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Interaction of recombinant Factor VIII and the nonionic surfactant Tween 80 at interfaces.

机译：重组因子VIII与非离子表面活性剂Tween 80在界面处的相互作用。

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The role of the nonionic surfactant Tween 80 on the behavior of the therapeutic recombinant protein Factor VIII (rFVIII) was investigated at solid/liquid and air/water interfaces. In order to provide a model system to compare results obtained for the complicated rFVIII - Tween system, a well-characterized globular protein lysozyme was used. The experimental scheme involved the introduction of the protein and Tween to the adsorption substrate in different manners, either lysozyme - Tween together or in sequence as lysozyme followed by Tween or vice versa. It was observed that the addition of Tween together with lysozyme reduced the amounts adsorbed at hydrophobic surfaces, while no such reduction was observed on hydrophilic surfaces. A high Tween concentration was required to effect the removal of the lysozyme molecules from the hydrophobic surface and Tween was not effective in removing lysozyme from the hydrophilic surface at any concentration. These results suggest that the Tween - surface interaction is important in determining lysozyme adsorption. Similar observations were made for the rFVIII - Tween system at hydrophobic and hydrophilic silica interfaces. In this case, the presence of interfacial and solution Tween together resulted in complete prevention of rFVIII adsorption. Electrostatic forces were observed to be play an important role in rFVIII adsorption. The rFVIII - Tween interactions at solid interfaces were also evaluated using intrinsic fluorescence and biological activity measurements. Results obtained with respect rFVIII adsorbed mass, and structure or biological activity change upon adsorption, were evaluated in parallel. This parallel evaluation suggested that rFVIII adsorption on hydrophilic, negatively charged surfaces is likely to be highly ordered and oriented in a manner that retains the solvent accessibility of the active sites in rFVIII. On the other hand, rFVIII may adsorb to hydrophobic surfaces in different orientations, with a likelihood of surface induced unfolding. rFVIII - Tween interaction at the air/water interface was investigated separately. Surface tension data recorded for rFVIII - Tween mixtures suggested that Tween dominated the air/water interface as the Tween concentration was increased. Reduced interface-induced unfolding was observed at high Tween concentrations. These results were also thought to contribute to the reduction in rFVIII aggregation typically observed as a result of exposure to the air/water interface.
机译：在固体/液体和空气/水界面处，研究了非离子表面活性剂吐温80对治疗性重组蛋白VIII因子（rFVIII）行为的作用。为了提供一个模型系统来比较复杂的rFVIII-Tween系统获得的结果，使用了一种特征明确的球状蛋白溶菌酶。实验方案涉及以不同的方式将蛋白质和吐温引入溶菌酶-溶菌酶-吐温一起或依次作为溶菌酶，然后吐温，反之亦然。观察到吐温和溶菌酶的加入减少了疏水表面上的吸附量，而在亲水表面上没有观察到这种减少。需要高的吐温浓度以实现从疏水表面去除溶菌酶分子，并且吐温在任何浓度下都不能有效地从亲水表面去除溶菌酶。这些结果表明，吐温-表面相互作用在确定溶菌酶吸附中很重要。对于rFVIII-Tween系统在疏水和亲水二氧化硅界面处也有类似的观察结果。在这种情况下，界面和吐温溶液的存在共同导致了rFVIII吸附的完全阻止。观察到静电力在rFVIII吸附中起重要作用。固体界面上的rFVIII-Tween相互作用也使用固有荧光和生物活性测量进行了评估。平行评估了关于rFVIII吸附质量以及吸附后结构或生物学活性变化的结果。该平行评估表明，rFVIII在亲水性，带负电荷的表面上的吸附很可能是高度有序的和定向的，从而保留了rFVIII中活性位点的溶剂可及性。另一方面，rFVIII可能以不同的方向吸附到疏水表面上，可能会引起表面展开。 rFVIII-空气/水界面的吐温相互作用被单独研究。记录的rFVIII-Tween混合物的表面张力数据表明，随着Tween浓度的增加，Tween主导了空气/水界面。在高吐温浓度下观察到界面诱导的展开减少。还认为这些结果有助于减少通常由于暴露于空气/水界面而观察到的rFVIII聚集。

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