Screening of specific binding peptide for β-lactoglobulin using phage display technology

被引:2
|
作者
Yu, Ning [1 ]
Yang, Yan [1 ,2 ]
Li, Yang [1 ,3 ]
Kang, Wenhan [1 ]
Zhang, Jiukai [1 ]
Chen, Ying [1 ]
机构
[1] Chinese Acad Inspect & Quarantine, Beijing 100176, Peoples R China
[2] Beijing Forestry Univ, Coll Biol Sci & Technol, Beijing 100083, Peoples R China
[3] Tianjin Univ Sci & Technol, Coll Food Sci & Engn, Tianjin 300457, Peoples R China
关键词
beta-Lg; Peptide aptamer; Display library technology; Molecular docking; Specificity; Binding ability; PROTEIN; SELECTION; APTAMER; PURIFICATION; DOCKING; DESIGN; LIGAND;
D O I
10.1016/j.foodchem.2024.139522
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
beta-lactoglobulin (beta-Lg) is a major food allergen, there is an urgent need to develop a rapid method for detecting beta-Lg in order to avoid contact or ingestion by allergic patients. Peptide aptamers have high affinity, specificity, and stability, and have broad prospects in the field of rapid detection. Using beta-Lg as the target, this study screened 11 peptides (P1-11) from a phage display library. Using molecular docking technology to predict binding energy and binding mode of proteins and peptides. Select the peptides with the best binding ability to beta-Lg (P5, P7, P8) through ELISA. Combining them with whey protein, casein, and bovine serum protein, it was found that P7 has the best specificity for beta-Lg, with an inhibition rate of 87.99%. Verified by molecular dynamics that P7 binds well with beta-Lg. Therefore, this peptide can be used for the recognition of beta-Lg, becoming a new recognition element for detecting beta-Lg.
引用
收藏
页数:8
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