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

Area of Science:

• Food Science
• Allergen Detection
• Biotechnology

Background:

• Beta-lactoglobulin (β-Lg) is a major food allergen, necessitating rapid detection methods for allergic individuals.
• Peptide aptamers offer high affinity, specificity, and stability, making them promising for rapid detection applications.

Purpose of the Study:

• To screen and identify peptide aptamers with high affinity and specificity for beta-lactoglobulin (β-Lg).
• To develop a novel recognition element for the rapid and specific detection of β-Lg.

Main Methods:

• Phage display library screening to identify potential β-Lg binding peptides.
• Molecular docking and ELISA to assess binding affinity and specificity of selected peptides.
• Molecular dynamics simulations to verify the binding interaction between the best peptide and β-Lg.

Main Results:

• Eleven peptides (P1-11) were screened, with P5, P7, and P8 showing the best binding to β-Lg via ELISA.
• Peptide P7 demonstrated superior specificity for β-Lg, with an inhibition rate of 87.99% against other proteins.
• Molecular dynamics confirmed stable binding of P7 to β-Lg.

Conclusions:

• Peptide P7 is a highly specific and effective recognition element for beta-lactoglobulin (β-Lg).
• This peptide has significant potential for developing rapid and reliable β-Lg detection assays, crucial for food safety and allergy management.