Evaluating pH-induced gastrointestinal aggregation of Arachis hypogaea 1 fragments as potential components of peanut allergy.

Evaluating pH-induced gastrointestinal aggregation of Arachis hypogaea 1 fragments as potential components of peanut allergy.
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DOI:
10.1021/jf401701t
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发表时间:
2013-09-04
影响因子:
6.1
通讯作者:
Nanda V
Nanda V
中科院分区:
农林科学1区
文献类型:
--
作者:
Khan IJ;Di R;Patel P;Nanda V

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种子贮藏糖蛋白Arachis hypogea 1(Ara h)1是花生中发现的主要过敏原。食物蛋白质对蛋白酶消化的生物化学抗性有助于其过敏性。Ara h 1在胃条件下的快速蛋白水解挑战了这一模型。进行了生物物理和体外消化实验,以确定Ara h 1表位如何在消化中存活,尽管它容易降解。阿糖胞苷h 1的bicupin核心可以在低pH值下展开,在较高pH值下可逆折叠。此外,来自模拟胃消化的肽片段在转移到碱基时主要形成非共价聚集体。这些聚集体中的二硫键交联仅在早期以相对低的量发生,因此在保护肽免于降解方面不起作用。我们提出,在胃条件下存活的肽片段在小肠等基本环境中形成大的聚集体,使表位可用于触发过敏反应。
The seed storage glycoprotein Arachis hypogea 1 (Ara h) 1 is a major allergen found in peanuts. The biochemical resistance of food proteins to protease digestion contributes to their allergenicity. The rapid proteolysis of Ara h 1 under gastric conditions challenges this model. Biophysical and in vitro digestion experiments were carried out to identify how Ara h 1 epitopes might survive digestion, despite its facile degradation. The bicupin core of Ara h 1 can be unfolded at low pH and reversibly folded at higher pH. Additionally, peptide fragments from simulated gastric digestion predominantly form non-covalent aggregates when transferred to base. Disulfide crosslinks within these aggregates occur in relatively low amounts only at early times and therefore play no role in shielding peptides from degradation. We propose that peptide fragments which survive gastric conditions form large aggregates in basic environments like the small intestine, making epitopes available for triggering an allergic response.
DOI: 10.1111/j.1432-1033.1991.tb16456.x
发表时间: 1991-12-18
期刊: EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子: --
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CERIOTTI, A;PEDRAZZINI, E;VITALE, A
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