博碩士論文 93324055 詳細資訊




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姓名 李柏毅(Po-I Lee)  查詢紙本館藏   畢業系所 化學工程與材料工程學系
論文名稱 以螢光光譜觀測蛋白質吸附於疏水表面後之構型變化與吸附位向
(Monitoring the Conformation and Orientation of Protein on a Hydrophobic Surface)
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摘要(中) 本研究的目的,在利用色胺酸的螢光光譜,來推測蛋白質在Octadecyltrimethoxysilane (ODS)疏水的表面吸附後之構形變化、吸附量及吸附位向。我們所選用的蛋白質,包括BAA、BSA及Lysozyme。首先,根據色胺酸螢光光譜的分析,我們發現當其所處環境為極性時,訊號強度會較所處環境為非極性時來得大。且在非極性環境時,最大波峰位置有藍移的現象發生。
在Lysozyme的吸附實驗中,我們發現當不含DL-Ditheothiol (DTT),吸附於ODS表面後,其構形改變不大。並推測Lysozyme先是以α-Domain的Trp123暴露區域為吸附位向,另外兩個暴露之色胺酸(β-Domain-Trp62、Trp63)再漸漸吸附至疏水表面。而當Lysozyme在含有DTT之情況下,吸附於ODS表面後,訊號強度明顯上升且波峰紅移,明顯表示其構形改變。應是因雙硫鍵被破壞,使得內部的Trp28及Trp108暴露出來。
BSA吸附的實驗中發現,吸附後之波峰位置由340nm先藍移至310nm最後漸漸紅移至325nm,我們認為BSA是以位於IB區域暴露之色胺酸(Trp158)吸附於表面,使得吸附後BSA第I與第II區域逐漸攤開轉向。吸附後色胺酸的螢光幾乎完全被淬滅。
在BAA吸附的實驗部份,我們發現BAA的訊號因吸附而下降,但λmax並無改變,因此構形並無隨時間而改變。並由淬滅率的計算推測,而其可能吸附位向為七個色胺酸的暴露面。
本研究利用色胺酸含量多於酪胺酸的Lysozyme探討時,其形變可由內部色胺酸之暴露而明顯的觀察到。又利用色胺酸含量遠少於酪胺酸的BSA探討,其初始吸附方位可很容易的由其明顯的藍位移及螢光淬滅程度而推測。最後,我們探討色胺酸及酪胺酸均富的BAA,也可由其螢光淬滅程度來推測其吸附位向。
摘要(英) In this study, the orientation and conformation change of protein hydrophobic adsorption were examined. There were three proteins been chosen, which were BAA, BSA and Lysozyme. The quartz surface was modified by octadecyltrimethoxysilane to form the hydrophobic surface. At first, according to the tryptophan fluorescence spectrum analysis, the intensity of tryptophan in polar environment was higher than nonpolar environment and the wavelength of lambda maximum was blue shift when tryptophan located in nonpolar environment. In the experiment of Lysozyme hydrophobic adsorption, it can be found that the structure of Lysozyme on ODS surface did not change obviously in phosphate buffer. The signal of tryptophan was quenched slowly as time increase, we could infer that Lysozyme adsorbed firstly by Try123 at α-Domain and then adsorbed gradually by Trp62 and Trp63 at β-Domain. However, when protein solution contained DL-Dithiothreitol, we could obtain that the intensity of lambda 340nm increased and the lambda maximum was red shift. These indicated that the protein structure was changed because of the disulfide bonds were broken which caused that Trp28 and Trp108 exposed outside the protein surface and oriented to polar environment. In the experiment of BSA, we found that when BSA adsorbed on ODS surface the wavelength was blue shift from 340nm to 310nm then gradually red shift to 325nm. We thought that BSA was adsorbed by Trp158 located at IB-domain firstly then forced the I domain and II domain of BSA changed the direction gradually, and the fluorescence of tryptophan was almost disappear after adsorption. Finally, in BAA hydrophobic adsorption experiment, we found that the intensity of 340nm was decrease due to tryptophan be quenched and the lambda maximum was no change which indicated that the native structure of BAA was still maintains on the ODS surface. Furthermore, by calculating the quench ratio of BAA, we could conjecture that the orientation was the plane of BAA which contained seven tryptophan. In consequence, the conformation change and orientation surmise of protein hydrophobic adsorption can be obtained via the fluorescence spectrum analysis directly.
