Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity.
Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity.
复制标题
花生凝结蛋白的抗消化肽的构象稳定性揭示了其过敏性的分子基础。
DOI：
10.1038/srep29249
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发表时间：
2016-07-05
影响因子：
4.6
通讯作者：
Koppelman SJ
中科院分区：
文献类型：
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作者：
Apostolovic D;Stanic-Vucinic D;de Jongh HH;de Jong GA;Mihailovic J;Radosavljevic J;Radibratovic M;Nordlee JA;Baumert JL;Milcic M;Taylor SL;Garrido Clua N;Cirkovic Velickovic T;Koppelman SJ
粘连素是主要的花生过敏原，因其对胃肠道消化的抵抗力而闻名。我们的目的是通过生物化学和生物物理方法对粘连蛋白的消化抵抗肽（DRPs）进行表征，并进行分子动力学模拟，以更好地了解食物蛋白致敏的分子基础。我们在N端和c端以及有限的内部片段上绘制了蛋白水解位点，而其他潜在的蛋白水解位点未受影响。分子动力学模拟表明，蛋白质水解只发生在蛋白质的活性区域。DRPs似乎是构象稳定的完整的粘连物。此外，DRPs的整体二级结构和ige结合能力与完整的粘连蛋白相当。粘胶蛋白对胃肠道消化的稳定性，加上所产生的DRPs的构象稳定性，为肠道免疫系统提供了最佳暴露条件，这就解释了花生粘胶蛋白非凡的致敏性。
Conglutins represent the major peanut allergens and are renowned for their resistance to gastro-intestinal digestion. Our aim was to characterize the digestion-resistant peptides (DRPs) of conglutins by biochemical and biophysical methods followed by a molecular dynamics simulation in order to better understand the molecular basis of food protein allergenicity. We have mapped proteolysis sites at the N- and C-termini and at a limited internal segment, while other potential proteolysis sites remained unaffected. Molecular dynamics simulation showed that proteolysis only occurred in the vibrant regions of the proteins. DRPs appeared to be conformationally stable as intact conglutins. Also, the overall secondary structure and IgE-binding potency of DRPs was comparable to that of intact conglutins. The stability of conglutins toward gastro-intestinal digestion, combined with the conformational stability of the resulting DRPs provide conditions for optimal exposure to the intestinal immune system, providing an explanation for the extraordinary allergenicity of peanut conglutins.