Adsorption of proteins at the liquid/air interface
Adsorption of proteins at the liquid/air interface
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DOI：
10.1021/jp9725036
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发表时间：
1998-01-08
影响因子：
3.3
通讯作者：
Miller, R
中科院分区：
文献类型：
--
作者：
Makievski, AV;Fainerman, VB;Miller, R
描述液体/流体界面上蛋白质吸附层的热力学方程是最近发表的理论的推广[J]。胶体界面学报，1993,26 [j]。在这个新理论中，考虑了焓（Flory-Huggins参数）和混合熵的非理想性，并考虑了蛋白质分子的电荷对表面压力的影响。用悬垂跌落实验（ADSA）得到的HA溶液的动力学和平衡表面张力数据对模型进行了验证，所得的等温线与实验数据吻合较好。所得的等温线参数、单分子表面积、HSA分子的电荷、吸附层厚度等值与文献中其他方法所得值接近。由此可见，HSA分子在溶液/空气界面几乎没有发生变性，并且占据约50 nm(2)的表面积，与吸附层中的填充无关，这符合三畴结构的概念。
Thermodynamic equations for describing protein adsorption layers at liquid/fluid interfaces are derived as a generalization of a theory published recently [J. Colloid Interface Sci. 1996, 183, 26]. In this new theory the nonideality of enthalpy (Flory-Huggins' parameter) and entropy of mixing are taken into account, and also the effect of the electric charge of the protein molecules on surface pressure is considered. The model is verified by experimental dynamic and equilibrium surface tension data for HA solutions obtained from pendent drop experiments (ADSA), The derived isotherm is in good agreement with the experimental data. The values of the isotherm parameters surface area per molecule, electric charge of the HSA molecule, and the adsorption layer thickness are close to values obtained by other methods in literature. It follows that HSA molecules undergo almost no denaturation at the solution/air interface and occupy a surface area of about 50 nm(2), independent of the packing in the adsorption layer, which is in agreement with the concept of a triple-domain structure.