本研究利用螢光顯微鏡法（fluorescence microscopy, FM）配合表面壓-面積等溫線的量測，探討於連續來回壓縮-擴張界面的條件下，牛血漿白蛋白（bovine serum albumin, BSA）對氣/液界面上 dipalmitoyl phosphatidylcholine (DPPC)/hexadecyltrimethylammonium- hexadecylsulfate (HTMA-HS)（莫耳比3:1）混合單分子層行為的影響。結果顯示DPPC和HTMA-HS可在氣/液界面上互相混合，且有很強的分子間交互作用。此外，添加的HTMA-HS可改善DPPC單分子層崩潰後的再分佈性。
在BSA吸附分子層存在之氣/液界面上分佈DPPC分子形成單分子層後，在壓縮界面的過程中，BSA的脫附會導致界面上DPPC分子的損失。當界面上BSA的量越多時， DPPC 分子的損失就越顯著。由FM影像可觀察到，在混合分子層的壓縮-擴張過程中，BSA會和DPPC分子形成複合物。DPPC 與BSA之間的交互作用可以解釋在BSA脫附的過程中DPPC 分子的損失，使得DPPC分子的動態界面活性受到抑制。
在BSA吸附分子層存在之氣/液界面上分佈HTMA-HS分子形成單分子層後，於連續來回壓縮-擴張界面的條件下，HTMA-HS分子的損失遠比DPPC分子顯著，即HTMA-HS分子容易隨BSA離開氣/液界面，導致界面上HTMA-HS分子的損失，使得HTMA-HS分子的動態界面活性受到抑制。HTMA-HS分子的損失可能與帶正電的頭基HTMA+和帶負電的BSA因靜電相吸，或HTMA-HS分子之碳氫鏈與BSA疏水結構的交互作用有關。因此當BSA離開界面時，也造成HTMA-HS分子的損失。且BSA的吸附量越多，損失的HTMA-HS分子就越多。
在BSA吸附分子層存在之氣/液界面上同時分佈DPPC和HTMA-HS分子形成混合單分子層後，發現BSA抑制單分子層動態界面活性的能力變弱，在BSA脫附的過程中，單分子層的分子損失較不顯著。推測因DPPC與HTMA-HS之間很強的分子間交互作用，使混合單分子層能穩定存在於氣/液界面上，較不易受到BSA的影響。此外，在有BSA的環境下，HTMA-HS仍有助於DPPC單分子層崩潰後的再分佈性。

In this study, the effects of bovine serum albumin (BSA) on the mixed dipalmitoyl phosphatidylcholine (DPPC)/hexadecyltrimethyl- ammonium-hexadecylsulfate (HTMA-HS) (molar ratio = 3:1) monolayer behavior at cyclic air/liquid interfaces were investigated by the fluorescence microscopy (FM) with the measurements of surface pressure-area isotherms. The results showed that DPPC and HTMA-HS were miscible at the air/water interface. In addition, added HTMA-HS could improve the respreading ability of the collapsed DPPC monolayer.
When spreading DPPC molecules onto the air/liquid interface with an adsorbed BSA layer, it was revealed the BSA desorption during the interface compression stage would induce the loss of DPPC molecules at the interface. The higher amount of BSA at the interface, the more pronounced loss of DPPC molecules. During the compression-expansion process for the mixed layers, one could observe from the FM images that BSA would form complexes with DPPC molecules. The interaction between DPPC and BSA could explain the DPPC molecule loss during the BSA desorption process, resulting in the inhibited dynamic surface activity of DPPC molecules.
After spreading HTMA-HS molecules onto the air/liquid interface with an adsorbed BSA layer, under the condition of continuous interface compression-expansion, it was found that the loss of HTMA-HS molecules was more pronounced than that of DPPC molecules. That is, HTMA-HS easily left the air/liquid interface with BSA, causing the loss of HTMA-HS molecules at the interface and the inhibited dynamic surface activity of HTMA-HS molecules. The loss of HTMA-HS molecules was probably related to the electrostatic interaction between the positively charged headgroup, HTMA+, and the negatively charged BSA or to the interaction between the hydrocarbon chains of HTMA-HS molecules and the hydrophobic part of BSA. Therefore, when BSA molecules left the interface, the loss of HTMA-HS molecules resulted. The higher amount of adsorbed BSA, the more pronounced loss of HTMA-HS molecules.
After spreading DPPC and HTMA-HS molecules onto the air/liquid interface with an adsorbed BSA layer, it was found that the ability of BSA to inhibit the dynamic surface activity of a monolayer was lowered. During the BSA desorption process, the molecule loss of the monolayer was less significant. It was proposed that the mixed monolayer could stably stay at the air/liquid interface due to the strong interaction between DPPC and HTMA-HS, and was thus less affected by BSA. Furthermore, in the presence of BSA, HTMA-HS could still improve the respreading ability of the collapsed DPPC monolayer.

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