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  • Title: Experimental and computational studies on the mechanism of the β-lactoglobulin-derived peptide inhibiting the antigenicity of β-lactoglobulin.
    Author: Chen L, Yang H, Jiao L, Pu P, Zheng X, Liang G.
    Journal: Food Chem; 2022 Nov 01; 393():133333. PubMed ID: 35661607.
    Abstract:
    In this study, through a combined simulated enzymolysis-molecular docking-molecular simulation-activity determination-action mechanism strategy, we screened a β-LG-derived peptide (VAGTWYSL) to inhibit the antigenicity of β-LG and explored its mechanism of action. Our results indicate that the inhibitory effect of the peptide on the antigenicity of β-LG is affected by different experimental conditions, including pH, reaction time and concentration. Three factors may contribute to the reduced allergenicity of β-LG. First, there must be sufficient forces between the peptide and β-LG, as a result, hydrophobic forces and hydrogen bonds are the main forces to maintain the structural stability of the complex. Second, the binding of the peptide changes the secondary structure of β-LG, especially with an increase in α-helices and a decrease in β-turns. Third, the peptide binds to the hydrophobic region of β-LG, involving the antigenic epitope region Val41-Lys60, which may reduce the antigenicity.
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