High-affinity phage-displayed peptide as a recognition probe for the detection of Cry2Ad2-3
文献类型： 外文期刊
作者： Wang, Yun 1 ; Zhang, Xiao 2 ; Xie, Yajing 2 ; Wu, Aihua 2 ; Zai, Xueming 1 ; Liu, Xianjin 2 ;
作者机构： 1.Jinling Inst Technol, Coll Hort, Nanjing 210038, Jiangsu, Peoples R China
2.Jiangsu Acad Agr Sci, Minist Sci & Technol, State Key Lab Cultivat Base, Jiangsu Key Lab Food Qual & Safety, Nanjing 210014, Jiangsu, Peoples R China
关键词： Cry2Ad2-3; BBMV-peptide Sandwich ELISA; Molecular docking
期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：6.953； 五年影响因子：6.737 ）
ISSN： 0141-8130
年卷期： 2019 年 137 卷
页码：
收录情况： SCI
摘要： Cry2A is widely used in transgenic crops in combination with Cry1 A toxins. The sensitive and robust detection of Cry2A toxin in food and the environment is necessary to monitor the safety of biopesticides. Here, we describe an approach that involves the use of phage-displayed peptide for the detection of Cry2Ad2-3-the main area of Cry2Ad2 insecticidal activity. After four rounds of panning, six positive monoclonal phage particles were obtained. Pep5 with a sequence of ACSYNHNSKCGGG displayed low cross-reactivity with other Cry toxins. The working range of detection for Cry2Ad2-3 toxin standards in the brush border membrane vesicle (BBMV)-peptide sandwich EUSA was 10-50.625 ng mL(-1) and the detection limit (LOD) was 8 ng mL(-1). Molecular insight into the interaction of Pep5 with Cry2Ad2-3 was gleaned using homology modeling and docking. Molecular docking results showed that high-affinity peptide tended to dock in the groove between the two domains of Cry2Ad2-3. The interactions within the toxin-pep5 complex were due to hydrogen bond and hydrophobic interaction. Pep5 also lead us to trap the binding region. Therefore, peptides may be a cost-efficient alternative for detecting Cry toxins and studying their mechanisms. (C) 2019 Elsevier B.V. All rights reserved.
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