Specific binding of glycoproteins with poly(aniline boronic acid) thin film
Specific binding of glycoproteins with poly(aniline boronic acid) thin film
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DOI：
10.1016/j.jelechem.2006.04.021
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发表时间：
2006-06-15
影响因子：
4.5
通讯作者：
Chen, Aicheng
中科院分区：
文献类型：
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作者：
Liu, Songqin;Bakovic, Linda;Chen, Aicheng
采用电聚合法在玻碳电极表面制备了聚苯胺硼酸（poly-APBA）薄膜，并将其用于糖蛋白的吸附。辣根过氧化物酶（HRP）和葡萄糖氧化酶（GOx）在这项研究中被用作模型糖蛋白，并显示与所形成的聚APBA薄膜的亲和相互作用。伏安法，计时电位，电化学阻抗谱研究和光度活性测量表明，糖蛋白（HRP和GOx）和聚APBA薄膜之间的亲和相互作用包括特异性和非特异性结合。特异性结合是由于硼酸-二醇相互作用，其中硼酸特异性结合HRP和GOx的糖基化位点。这种特异性结合是可逆的：它可以在酸性溶液中释放，也可以被糖分解。我们的对照实验表明，聚（苯胺）和聚（氨基苯甲酸），没有硼酸酯基团，也可以与HRP结合。然而，总结合是非特异性的，不能与糖分开。当使用非糖蛋白（牛血清白蛋白）代替糖蛋白与聚APBA膜结合时，也没有发现特异性结合。(c)2006 Elsevier B. V.保留所有权利。
A thin film of poly(aniline boronic acid) (poly-APBA) has been synthesized by electropolymerization on a glassy carbon electrode surface for the adsorption of glycoproteins. Horseradish peroxidase (HRP) and glucose oxidase (GOx) are used as the model glycoproteins in this study and show affinity interaction with the formed poly-APBA thin film. Voltammetric, chronopotentiometric, electrochemical impedance spectroscopic studies and photometric activity measurements show that the affinity interaction between the glycoproteins (HRP and GOx) and the poly-APBA thin film includes specific and non-specific binding. The specific binding is due to boronic acid-diols interaction, where the boronic acid specifically binds the glycosylation sites of the HRP and GOx. This specific binding is reversible: it can be released in acidic solutions and can also be split by sugars. Our control experiments show that the poly(aniline) and poly(aminobenzoic acid), without the boronate group, can also bind with HRP. However, the total binding is non-specific and can not be split with sugar. Also no specific binding can be found when non-glycoprotein (bovine serum albumin) instead of glycoprotein is used to bind with the poly-APBA film. (c) 2006 Elsevier B.V. All rights reserved.