Impact of Interaction with Docosahexaenoic Acid on the Allergenicity of β-Lactoglobulin
β-Lactoglobulin(β-LG)is a major allergen in cow's milk.In this study,synchronous fluorescence spectroscopy,three-dimensional fluorescence spectroscopy,circular dichroism(CD)spectroscopy,molecular docking,and indirect competitive enzyme-linked immunosorbent assay were used to explore the interaction of docosahexaenoic acid(DHA)with β-LG and its influence on the allergenicity of β-LG.The results showed that the binding of DHA to β-LG significantly changed the microenvironment of the aromatic residues of β-LG and increased its polarity.DHA bound to β-LG to form a stable complex through hydrophobic interactions,changing the secondary structure of β-LG and resulting in folding of its backbone.The relative content of β-sheet increased and then decreased with increasing concentration of DHA,while the relative content of α-helix showed an opposite trend.However,the relative contents of β-turn and random coil showed irregular changes.In addition,the antigenicity of β-LG decreased after combination with DHA,and the immunoglobulin E(IgE)binding ability inhibition rate was about 29%by 3 mmol/L DHA.
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