Abstract
Food allergy has become a worldwide problem. To find an effective way to reduce the allergic effect of allergen is an interesting topic. In this work, the interaction between ovalbumin(OVA) and tangeretin was studied by means of spectroscopy, molecular docking calculation and animal experiment. As the results show, static quenching of fluorescence intensity happened due to the interaction between OVA and tangeretin. Binding constants, binding sites, and thermometric parameters were obtained. The conformation changing of OVA occurred due to the interaction between it and tangeretin. The molecular docking calculation results show that the epitopes Arginine 84(ARG84), Leucine 87(LEU87), Asparagine 88(ASN88), Serine 103(SER103), Arginine 104(ARG104), Leucine 124(LEU124), Arginine 126(ARG126), Glycine 127(GLY127), Glycine 128(GLY128) and Tryptohan 148(TRP148) of OVA were occupied by tangeretin after the docking, which means tangeretin may have some inhibition effects. As the results of animal experiments, the amount of IgE and lung tissue sections of female BALB/c mice in different groups show that tangeretin with different concentrations has better effects than dexamethasone. In conclusion, the tangeretin may have the effects to reduce the allergic effects of OVA via occupying the IgE-binding epitopes of OVA.
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