Aptamer-MIP hybrid receptor for highly sensitive electrochemical detection of prostate specific antigen
Aptamer-MIP hybrid receptor for highly sensitive electrochemical detection of prostate specific antigen
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DOI：
10.1016/j.bios.2015.08.043
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发表时间：
2016-01-15
影响因子：
12.6
通讯作者：
Bowen, Jenna L.
中科院分区：
文献类型：
--
作者：
Jolly, Pawan;Tamboli, Vibha;Bowen, Jenna L.
本研究报道了一种基于生物分子识别元件和分子印迹融合的新型合成受体传感器的设计和评价，以克服传统蛋白质印迹所面临的一些挑战。在固定在金电极表面之前，将具有前列腺特异性抗原（PSA）亲和力的巯基化DNA适体与PSA络合。在复合物周围控制多巴胺的电聚合，既可以捕获复合物，将适体保持在或接近其结合构象，又可以定位传感器表面的PSA结合位点。在去除PSA后，提出分子印迹聚合物（MIP）腔将与嵌入的适体协同作用形成杂交受体（apta-MIP），其识别性能优于单独的适体。电化学阻抗谱（EIS）用于评价PSA随后与apta-MIP表面的再结合。apta-MIP传感器对PSA的检测灵敏度在100 pg/ml ~ 100 ng/ml范围内呈线性响应，检测限为1 pg/ml，是单一适体传感器的3倍。此外，该传感器与同源蛋白（人Kallilcrein 2）的交叉反应性较低，对人血清白蛋白（HSA）的反应较低，这表明该传感器可能对血清蛋白的非特异性结合具有弹性。(C) 2015年作者。这是一篇基于CC by许可（http://creativecommons.org/licenses/by/4.0/）的开放获取文章。
This study reports the design and evaluation of a new synthetic receptor sensor based on the amalgamation of biomolecular recognition elements and molecular imprinting to overcome some of the challenges faced by conventional protein imprinting. A thiolated DNA aptamer with established affinity for prostate specific antigen (PSA) was complexed with PSA prior to being immobilised on the surface of a gold electrode. Controlled electropolymerisation of dopamine around the complex served to both entrap the complex, holding the aptamer in, or near to, it's binding conformation, and to localise the PSA binding sites at the sensor surface. Following removal of PSA, it was proposed that the molecularly imprinted polymer (MIP) cavity would act synergistically with the embedded aptamer to form a hybrid receptor (apta-MIP), displaying recognition properties superior to that of aptamer alone. Electrochemical impedance spectroscopy (EIS) was used to evaluate subsequent rebinding of PSA to the apta-MIP surface. The apta-MIP sensor showed high sensitivity with a linear response from 100 pg/ml to 100 ng/ml of PSA and a limit of detection of 1 pg/ml, which was three-fold higher than aptamer alone sensor for PSA. Furthermore, the sensor demonstrated low cross-reactivity with a homologous protein (human Kallilcrein 2) and low response to human serum albumin (HSA), suggesting possible resilience to the non-specific binding of serum proteins. (C) 2015 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).