Department of Colloid Chemistry, St. Petersburg State University, Universitetsky Pr. 26, St. Petersburg 198504, Russia.
Chemical Engineering Department, National Taiwan University of Science and Technology, 43 Keelung Road, Section 4, Taipei 106, Taiwan.
Langmuir. 2023 Jun 20;39(24):8424-8434. doi: 10.1021/acs.langmuir.3c00480. Epub 2023 Jun 6.
The strong influence of an amphiphilic polyelectrolyte, poly(,-diallyl--hexyl--methylammonium chloride), on the surface properties of solutions of globular proteins (lysozyme, β-lactoglobulin, bovine serum albumin, and green fluorescent protein) depends on the protein structure and allows elucidation of the contribution of hydrophobic interactions in the protein-polyelectrolyte complex formation at the liquid-gas interface. At the beginning of adsorption, the surface properties are determined by the unbound amphiphilic component, but the influence of the protein-polyelectrolyte complexes of high surface activity increases at the approach to equilibrium. The kinetic dependencies of the dilational dynamic surface elasticity with one or two local maxima give a possibility to distinguish clearly between different steps of the adsorption process and to trace the formation of the distal region of the adsorption layer. The conclusions from the surface rheological data are corroborated by ellipsometric and tensiometric results.
两亲性聚电解质聚（-二烯丙基- 六烷基- 甲基氯化铵）对球状蛋白质（溶菌酶、β-乳球蛋白、牛血清白蛋白和绿色荧光蛋白）溶液表面性质的强烈影响取决于蛋白质结构，并允许阐明疏水性相互作用在蛋白质-聚电解质复合物在气-液界面形成中的贡献。在吸附的初始阶段，表面性质由未结合的两亲性组分决定，但随着接近平衡，高表面活性的蛋白质-聚电解质复合物的影响增加。具有一个或两个局部最大值的扩张动态表面弹性的动力学依赖性使得能够清楚地区分吸附过程的不同步骤，并追踪吸附层的远域的形成。表面流变数据的结论得到了椭圆偏振和张力计结果的证实。
