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

β-lactoglobulin (β-Lg) is a major food allergen, there is an urgent need to develop a rapid method for detecting β-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 β-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 β-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 β-Lg, with an inhibition rate of 87.99%. Verified by molecular dynamics that P7 binds well with β-Lg. Therefore, this peptide can be used for the recognition of β-Lg, becoming a new recognition element for detecting β-Lg. • 11 binding peptides of β-Lg were screened by display library technology. • The interaction between peptides and β-Lg was predicted with molecular docking. • Indirect ELISA was used to verify the actual binding ability of the peptides. • The specific binding ability of the screened peptides was also evaluated. [ABSTRACT FROM AUTHOR]