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Electrochemical desorption of proteins from gold electrode surface

机译：蛋白质从金电极表面电化学解吸

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The goal of this study was to enable rational modulation of biological interfaces using electrochemical desorption of surface-bound proteins. Coupled, surface plasmon resonance (SPR) - electrochemistry instrument was used to monitor molecular assembly events on gold electrodes and to correlate these events with changes in electrochemical properties of the substrate. Model proteins, bovine serum albumin (BSA) and immunoglobulin G (IgG), were conjugated via carbodiimide (EDC) chemistry to a layer of mercaptoundecanoic acid (MUA) assembled on SPR sensor surface. Deposition of alkanethiols and proteins were monitored by ellipsometry and SPR techniques, and was further confirmed by cyclic voltammetry with potassium ferricyanide serving as a reporter molecule. The surface-bound proteins were completely removed by applying a reductive potential of - 1200 mV vs. Pt electrode in a physiological saline buffer. Importantly, the sequence of protein immobilization followed by desorption could be repeated multiple times, thus demonstrating ability to modulate interfacial properties. Controlled removal of protein molecules from electrode surfaces is envisioned to have important applications in affinity or cell-based biosensing, cellular micropatterning and cell sorting.
机译：这项研究的目的是通过使用表面结合蛋白的电化学解吸来合理调节生物界面。耦合的表面等离振子共振（SPR）-电化学仪器用于监测金电极上的分子组装事件，并将这些事件与基材电化学性能的变化关联起来。通过碳二亚胺（EDC）化学方法将模型蛋白，牛血清白蛋白（BSA）和免疫球蛋白G（IgG）偶联至在SPR传感器表面组装的巯基十一烷酸（MUA）层。通过椭圆偏光法和SPR技术监测链烷硫醇和蛋白质的沉积，并通过循环伏安法以铁氰化钾作为报告分子进一步证实。通过在生理盐水缓冲液中施加相对于Pt电极约1200 mV的还原电位，可以完全去除表面结合的蛋白质。重要的是，蛋白质固定后解吸的顺序可以重复多次，从而证明了调节界面特性的能力。预期从电极表面控制去除蛋白质分子将在亲和或基于细胞的生物传感，细胞微模式和细胞分选中具有重要的应用。

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