關鍵字(中) ★ 吸附
★ 蛋白質
★ 變性
關鍵字(英) ★ protein
★ adsorption
★ denature
論文目次 中文摘要 I
英文摘要 III
誌謝 V
目錄 VIII
圖目錄 XI
表目錄 XIII
第一章 緒論 1
1.1 研究動機與目的 1
1.2 研究目的 3
第二章 文獻回顧 4
2.1 蛋白質吸附量、構型變化及吸附位向之量測方式 4
2.1.1吸附量之量測 4
2.1.1.1 Depetion消耗量 4
2.1.1.2 Quartz Crystal Microbalance石英晶體振盪 5
2.1.1.3 Surface Plasma Resonance表面電漿共振(SPR) 6
2.1.2吸附構形改變之量測 8
2.1.2.1 圓極偏光光譜儀(circular dichroism) 8
2.1.2.2 原子力顯微鏡(Atomic Force Microscopy) 10
2.1.2.3 Total internal reflection fluorescence 12
2.1.2.4 Fluorescence Spectroscopy螢光光譜儀 13
2.1.2.4.1 螢光光譜之簡介 13
2.1.3吸附位向之量測 16
2.1.3.1 分子模擬 16
2.1.3.2 ENZYME–LINKED IMMUNOSORBENT ASSAY免疫酵素分析 17
2.2 蛋白質介紹 19
2.2.1 溶菌酶(Lysozyme)介紹 19
2.2.2 α-amylase 澱粉分解脢簡介 21
2.2.3 Bovine serum albumin牛血清蛋白簡介 23
第三章 研究設計與原理 25
3.1 利用螢光光譜觀測色胺酸與酪胺酸之螢光訊號 25
3. 2 利用色胺酸與酪胺酸之螢光訊號偵測蛋白質吸附於疏水表面之構形改變、吸附量與吸附位向 27
3.2.1 構形變化 27
3.2.2 吸附量 29
3.2.3 吸附位向 31
3.3 研究原理之整理 32
第四章 實驗藥品、設備與方法 33
4.1 實驗藥品 33
4.2 實驗設備 35
4.3 實驗方法 36
4.3.1 蛋白質濃液配製 36
4.3.2 基材表面酸處理 37
4.3.3 基材表面疏水改質 38
4.3.4 夾具製備 39
4.3.5 蛋白質吸附實驗 40
第五章 結果與討論 41
5.1 疏水性表面改質 42
5.1.1 接觸角(Contact Angle)量測 42
5.1.2 利用Atomic Force Microscopy (AFM)量測表面形貌 43
5.2 Lysozyme吸附 45
5.2.1 Lysozyme存在於親水之OH系統中,DTT存在與否之影響 47
5.2.1.1 螢光訊號觀察 47
5.2.1.2 DTT對Lysozyme在親水系統中構形變化討論 49
5.2.2 Lysozyme在不含DTT的環境中吸附於ODS表面 50
5.2.2.1 螢光訊號觀察 50
5.2.2.2構形變化討論 52
5.2.2.3 Lysozyme吸附量探討 52
5.2.2.4 吸附位向的探討 53
5.2.3 Lysozyme在含有DTT的環境中吸附於ODS表面 55
5.2.3.1 疏水作用力的影響 55
5.2.3.1.1 螢光訊號觀察 55
5.2.3.1.2 sozyme吸附構形變化討論 58
5.2.4 Lysozyme吸附結論 59
5.2.4.1 吸附位向及構形變化機制的探討 59
5.3 BSA(Bovine serum albumin)吸附 61
5.3.1 BSA構形變化、吸附量與吸附位向之探討 62
5.3.1.1 螢光訊號觀察 62
5.3.1.2 BSA構形變化之討論 68
5.3.1.3 BSA吸附量探討 70
5.3.1.4 吸附位向之探討 71
5.3.2 BSA吸附結論 73
5.4 BAA(Bacillus amyloliquefaciens α-amylase)吸附 74
5.4.1 BAA構形變化、吸附量與吸附位向之探討 75
5.4.1.1 螢光訊號觀察 75
5.4.1.2 BAA構形變化之討論 81
5.4.1.3 BAA吸附量探討 82
5.4.1.4 吸附位向之探討 84
第六章 結論與建議 86
6.1 結論 86
參考文獻 89
附錄 100
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指導教授 阮若屈(Ruoh-Chyu Ruaan) 審核日期 2006-7-20
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