Electrode Surface Potential-Driven Protein Adsorption and Desorption through Modulation of Electrostatic, van der Waals, and Hydration Interactions.
Electrode Surface Potential-Driven Protein Adsorption and Desorption through Modulation of Electrostatic, van der Waals, and Hydration Interactions.
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DOI：
10.1021/acs.langmuir.1c00828
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发表时间：
2021-06-01
期刊：
影响因子：
--
通讯作者：
Schroën CGPH
中科院分区：
文献类型：
--
作者：
Fritz PA;Bera B;van den Berg J;Visser I;Kleijn JM;Boom RM;Schroën CGPH
当水溶液中的蛋白质暴露于固体基质时，它们会由于静电、范德华力和水合相互作用的动态相互作用而进行吸附，并且以相当不可逆的方式进行吸附，这使得蛋白质回收变得困难。在这里，我们使用金电极作为固体基质并调节表面电位以系统地诱导蛋白质吸附和部分解吸。我们使用不同的方法，如表面等离振子共振、原子力显微镜和电润湿，结果表明，将电极偏置到更负的电位（与 pH 6 时的开路电位相比，偏压 -0.4 V）会导致带负电的蛋白质 β-乳球蛋白的吸附势垒增加 6 kJ mol-1。此外，我们清楚地证明这是由于-0.06 V 的双层电势增加和水合排斥力的增加所致。这表明电势可以直接影响表面相互作用，从而诱导部分β-乳球蛋白解吸。这些观察结果可以作为生物传感器和分离技术的基础，这些技术仅使用一种触发器来引导蛋白质吸附和解吸，其能量需求较低，并且不会像标准蛋白质分离技术那样产生大量废物流。
When proteins in aqueous solutions are exposed to solid substrates, they adsorb due to the dynamic interplay of electrostatic, van der Waals, and hydration interactions and do so in a rather irreversible fashion, which makes protein recovery troublesome. Here, we use a gold electrode as the solid substrate and modulate the surface potential to systematically induce protein adsorption as well as partial desorption. We use different methods such as surface plasmon resonance, atomic force microscopy, and electrowetting and show that biasing the electrode to more negative potentials (by −0.4 V compared to the open-circuit potential at pH 6) results in an increased adsorption barrier of 6 kJ mol–1 for the negatively charged protein β-lactoglobulin. Further, we clearly demonstrate that this is due to an increased double layer potential of −0.06 V and an increase in hydration repulsion. This indicates that an electric potential can directly influence surface interactions and thus induce partial β-lactoglobulin desorption. These observations can be the basis for biosensors as well as separation technologies that use only one trigger to steer protein ad- and desorption, which is low in energy requirement and does not generate large waste streams, as is the case for standard protein separation technologies.
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