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Functionalized carbon nanotubes for detecting viral proteins

机译：用于检测病毒蛋白的功能化碳纳米管

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摘要

We investigated the biocompatibility, specificity, and activity of a ligand-receptor-protein system covalently bound to oxidized single-walled carbon nanotubes (SWNTs) as a model proof-of-concept for employing such SWNTs as biosensors. SWNTs were functionalized under ambient conditions with either the Knob protein domain from adenovirus serotype 12 (Ad 12 Knob) or its human cellular receptor, the CAR protein, via diimide-activated amidation. We confirmed the biological activity of Knob protein immobilized on the nanotube surfaces by using its labeled conjugate antibody and evaluated the activity and specificity of bound CAR on SWNTs, first, in the presence of fluorescently labeled Knob, which interacts specifically with CAR, and second, with a negative control protein, YieF, which is not recognized by biologically active CAR proteins. In addition, current-gate voltage (I-V-g) measurements on a dozen nanotube devices explored the effect of protein binding on the intrinsic electronic properties of the SWNTs, and also demonstrated the devices' high sensitivity in detecting protein activity. All data showed that both Knob and CAR immobilized on SWNT surfaces fully retained their biological activities, suggesting that SWNT-CAR complexes can serve as biosensors for detecting environmental adenoviruses..
机译：我们研究了共价键合到氧化单壁碳纳米管（SWNTs）的配体-受体-蛋白质系统的生物相容性，特异性和活性，作为将此类SWNTs用作生物传感器的模型概念验证。在环境条件下，SWNT通过二酰亚胺活化的酰胺化作用被腺病毒血清型12的Knob蛋白结构域（Ad 12 Knob）或其人细胞受体CAR蛋白功能化。我们通过使用其标记的偶联抗体来确认固定在纳米管表面的旋钮蛋白的生物活性，并评估结合的CAR在SWNT上的活性和特异性，首先是在荧光标记的旋钮的存在下，该旋钮与CAR特异性相互作用，其次，带有阴性对照蛋白YieF，而该蛋白不能被具有生物活性的CAR蛋白识别。此外，在十二个纳米管器件上进行的电流门电压（I-V-g）测量探索了蛋白质结合对单壁碳纳米管固有电子性能的影响，还证明了该器件在检测蛋白质活性方面具有很高的灵敏度。所有数据表明固定在SWNT表面上的旋钮和CAR都完全保留了它们的生物学活性，这表明SWNT-CAR复合物可以用作检测环境腺病毒的生物传感器。

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