Quantification of the affinities and kinetics of protein interactions using silicon nanowire biosensors.
Quantification of the affinities and kinetics of protein interactions using silicon nanowire biosensors.
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DOI：
10.1038/nnano.2012.82
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发表时间：
2012-05-27
影响因子：
38.3
通讯作者：
中科院分区：
文献类型：
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监测蛋白质相互作用的结合亲和力和动力学对于临床诊断和药物开发非常重要，因为此类信息用于识别新的候选治疗药物。表面等离子体共振是目前用于此类分析的标准方法，但这受到低灵敏度和低通量分析的限制。在这里，我们证明硅纳米线场效应晶体管可以用作生物传感器来测量蛋白质-配体结合亲和力和动力学，灵敏度低至飞摩尔浓度。基于这种传感机制，我们开发了一个分析模型来校准传感器响应并量化两个代表性蛋白质-配体结合对的分子结合亲和力。通过监测反应动力学来确定蛋白质-配体对的结合和解离的速率常数，这表明硅纳米线场效应晶体管可以很容易地用作高通量生物传感器来量化蛋白质相互作用。
Monitoring the binding affinities and kinetics of protein interactions is important in clinical diagnostics and drug development because such information is used to identify new therapeutic candidates. Surface plasmon resonance is at present the standard method used for such analysis, but this is limited by low sensitivity and low-throughput analysis. Here, we show that silicon nanowire field-effect transistors can be used as biosensors to measure protein–ligand binding affinities and kinetics with sensitivities down to femtomolar concentrations. Based on this sensing mechanism, we develop an analytical model to calibrate the sensor response and quantify the molecular binding affinities of two representative protein–ligand binding pairs. The rate constant of the association and dissociation of the protein–ligand pair is determined by monitoring the reaction kinetics, demonstrating that silicon nanowire field-effect transistors can be readily used as high-throughput biosensors to quantify protein interactions.
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影响因子：
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作者：
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通讯作者：
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作者：
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