Synthesis and electrochemical characterization of myoglobin-antibody protein immobilized self-assembled gold nanoparticles on ITO-glass plate
Synthesis and electrochemical characterization of myoglobin-antibody protein immobilized self-assembled gold nanoparticles on ITO-glass plate
复制标题
DOI：
10.1016/j.matchemphys.2011.10.024
复制
发表时间：
2012-01-16
影响因子：
4.6
通讯作者：
Biradar, Ashok M.
中科院分区：
文献类型：
--
作者：
Rajesh;Sharma, Vikash;Biradar, Ashok M.
我们报道了一种在氧化铟锡（ITO）镀膜玻璃板上固定金纳米粒子（GNPs）的蛋白质自组装单层（SAM）。以N-（3-二甲氨基丙基）-N′-乙基碳二亚胺（EDC）和N-羟基琥珀酰亚胺（NHS）为偶联剂，通过11-巯基十一酸（MUA）和3-巯基丙酸（MPA）的混合SAM，将抗体Mb-Ab蛋白固定在GNPs的自组装上。整个组装体构建在0.25 cm(2)面积的ito玻璃板（Mb-Ab/MUA-MPA/GNPs/APTES/ITO-glass）上，并对其在肌红蛋白检测中的应用进行了阻抗研究。通过扫描电子显微镜、原子力显微镜和电化学技术对该原型组件进行了表征。修饰后的电极与蛋白抗原偶联后的电子转移阻力增加。Mb-Ag，在氧化还原探针[Fe(CN)(6)]（3-/4-）存在下。其对肌红蛋白抗原Mb-Ag的浓度呈0.01 μ g ~ 1.65 μ g mL（-1）线性响应，最低检出限为1.4 ng mL（-1）。(C) 2011 Elsevier B.V.版权所有
We report a protein immobilized self-assembled monolayer (SAM) of gold nanoparticles (GNPs) on indium-tin-oxide ( ITO) coated glass plate. The protein-antibody, Mb-Ab, was covalently immobilized over the self-assembly of GNPs through a mixed SAM of 11-mercapto undecanoic acid (MUA) and 3-mercapto propionic acid (MPA) via carbodiimide coupling reaction using N-(3-dimethylaminopropyl)-N'-ethyl carbodiimide (EDC) and N-hydroxy succinimide (NHS). The whole assembly was constructed on 0.25 cm(2) area of ITO-glass plate (Mb-Ab/MUA-MPA/GNPs/APTES/ITO-glass) and an impedimetric study was carried out for its application in myoglobin detection. This prototype assembly was characterized by scanning electron microscopy, atomic force microscopy and electrochemical techniques. The modified electrode showed an increased electron-transfer resistance on coupling with protein antigen. Mb-Ag, in the presence of a redox probe [Fe(CN)(6)](3-/4-). Its exhibits an electrochemical impedance response to protein myoglobin-antigen, Mb-Ag, concentration in a linear range from 0.01 mu g to 1.65 mu g mL(-1) with a lowest detection limit of 1.4 ng mL(-1). (C) 2011 Elsevier B.V. All rights reserved.