜肽的圓二色光譜 ………………………… 34
2-7 螢光光譜儀 …………………………………………………… 36
第三章實驗部分
3-1　實驗藥品 ……………………………………………………… 38
3-2　實驗設備 ……………………………………………………… 39
3-3　實驗步驟 ……………………………………………………… 40
3-3-1 溶液配製 ……………………………………………… 40
3-3-1-1 緩衝溶液的配製 ……………………………………… 40
3-3-1-2 變性劑和/或還原劑溶液的配製 …………………… 40
3-3-1-3 蛋白質溶液的配製…………………………………… 40
3-3-1-4 晶片改質步驟 ……………………………………… 41
3-3-2 實驗量測 ……………………………………………… 42
3-3-2-1 表面電漿生物感測器………………………………… 42
3-3-2-2 單分子模型槽………………………………………… 43
3-3-2-3 圓二色光譜儀………………………………………… 45
3-3-2-4 螢光光譜儀…………………………………………… 45
第四章結果與討論
4-1 表面電漿共振生物感測器實驗………………………………… 46
4-1-1 蛋白質與溶液的效應 ………………………………… 48
4-1-2 變性劑對固定化蛋白質構形的影響 ………………… 50
4-1-3 固定化蛋白質的復性…………………………………… 55
4-2 單分子模型槽實驗……………………………………………… 58
4-2-1 蛋白質單分子層經不同濃度變性劑和/或還原劑前處理後於氣/液界面上每分子佔據面積………………………… 58
4-2-2 蛋白質單分子層經不同濃度變性劑和/或還原劑前處理後在氣/液界面上之表面壓力與時間的等溫線…………… 70
4-2-2-1 經變性後的RNase A單分子層在氣/液界面上的平衡表面壓…………………………………………………… 78
4-2-2-2 經變性後的Lysozyme單分子層在氣/液界面上的平衡表面壓………………………………………………… 80
4-3 圓二色光譜儀實驗……………………………………………… 82
4-3-1 利用圓二色光譜儀量測RNase A的結構變化………… 82
4-3-2 利用圓二色光譜儀量測Lysozyme的結構變化 ……… 85
4-4 螢光光譜儀實驗………………………………………………… 88
4-4-1 經不同濃度變性劑和/或還原劑處理後的RNase A螢光變化量 ……………………………………………………… 88
4-4-2 經不同濃度變性劑和/或還原劑處理後的Lysozyme螢光變化量 ……………………………………………………… 93
第五章結論………………………………………………………… 97
參考文獻……………………………………………………………… 99

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96. 數據是由本實驗室林仕淳學姊所提供。

指導教授

陳文逸(Wen-Yih Chen)

審核日期

2004-6-24

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