Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity

被引：63

作者：

Apostolovic, Danijela ^{[1
]}

Stanic-Vucinic, Dragana ^{[1
]}

de Jongh, Harmen H. J. ^{[2
]}

de Jong, Govardus A. H. ^{[3
]}

Mihailovic, Jelena ^{[1
]}

Radosavljevic, Jelena ^{[1
]}

Radibratovic, Milica ^{[4
]}

Nordlee, Julie A. ^{[5
]}

Baumert, Joseph L. ^{[5
]}

Milcic, Milos ^{[1
]}

Taylor, Steve L. ^{[5
]}

Clua, Nuria Garrido ^{[2
]}

Velickovic, Tanja Cirkovic ^{[1
]}

Koppelman, Stef J. ^{[5
]}

机构：

[1] Univ Belgrade, Fac Chem, Ctr Excellence Mol Food Sci, Studentski Trg 16, Belgrade 11000, Serbia

[2] TI Food & Nutr, POB 557, NL-6700 AN Wageningen, Netherlands

[3] TNO, Utrechtseweg 48, NL-3704 HE Zeist, Netherlands

[4] Inst Chem Technol & Met, Ctr Chem, Njegoseva 12, Belgrade, Serbia

[5] Univ Nebraska, Food Allergy Res & Resource Program, 279 Food Innovat Ctr, Lincoln, NE 68588 USA

来源：

SCIENTIFIC REPORTS | 2016年 / 6卷

关键词：

ARA H 2; IN-VITRO; IGE-BINDING; BREAST-MILK; PROTEIN; ALBUMIN; ISOFORMS; REACTIVITY; DYNAMICS; ARA-H-2;

D O I：

10.1038/srep29249

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Conglutins represent the major peanut allergens and are renowned for their resistance to gastrointestinal 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.

引用

页数：12

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