The effects of pH-shifting combined with quercetin binding on peanut Ara h 2 were evaluated using multispectroscopy, cell models, molecular simulation, and correlation analysis. After dual treatment, Ara h 2 exhibited significant structural changes, as evidenced by decreased intrinsic fluorescence and converted α-helix into β-sheet, leading to reduced IgE-binding capacity and diminished ability of dendritic cells and T cells to differentiate toward the Th2 pathway due to the masking of epitopes. Moreover, the binding sites of quercetin gradually shifted toward the hydrophobic core of Ara h 2 with pH changes, which inhibited fluctuations in the aa50-70 region. Finally, according to the correlation analysis, pH-shifting combined with quercetin binding may reduce the allergenicity of Ara h 2 by the migration of many Trp and Tyr residues to the protein surface, which disrupted the conformational epitopes. Therefore, this study provides an approach for the development of hypoallergenic peanut products.
Gao et al. (Tue,) studied this question.