TY - JOUR
T1 - Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity
AU - Apostolovic, Danijela
AU - Stanic-Vucinic, Dragana
AU - De Jongh, Harmen H.J.
AU - De Jong, Govardus A.H.
AU - Mihailovic, Jelena
AU - Radosavljevic, Jelena
AU - Radibratovic, Milica
AU - Nordlee, Julie A.
AU - Baumert, Joseph L.
AU - Milcic, Milos
AU - Taylor, Steve L.
AU - Garrido Clua, Nuria
AU - Cirkovic Velickovic, Tanja
AU - Koppelman, Stef J.
N1 - Copyright:
Copyright 2016 Elsevier B.V., All rights reserved.
PY - 2016/7/5
Y1 - 2016/7/5
N2 - 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.
AB - 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.
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U2 - 10.1038/srep29249
DO - 10.1038/srep29249
M3 - Article
C2 - 27377129
AN - SCOPUS:84977267167
VL - 6
JO - Scientific Reports
JF - Scientific Reports
SN - 2045-2322
M1 - 29249
ER -