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首页> 外文期刊>Electrochimica Acta >Interactions between Human Antibodies and Synthetic Conformational Peptide Epitopes: Innovative Approach for Electrochemical Detection of Biomarkers of Multiple Sclerosis at Platinum Electrodes
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Interactions between Human Antibodies and Synthetic Conformational Peptide Epitopes: Innovative Approach for Electrochemical Detection of Biomarkers of Multiple Sclerosis at Platinum Electrodes

机译:人类抗体与合成构象肽表位之间的相互作用:铂电极上多发性硬化生物标记物电化学检测的创新方法。

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摘要

The detection of human antibodies of Multiple Sclerosis patients was investigated based on the electrochemical oxidation of a synthetic antigenic probe, a glycopeptide Fc-CSF114(Glc) bearing a ferrocenyl moiety. Electrochemical measurements were carried out at platinum microband electrodes without any electrode surface modification. A microfluidic device was designed in order to both minimize peptide consumption and increase the number of experiments with low volumes of samples. The specific interactions between Fc-CSF114(Glc) and antibodies were evidenced through comparison with electrochemical responses obtained from the ferrocenyl unglycosylated peptide Fc-CSF114 used as negative control. The interactions between Fc-CSF114(Glc) and autoantibodies were characterized by a shift of the oxidation potential towards positive values. A mechanism for peptide oxidation was proposed based on a diffusion control of mass transport and the formation of adsorbed layers able to mediate electron transfer. Results showed efficient antigen-antibody recognition without any electrode grafting or further addition of labels in solution. Preliminary tests using human sera from Multiple Sclerosis patients and healthy donors validated this new approach aimed at developing innovative and fast diagnostic tools, based on electrochemical synthetic antigenic probes. (C) 2015 Elsevier Ltd. All rights reserved.
机译:基于合成抗原探针,带有二茂铁基部分的糖肽Fc-CSF114(Glc)的电化学氧化,研究了多发性硬化症患者的人抗体检测。在没有任何电极表面修饰的情况下,在铂微带电极上进行电化学测量。设计了一种微流控设备,以最大程度地减少肽消耗并增加少量样品的实验次数。通过与从用作阴性对照的二茂铁基未糖基化肽Fc-CSF114获得的电化学反应进行比较,证明了Fc-CSF114(Glc)与抗体之间的特异性相互作用。 Fc-CSF114(Glc)与自身抗体之间的相互作用以氧化电位向正值的移动为特征。提出了一种基于质量传输的扩散控制和能够介导电子转移的吸附层形成的肽氧化机制。结果显示有效的抗原-抗体识别无需任何电极接枝或在溶液中进一步添加标记。使用多发性硬化症患者和健康捐献者的人类血清进行的初步测试验证了这种新方法,该方法旨在开发基于电化学合成抗原探针的创新且快速的诊断工具。 (C)2015 Elsevier Ltd.保留所有权利。

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