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| Electrochemical Evaluation of the Mechanism of Acetylcholinesterase Inhibition Based on an Electrodeposited Thin Film | |
Zhang, Hongxia1,2,3; Ding, Jiawang1,2 ; Du, Dan4; Ding, JW (reprint author), Chinese Acad Sci, Yantai Inst Coastal Zone Res YIC, Key Lab Coastal Environm Proc & Ecol Remediat, Yantai 264003, Shandong, Peoples R China. jwding@mail.ccnu.edu.cn
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| 发表期刊 | INTERNATIONAL JOURNAL OF ELECTROCHEMICAL SCIENCE
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| ISSN | 1452-3981 |
| 2015-02-01 | |
| 卷号 | 10期号:2页码:1632-1645 |
| 关键词 | Acetylcholinesterase Biosensor Inhibition Mechanism Electrochemical Electrodeposition |
| 产权排序 | [Zhang, Hongxia; Ding, Jiawang] Chinese Acad Sci, Yantai Inst Coastal Zone Res YIC, Key Lab Coastal Environm Proc & Ecol Remediat, Yantai 264003, Shandong, Peoples R China; [Zhang, Hongxia; Ding, Jiawang] YICCAS, Shandong Prov Key Lab Coastal Environm Proc, Yantai 264003, Shandong, Peoples R China; [Zhang, Hongxia] Univ Chinese Acad Sci, Beijing 100049, Peoples R China; [Du, Dan] Huazhong Normal Univ, Minist Educ, Key Lab Pesticide & Chem Biol, Wuhan 430079, Peoples R China |
| 作者部门 | 中科院海岸带环境过程与生态修复重点实验室 |
| 英文摘要 | An interface embedded gold nanoparticles in sol-gel thin film was constructed by one-step electrochemical deposition. Acetylcholinesterase (AChE) was physically absorbed onto to the interface to form a thin enzymatic layer. The proposed thin enzymatic layer, having kinetics similar to that of the enzyme in solution, provides an ideal sensing platform to electrochemically evaluate the chemical mechanism of enzyme inhibition. Lineweaver-Burk plot and surface plasmon resonance confirmed that the inhibition of AChE by malathion followed an irreversible mechanism and was a mixed type of competitive and noncompetitive. On the contrary, the degrees of inhibition by Pb2+ and Fe3+ were independent of the incubation time and the AChE concentrations, showing the reversibility of the inhibition. Furthermore, UV-vis absorption spectra indicated that the AChE mediated the hydrolysis of acetylthiocholine to yield a reducing agent thiocholine that reduced Fe3+ to Fe2+ and Fe2+ presented an effect of activation. To meet the demand of the biosensor design, we further investigated the relationship between inhibition percentage and both incubation time and inhibitor concentration. The enzyme's sensitivity to solvent effects and reactivation of the biosensor were also evaluated. It is anticipated that a rapid evaluation of the chemical mechanism of AChE inhibition could paves the way to rationally design biosensors and new compounds, as candidates for the treatment of Alzheimer's disease and pesticides.; An interface embedded gold nanoparticles in sol-gel thin film was constructed by one-step electrochemical deposition. Acetylcholinesterase (AChE) was physically absorbed onto to the interface to form a thin enzymatic layer. The proposed thin enzymatic layer, having kinetics similar to that of the enzyme in solution, provides an ideal sensing platform to electrochemically evaluate the chemical mechanism of enzyme inhibition. Lineweaver-Burk plot and surface plasmon resonance confirmed that the inhibition of AChE by malathion followed an irreversible mechanism and was a mixed type of competitive and noncompetitive. On the contrary, the degrees of inhibition by Pb2+ and Fe3+ were independent of the incubation time and the AChE concentrations, showing the reversibility of the inhibition. Furthermore, UV-vis absorption spectra indicated that the AChE mediated the hydrolysis of acetylthiocholine to yield a reducing agent thiocholine that reduced Fe3+ to Fe2+ and Fe2+ presented an effect of activation. To meet the demand of the biosensor design, we further investigated the relationship between inhibition percentage and both incubation time and inhibitor concentration. The enzyme's sensitivity to solvent effects and reactivation of the biosensor were also evaluated. It is anticipated that a rapid evaluation of the chemical mechanism of AChE inhibition could paves the way to rationally design biosensors and new compounds, as candidates for the treatment of Alzheimer's disease and pesticides. |
| 文章类型 | Article |
| 资助机构 | Electrochemistry |
| 收录类别 | SCI |
| 语种 | 英语 |
| 关键词[WOS] | GOLD NANOPARTICLES ; IMMOBILIZED ACETYLCHOLINESTERASE ; ORGANOPHOSPHOROUS INSECTICIDE ; AMPEROMETRIC DETECTION ; AU NANOPARTICLES ; BIOSENSOR DESIGN ; SILICATE FILMS ; CHITOSAN ; CARBON ; THIOCHOLINE |
| 研究领域[WOS] | Electrochemistry |
| WOS记录号 | WOS:000348365800047 |
| 引用统计 | |
| 文献类型 | 期刊论文 |
| 条目标识符 | http://ir.yic.ac.cn/handle/133337/8658 |
| 专题 | 中国科学院海岸带环境过程与生态修复重点实验室 |
| 通讯作者 | Ding, JW (reprint author), Chinese Acad Sci, Yantai Inst Coastal Zone Res YIC, Key Lab Coastal Environm Proc & Ecol Remediat, Yantai 264003, Shandong, Peoples R China. jwding@mail.ccnu.edu.cn |
| 作者单位 | 1.Chinese Acad Sci, Yantai Inst Coastal Zone Res YIC, Key Lab Coastal Environm Proc & Ecol Remediat, Yantai 264003, Shandong, Peoples R China 2.YICCAS, Shandong Prov Key Lab Coastal Environm Proc, Yantai 264003, Shandong, Peoples R China 3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 4.Huazhong Normal Univ, Minist Educ, Key Lab Pesticide & Chem Biol, Wuhan 430079, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zhang, Hongxia,Ding, Jiawang,Du, Dan,et al. Electrochemical Evaluation of the Mechanism of Acetylcholinesterase Inhibition Based on an Electrodeposited Thin Film[J]. INTERNATIONAL JOURNAL OF ELECTROCHEMICAL SCIENCE,2015,10(2):1632-1645. |
| APA | Zhang, Hongxia,Ding, Jiawang,Du, Dan,&Ding, JW .(2015).Electrochemical Evaluation of the Mechanism of Acetylcholinesterase Inhibition Based on an Electrodeposited Thin Film.INTERNATIONAL JOURNAL OF ELECTROCHEMICAL SCIENCE,10(2),1632-1645. |
| MLA | Zhang, Hongxia,et al."Electrochemical Evaluation of the Mechanism of Acetylcholinesterase Inhibition Based on an Electrodeposited Thin Film".INTERNATIONAL JOURNAL OF ELECTROCHEMICAL SCIENCE 10.2(2015):1632-1645. |
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