Department of Chemistry, University of Oxford, South Parks Road, Oxford, OX1 3QZ, United Kingdom.
Department of Chemistry, University of Otago, Dunedin 9054, New Zealand.
Anal Chem. 2023 Mar 14;95(10):4721-4727. doi: 10.1021/acs.analchem.2c05398. Epub 2023 Mar 1.
We introduce a facile assessment of binding kinetics at bioreceptive redox-active interfaces as a means of quantifying target proteins. This is achieved by monitoring the redox capacitance () of a receptor-modified conductive polymer interface under continuous flow. Exemplified with the quantification of C-reactive protein (CRP), capacitance analyses resolve both the association and dissociation regimes in real-time. Significantly, the rate of electrochemical signal change within the association regime is a sensitive function of target concentration, enabling marker assaying down to picomolar levels, comparable to end-point assays, in 15 s. This reagentless proof-of-principle methodology is envisioned to be widely applicable to the facile quantification of a range of other pertinent, clinically relevant targets.
我们介绍了一种在生物亲和氧化还原活性界面上评估结合动力学的简便方法,可用于定量目标蛋白。该方法通过在连续流动下监测受体修饰的导电聚合物界面的氧化还原电容 ( ) 来实现。以 C 反应蛋白 (CRP) 的定量为例,电容分析实时解析结合和解离区域。重要的是,在结合区域内电化学信号变化的速率是目标浓度的敏感函数,使标记分析能够在 15 秒内达到皮摩尔级别的检测限,与终点分析相当。这种无需试剂的原理验证方法预计将广泛适用于其他相关的、临床相关的目标的简便定量。