Citation: ZHANG Yu-Qi, ZHANG Jin-Ru, WANG Feng, LI Jia-Dong, SI Rui, LYU Li-Shan, SHEN Yu-Dong, WANG Hong, HAMMOCK Bruce D, SUN Yuan-Ming. Selection of Nanobody and Recognition Mechanism between Nanobody and Parathion[J]. Chinese Journal of Analytical Chemistry, ;2019, 47(9): 1419-1426. doi: 10.19756/j.issn.0253-3820.181772 shu

Selection of Nanobody and Recognition Mechanism between Nanobody and Parathion

1.
Guangdong Provincial Key Laboratory of Food Quality and Safety, National-Local Joint Engineering Research Center for Processing and Safety Control of Livestock and Poultry Products, College of Food Science, South China Agricultural University, Guangzhou 510642, China;
2.
Department of Entomology and UCD Comprehensive Cancer Center, University of California, Davis, California 95616, United States;
3.
Guangzhou Annuo Technology Co., Ltd, Guangzhou 510663, China

Received Date: 11 December 2018
Revised Date: 28 June 2019

Fund Project: This work was supported by the National Key R&D Program of China (Nos. 2016YFE0106000, 2018YFC1602904),the Science and Technology Planning Project of Guangzhou City (No. 201804020077), Key Area R&D Program of Guangdong Province (No. 2019B020211002) and the Guangdong Province Universities and Colleges Pearl River Scholar Funded Scheme (2017).

The organophosphorus pesticides are widely used in agriculture and food in China. Parathion, which is highly toxic and persistent, is one of the most widely used organophosphorus pesticides. Variable domain of the H chain of heavy-chain antibodies (VHH) is a fragment derived from camelids antibody. Due to its small size (only 15 kDa), high stability, ease of expression, and intact antigen-binding activity, VHHs have recently emerged as attractive reagents for immunodetection of chemical contaminants in food. In this study, five VHHs namely VHH1, VHH6, VHH13, VHH21 and VHH24 were selected from phage display library. Among these VHHs, VHH1 with the highest binding ability to parathion was selected for further analysis. VHH1 and parathion recognition mechanism predicted by homology modeling and molecule docking revealed the H bond and hydrophobic force, indicating the key amino acids Ser60, Lys104, Phe105, Gly106 and Arg107, which provided insights into antibody modification and antigen design.
- Variable domain of the H chain of heavy-chain antibodies,
- Parathion,
- Phage display,
- Molecule modeling
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