本研究利用螢光顯微鏡分析法 (fluorescence microscopy, FM)的觀測，配合表面壓-面積等溫線的量測，探討在來回壓縮-擴張界面的情況下，氣/液界面上dipalmitoyl phosphatidylcholine (DPPC)/albumin 及 DPPC/fibrinogen 混合分子層的行為，以了解血漿蛋白質對DPPC 之動態界面活性的抑制效應。
在壓縮界面的過程中，DPPC/血漿蛋白質混合分子層中的水溶性蛋白質，會因界面密度的升高而被擠出氣/液界面。在後續擴張界面的過程中，血漿蛋白質則會再吸附至氣/液界面上，並影響界面上受壓縮之DPPC 單分子層的再分佈行為。然而血漿蛋白質在氣/液界面上的再吸附行為，與液相中的濃度有關。當濃度較高時，蛋白質分子的再吸附行為會較明顯，且fibrinogen在氣/液界面上的再吸附行為較albumin 顯著。此外，albumin 及fibrinogen 分子會擾亂界面壓縮時DPPC 分子的排列與聚集。而由觀察界面壓縮過程中DPPC分子液體凝縮相聚集結構的生成，發現fibrinogen 對DPPC 分子排列的影響較albumin 明顯。
實驗結果也顯示，在界面壓縮過程中的血漿蛋白質被擠出行為，會導致界面上自由DPPC 分子的損失。且當界面上蛋白質分子的量越多時，造成的DPPC 分子損失就越顯著。而在相同的液相濃度下，fibrinogen 分子被擠出界面所伴隨的DPPC 分子損失量較albumin 分子被擠出時多。此外，在界面的壓縮-擴張過程中，混合分子層中的血漿蛋白質可能和DPPC 作用形成複合物。因此，在FM 影像中，當界面擴張程度較顯著時，於100及10ppm 血漿蛋白質水溶液的氣/液界面上，可觀察到DPPC/血漿蛋白質複合物的結構。DPPC 與血漿蛋白質之間的交互作用，可以解釋在壓縮界面時，自由DPPC 分子為何會隨著蛋白質分子的脫附而離開氣/液界面，使得DPPC 的動態界面活性受到抑制。

The behavior of mixed dipalmitoyl phosphatidylcholine (DPPC)/albumin and DPPC/fibrinogen layers at cyclic air/liquid interfaces was investigated by the fluorescence microscopy (FM) observation with the measurements of surface pressure-area isotherms, in order to understand the inhibitory effects of plasma proteins on the dynamic surface activity of DPPC.
During the interface compression stage, the soluble proteins in the mixed DPPC/plasma protein layers were expelled from air/liquid interfaces because of the increased surface density. During the following interface expansion stage, the proteins would readsorb onto air/liquid interfaces, affecting the respreading behavior of the compressed DPPC monolayer. However, the readsorption behavior of plasma proteins at air/liquid interfaces was related to the subphase concentration. The readsorption behavior of plasma proteins was more significant when the subphase concentration was higher, and fibrinogen showed more pronounced readsorption behavior than albumin. Moreover, albumin and fibrinogen would disturb the arrangement and packing of DPPC molecules during the interface compression stage. With the observation of the DPPC liquid-condensed domain formation during the interface compression stage, one could find that fibrinogen had a more pronounced influence than albumin on the arrangement of DPPC molecules.
The results also showed that the squeeze-out of plasma proteins during the interface compression stage would induce the loss of free DPPC molecules at interfaces. In addition, the induced loss of free DPPC molecules became significant when more protein molecules were available at interfaces. With the same subphase concentration, the fibrinogen exclusion induced a more significant loss of free DPPC molecules than the albumin exclusion. Furthermore, plasma proteins might interact with DPPC in the mixed layers to form complexes during the interface compression-expansion process. As a result, one could observe the DPPC-plasma protein complex domains in FM images at air/liquid interfaces of 100 and 10 ppm plasma protein solutions, when the interface expansion became pronounced. The interaction between DPPC and plasma proteins may explain the induced loss of free DPPC molecules at air/liquid interfaces by the expelled plasma proteins during the interface compression stage, which resulted in the inhibition of DPPC dynamic surface activity.

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