Interaction between wheat gliadin and quercetin under different pH conditions analyzed by multi-spectroscopy methods.

Polyphenols have been known to have significant binding affinity for proteins, and the specific condition (such as pH) could affect the degree of binding, the formation of covalent bond, and non-covalent interaction. In this study, characteristics of binding quercetin (Q) to wheat gliadin (G) which is a strong food allergen, were studied from pH 2.0 to pH 9.0. The results showed that Q quenched the fluorescence intensity of G by dynamic and static quenching modes and the stoichiometry of binding was close to 1. Intermolecular binding distances were smaller than 8 nm. Thermodynamic parameters suggested that hydrophobic force took charge of the formation of complexes at pH 2.0-4.0, whereas hydrogen bonds and van der Waals forces at pH 5.0-9.0. Analyses of the Fourier transform infrared and the Raman spectra along with synchronous fluorescence spectra revealed secondary and tertiary structural alterations and microenvironmental changed around protein fluorophores upon complexation with Q. The gauche-gauche-trans conformation increased at the expenses of the gauche-gauche-gauche conformation and the transition from β-turn and random coil to α-helix and β-sheet at pH 5.0 might decrease the allergenicity of G. These results provided new insights into G/Q interactions at different pH values, which may have potentials in decreasing allergen immunoreactivity.