Department of Biological Sciences, Faculty of Science and Technology, Sunway University, No. 5, Jalan Universiti, Bandar Sunway, Petaling Jaya, Selangor 46150, Malaysia ; Department of Chemistry, Faculty of Science, University of Malaya, Kuala Lumpur 50603, Malaysia.
Department of Chemistry, Faculty of Science, University of Malaya, Kuala Lumpur 50603, Malaysia.
Nanoscale Res Lett. 2014 May 7;9(1):218. doi: 10.1186/1556-276X-9-218. eCollection 2014.
The fluid mosaic model of Singer and Nicolson in 1972 shows how proteins are embedded in membranes. To elucidate the interactions between proteins and the surrounding lipids, stearic acid (SA) and bovine serum albumin (BSA) were used as lipid-protein components to mimic the normal membrane bilayer environment using the Langmuir-Blodgett technique. Surface pressure (π)-molecular area (A) isotherms were recorded for the SA monolayer in the presence of BSA on water. The mixed monolayer was successfully transferred onto an oxidized silicon wafer and imaged by tapping mode atomic force microscopy (AFM). Miscibility, compressibility and thermodynamic stability of the mixed system were examined. A large negative deviation of A ex, together with the minimum value of ΔG ex, was observed when the mole fraction of BSA (X BSA) was 0.8, indicating this to be the most stable mixture. In a compressibility analysis, X BSA was observed at below 50 mN m(-1), denoting a liquid-expanded phase and showing the occurrence of a strong interaction of SA with BSA molecules in this phase. AFM observations supported the quantitative data indicating that BSA was strongly attracted onto the membrane surface as predicted.
1972 年，辛格和尼科利森提出的流动镶嵌模型表明了蛋白质是如何嵌入膜中的。为了阐明蛋白质与周围脂质之间的相互作用，使用硬脂酸（SA）和牛血清白蛋白（BSA）作为脂质-蛋白质成分，使用 Langmuir-Blodgett 技术模拟正常的膜双层环境。在水存在下，记录了 SA 单层中 BSA 的表面压力（π）-分子面积（A）等温线。成功地将混合单层转移到氧化硅晶片上，并通过轻敲模式原子力显微镜（AFM）对其进行成像。对混合体系的混溶性、可压缩性和热力学稳定性进行了研究。当 BSA 的摩尔分数（XBSA）为 0.8 时，观察到 Aex 的大负偏差，以及 ΔGex 的最小值，表明这是最稳定的混合物。在可压缩性分析中，在低于 50 mN m-1 的 XBSA 处观察到，表明存在液体膨胀相，并表明在该相中 SA 与 BSA 分子之间发生了强烈的相互作用。AFM 观察结果支持定量数据，表明 BSA 如预测的那样强烈地被吸引到膜表面上。
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