Electrochemical pesticide sensitivity test using acetylcholinesterase biosensor based on colloidal gold nanoparticle modified sol-gel interface
Electrochemical pesticide sensitivity test using acetylcholinesterase biosensor based on colloidal gold nanoparticle modified sol-gel interface
复制标题
基于胶体金纳米粒子修饰溶胶-凝胶界面的乙酰胆碱酯酶生物传感器电化学农药敏感性测试
DOI：
10.1016/j.talanta.2007.07.014
复制
发表时间：
2008-01-15
期刊：
影响因子：
6.1
通讯作者：
Zhang, Aidong
中科院分区：
文献类型：
--
作者：
Du, Dan;Chen, Shizhen;Zhang, Aidong
基于农药诱导酶活性的电化学行为变化，建立了一种新的农药敏感性电化学检测方法--乙酰胆碱酯酶（AChE）生物传感器。溶胶-凝胶衍生的硅酸盐网络组装金纳米粒子（AuNPs-SiSG）提供了一个生物相容性的微环境周围的酶分子，以稳定其生物活性，并防止他们泄漏出接口。该复合材料的特点是使用原子力显微镜，并证明是化学清洁，多孔和均匀。AuNPs促进了电子转移的导电途径，并在较低电位下改善了电化学反应。选择久效磷、甲基双硫磷、西维因等典型农药进行药敏试验。由于农药的抑制作用，底物在乙酰胆碱酯酶传感器上的电化学响应大大降低。抑制曲线与紫外分光光度法测定结果一致。该方法灵敏度高、准确度好、成本低、操作简便。该方法可作为筛选高效酶抑制剂和研究对酶有毒性的化合物的常规方法。(c)2007 Elsevier B. V.保留所有权利。
Based on the change in electrochemical behavior of enzymatic activity induced by pesticide, a novel electrochemical method for investigation of pesticide sensitivity using acetylcholinesterase (AChE) biosensor was developed. The sol-gel-derived silicate network assembling gold nanoparticles (AuNPs-SiSG) provided a biocompatible microenvironment around the enzyme molecule to stabilize its biological activity and prevented them from leaking out of the interface. The composite was characterized using atomic force microscopy and proved to be chemically clean, porous and homogeneous. AuNPs promoted a conductive pathway for electron transfer and improved electrochemical reactions at a lower potential. Typical pesticides such as monocrotophos, methyl parathion and carbaryl were selected for pesticide sensitivity tests. Due to the inhibitions of pesticides, the electrochemical responses of substrate on AChE-sensors decreased greatly. The inhibition curves showed good correspondence with the results by UV spectrophotometry assay. The proposed electrochemical pesticide sensitivity test exhibited high sensitivity, desirable accuracy, low cost and simplified procedures. This method could be developed as a conventional method to select efficient enzyme inhibitors and investigate toxic compounds against to enzyme. (c) 2007 Elsevier B.V. All rights reserved.