本研究利用Brewster angle microscopy (BAM)配合表面壓-面積與表面電位-面積等溫線的分析，探討於動態壓縮/擴張氣液界面面積的情況下，氣液界面上DPPC/albumin混合分子層的行為。在第一次壓縮混合分子層的過程中，BAM的影像顯示吸附於界面上的albumin分子層，並未能完全與分佈於氣液界面上的DPPC單分子層混合。而在albumin的存在下，氣液界面上的DPPC分子會聚集成亮點domains，或以固態相的狀態存在。此外，由BAM也可觀察到明亮且均勻的albumin聚集domains。
在空氣/10 ppm albumin溶液的氣液界面上，於第二及第三次壓縮DPPC/albumin混合分子層的過程中，可發現扭曲的DPPC 液體-凝縮相 domains。這結果顯示DPPC與albumin雖然未能達到分子層級的混合，但albumin的存在明顯造成界面上DPPC分子聚集行為的改變。
在第二及第三次壓縮混合分子層的過程中，若進一步壓縮分子層至表面壓20 mN/m左右，由BAM可觀察到網狀結構的形成，而此結構的特性會受到albumin濃度的影響。在較高的albumin濃度下，會形成較緊密的網狀結構；反之，所形成的網狀結構則較為鬆散。網狀結構的形成，代表albumin會對DPPC固態相的形態造成改變。
此外，在連續壓縮/擴張分子層的過程中，利用BAM可觀察到界面上DPPC自由分子的減少。在相同表面壓下，於第三次壓縮過程中所出現富含DPPC的domains，明顯比在第二次壓縮過程中所出現的數量還少。
實驗結果顯示， DPPC於氣液界面上的界面活性受到albumin的抑制，可能與DPPC自由分子的損失，以及形成不規則的聚集domains有關。

The behavior of mixed DPPC/albumin layers at air/liquid interfaces under dynamic compression-expansion conditions has been investigated by the analysis of surface pressure-area isotherms with Brewster angle microscopy (BAM) observations. During the initial first compression stage, BAM images revealed that the adsorbed protein layer was not mixed homogeneously with the spread DPPC monolayer. DPPC domains seemed to aggregate into bright dots or become solid state in the presence of proteins. The bright homogeneous protein islands were also observed.
During the second and third compression stages, distorted DPPC liquid condensed domains were observed in the mixed spread DPPC/adsorbed albumin layer on a 10 ppm albumin subphase. It indicated that although albumin and DPPC were not mixed very well in the molecular scale, the existence of albumin apparently disturbed the packing (characteristic length) of DPPC molecules at the interface.
For further compression in the second and third compression stages, one could observe the formation of network structures at ~ 20 mN/m. The characteristic of network structures also depended on the bulk albumin concentrations. Taut and slack network structures were detected at higher and lower albumin concentrations, respectively. The formation of network structures implied the disruption of the DPPC solid state morphology by albumin.
The decrease of free DPPC molecules at the interface upon consecutive compression/expansion cycles was supported by BAM observations. At same surface pressures, it appeared that the fraction of DPPC-rich domains observed during the third compression stage decreased in comparison to that observed during the second compression stage.
In general, the results indicated that the albumin inhibition of DPPC surface active at the interface may be contributed to the decrease of free DPPC molecule fraction at the interface and the formation of the other irregular aggregated at the interface, which therefore change the morphology of mixed layer.

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