| 研究生: |
李寶琴 Li, Bao-Chin |
|---|---|
| 論文名稱: |
以反射吸收式紅外光譜分析技術探討氣/液界面上DPPC/Albumin混合分子層行為的研究 A Study of the Mixed DPPC/Albumin Layer Behavior at the Air/Liquid Interfaces by Infrared Reflection-Absorption Spectroscopy |
| 指導教授: |
張鑑祥
chang, chien - hsiang |
| 學位類別: |
碩士 Master |
| 系所名稱: |
工學院 - 化學工程學系 Department of Chemical Engineering |
| 論文出版年: | 2004 |
| 畢業學年度: | 92 |
| 語文別: | 中文 |
| 論文頁數: | 112 |
| 中文關鍵詞: | 氣液界面 、單分子層 、反射吸收式紅外光譜分析技術 |
| 外文關鍵詞: | DPPC, albumin, IRRAS, IR |
| 相關次數: | 點閱:111 下載:2 |
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中文摘要
本研究利用反射吸收式紅外光譜分析技術,探討於動態壓縮-擴張氣液界面面積的情況下,albumin對DPPC分子層行為的影響。
在空氣/albumin水溶液界面上,DPPC單分子層的碳氫鏈排列會因為albumin水溶液濃度的不同而受到不同程度的影響。當albumin水溶液濃度為10 ppm時,在壓縮-擴張氣液界面的過程中,DPPC碳氫鏈的排列行為與氣液界面上單純只有DPPC存在時的行為相似,顯示低濃度的albumin水溶液對氣液界面上DPPC碳氫鏈的排列位向影響較小,且在經過第一次壓縮後,於氣液界面擴張過程中albumin分子再吸附於界面上的量較少。反之,高濃度的albumin水溶液會使界面上DPPC分子排列更緊密,且分子碳氫鏈的排列位向更垂直於氣液界面,而存於氣液界面上自由DPPC分子的量,隨著albumin濃度增加而減少。此外,在高濃度的albumin水溶液中,albumin吸附於氣液界面上的速率較快,使得在三次壓縮擴張氣液界面的過程中,界面上自由的DPPC分子持續處於排列較緊密的狀態。
經由改變DPPC及albumin分子層的分佈次序,並從事後續分子層的壓縮-擴張實驗,也發現界面上DPPC分子碳氫鏈的排列位向及緊密程度會受到分佈次序的影響。
Abstract
This study investigated the influence of albumin on dipalmitoyl phosphatidylcholine (DPPC) monolayer behavior at cyclic air/liquid interfaces by infrared reflection-absorption spectroscopy (IRRAS).
For a DPPC monolayer at the interfaces of air/albumin solutions, the orientation of DPPC hydrocarbon chains was affected with the extent dependent on albumin concentration. When the albumin concentration was 10 ppm, during the interface compression/expansion, the orientation of DPPC hydrocarbon chains was similar to that obtained for a DPPC monolayer on a pure water subphase. This result indicated that with lower albumin concentrations, the orientation of DPPC hydrocarbon chains was affected insignificantly and the amount of albumin re-adsorption during interface expansion could be neglected. On the contrary, with higher albumin concentrations, DPPC molecules at the interface were close-packed and the orientation of DPPC hydrocarbon chains became vertical to the interface. The amount of free DPPC molecules at interfaces was found to decrease with increasing albumin concentration. Moreover, for an albumin subphase with higher concentrations, the adsorption rate of albumin at the interface was faster. As a result, the free DPPC molecules at the interface were always close-packed during three cycles of interface compression/expansion.
By changing the spreading order of DPPC and albumin at the interface to form mixed monolayers, it was found that the hydrocarbon chain orientation and surface density of DPPC molecules were affected by the spreading order, as judging from the experimental results.
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