Recognition of Glycoprotein Peroxidase via Con A-Carrying Self-Assembly Layer on Gold
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- 作者：Songqin Liu ; Kewei Wang ; Dan Du ; Yueming Sun ; Lin He
- 刊名：Biomacromolecules
- 出版年：2007
- 出版时间：July 2007
- 年：2007
- 卷：8
- 期：7
- 页码：2142 - 2148
- 全文大小：137K
- 年卷期：v.8,no.7(July 2007)
- ISSN：1526-4602
文摘
We have successfully fabricated a self-assembled layer of concanavalin A (Con A) on a gold surface for recognitionof glycoproteins. The type IV Con A is covalently bound to 11-mercaptoundecanoic acid (MUA) on gold witha 2-(5-norbornene-2,3-dicarboximido)-1,1,3,3-tetramethyluronium tetrafluoroborate (TNTU) linkage. The bindinginteraction between glycoproteins and self-assembled Con A is studied using horseradish peroxidase (HRP) as amodel glycoprotein. Voltammetric, electrochemical impedance studies, and photometric activity measurementsshow the presence of both specific and nonspecific bindings of HRP to the Con A interface. The specific bindingis attributed to the Con A-sugar interaction where Con A selectively recognizes the glycosylation sites of HRP.The catalytic current of the HRP-loaded electrode, because of catalytic oxidation of thionine in the presence ofhydrogen peroxide (H2O2), is found to be proportional to the HRP concentrations in the incubation solution. Alinear correlation coefficient of 0.993 was obtained over a wide HRP concentration range of 12.5 
g/mL to 1mg/mL. The approach described in this study provides a simple yet selective means to immobilize glycoproteinson a solid support. The specific binding achieved is desirable in biosensor fabrication, glycoprotein separation,recognition, and purification as well as in drug-releasing systems.
g/mL to 1mg/mL. The approach described in this study provides a simple yet selective means to immobilize glycoproteinson a solid support. The specific binding achieved is desirable in biosensor fabrication, glycoprotein separation,recognition, and purification as well as in drug-releasing systems.