Belicky Stefan, Černocká Hana, Bertok Tomas, Holazova Alena, Réblová Kamila, Paleček Emil, Tkac Jan, Ostatná Veronika
Institute of Chemistry, Slovak Academy of Sciences, Dubravska cesta 9, 845 38 Bratislava, Slovak Republic.
Institute of Biophysics, Czech Academy of Sciences, Kralovopolská 135, 612 65 Brno, Czech Republic.
Bioelectrochemistry. 2017 Oct;117:89-94. doi: 10.1016/j.bioelechem.2017.06.005. Epub 2017 Jun 19.
In recent decades, it has become clear that most of human proteins are glycosylated and that protein glycosylation plays an important role in health and diseases. At present, simple, fast and inexpensive methods are sought for clinical applications and particularly for improved diagnostics of various diseases, including cancer. We propose a label- and reagent-free electrochemical method based on chronopotentiometric stripping (CPS) analysis and a hanging mercury drop electrode for the detection of interaction of sialylated protein biomarker a prostate specific antigen (PSA) with two important lectins: Sambucus nigra agglutinin (SNA) and Maackia amurensis agglutinin (MAA). Incubation of PSA-modified electrode with specific SNA lectin resulted in an increase of CPS peak H of the complex as compared to this peak of individual PSA. By adjusting polarization current and temperature, PSA-MAA interaction can be either eliminated or distinguished from the more abundant PSA-SNA complex. CPS data were in a good agreement with the data obtained by complementary methods, namely surface plasmon resonance and fluorescent lectin microarray. It can be anticipated that CPS will find application in glycomics and proteomics.
近几十年来，很明显大多数人类蛋白质都被糖基化，并且蛋白质糖基化在健康和疾病中起着重要作用。目前，正在寻找简单、快速且廉价的方法用于临床应用，特别是用于改进包括癌症在内的各种疾病的诊断。我们提出了一种基于计时电位溶出（CPS）分析和悬汞滴电极的无标记、无试剂的电化学方法，用于检测唾液酸化蛋白生物标志物前列腺特异性抗原（PSA）与两种重要凝集素：黑接骨木凝集素（SNA）和龙牙草凝集素（MAA）的相互作用。与单独的PSA的CPS峰H相比，用特异性SNA凝集素孵育PSA修饰电极会导致复合物的CPS峰H增加。通过调节极化电流和温度，可以消除PSA-MAA相互作用，或者将其与更丰富的PSA-SNA复合物区分开来。CPS数据与通过互补方法（即表面等离子体共振和荧光凝集素微阵列）获得的数据高度一致。可以预期CPS将在糖组学和蛋白质组学中得到应用。
