Interpretation of Protein Adsorption through Its Intrinsic Electric Charges: A Comparative Study Using a Field-Effect Transistor, Surface Plasmon Resonance, and Quartz Crystal Microbalance
Interpretation of Protein Adsorption through Its Intrinsic Electric Charges: A Comparative Study Using a Field-Effect Transistor, Surface Plasmon Resonance, and Quartz Crystal Microbalance
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DOI：
10.1021/la302977s
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发表时间：
2012-10-16
期刊：
影响因子：
3.9
通讯作者：
Miyahara, Yuji
中科院分区：
文献类型：
--
作者：
Goda, Tatsuro;Miyahara, Yuji
我们描述了高灵敏度的检测蛋白质的非特异性吸附到1-十一烷乙撑醇自组装单层（SAM）形成的金电极通过并行分析，使用场效应晶体管（FET），表面等离子体共振（SPR），和石英晶体微天平（QCM）传感器。PET传感器检测在电极/溶液界面处吸附的蛋白质的固有电荷，将电荷密度的变化真实的实时地转换成电位信号，而不需要标记。特别是，使用Debye-Huckel模型，电位偏移的程度与吸附的白蛋白和β-酪蛋白的干质量成比例。的FET信号与SPR和QCM数据的比较，通过观察信号之间的相关斜率的特征断点提供的信息的表面结合的蛋白质的构象和取向。这些斜率转换反映了一个多阶段的过程，发生在蛋白质吸附作为蛋白质浓度的函数，包括临时覆盖，薄膜脱水，和单层冷凝。FET生物传感器，结合SPR和QCM，代表了一种新的技术，用于询问蛋白质-材料相互作用的定量和定性。
We describe the highly sensitive detection of the nonspecific adsorption of proteins onto a 1-undecanethiol self-assembled monolayer (SAM)-formed gold electrode by parallel analysis using field effect transistor (FET), surface plasmon resonance (SPR), and quartz crystal microbalance (QCM) sensors. The PET sensor detects the innate electric charges of the adsorbed protein at the electrode/solution interface, transforming the change in charge density into a potentiometric signal in real time, without the requirement for labels. In particular, using the Debye-Huckel model, the degree of potential shift was proportional to the dry mass of adsorbed albumin and beta-casein. A comparison of the FET signal with SPR and QCM data provided information on the conformation and orientation of the surface-bound protein by observing characteristic break points in the correlation slopes between the signals. These slope transitions reflect a multistage process that occurs upon protein adsorption as a function of protein concentration, including interim coverage, film dehydration, and monolayer condensation. The FET biosensor, in combination with SPR and QCM, represents a new technology for interrogating protein-material interactions both quantitatively and qualitatively.