Effects of covalent conjugation with quercetin and its glycosides on the structure and allergenicity of Bra c p from bee pollen

文献类型： 外文期刊

第一作者： Zhou, Enning

作者： Zhou, Enning;Xue, Xiaofeng;Zhao, Liuwei;Wu, Liming;Li, Qiangqiang;Xu, Haoxie

作者机构：

关键词： Bee pollen allergen; Profilin; Quercetin; Covalent conjunction; Structural changes; Allergenicity

期刊名称：FOOD CHEMISTRY （ 影响因子：8.8； 五年影响因子：8.6 ）

ISSN： 0308-8146

年卷期： 2023 年 406 卷

页码：

收录情况： SCI

摘要： Profilin family members are potential pan-allergens in foods, presenting public health hazards. However, studies on the allergenicity modification of profilin allergens are limited. Herein, quercetin and its glycosides (iso-quercitrin and rutin) were applied to modify the allergenicity of a profilin allergen (Bra c p) from Brassica campestris bee pollen. Results showed that only quercetin can be closely covalently bound to Bra c p among the three, and the binding site was located at the Cys98 residue. After covalently conjunction, the relative content of alpha-helix structure in Bra c p was reduced by 40.05%, while random coil was increased by 42.89%; moreover, the Tyr and Phe residues in Bra c p were masked. These structural changes could alter the conformational antigenic epitopes of Bra c p, resulting in its allergenicity reduction. Our findings might provide a technical foundation for reducing the allergenicity of bee pollen and foods containing profilin family allergens.

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