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 s...ystem, providing an explanation for the extraordinary allergenicity of peanut conglutins.
TY - JOUR
AU - Apostolovic, Danijela
AU - Stanić-Vučinić, Dragana
AU - de, Jongh Harmen H J
AU - de, Jong Govardus A H
AU - Mihailović, Jelena
AU - Radosavljević, Jelena
AU - Radibratović, Milica
AU - Nordlee, Julie A
AU - Baumert, Joseph L
AU - Milčić, Miloš
AU - Taylor, Steve L
AU - Clua, Nuria Garrido
AU - Ćirković Veličković, Tanja
AU - Koppelman, Stef J
PY - 2016
UR - https://cer.ihtm.bg.ac.rs/handle/123456789/1853
AB - 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.
PB - Nature Publishing Group, London
T2 - Scientific Reports
T1 - Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity
VL - 6
DO - 10.1038/srep29249
ER -
@article{
author = "Apostolovic, Danijela and Stanić-Vučinić, Dragana and de, Jongh Harmen H J and de, Jong Govardus A H and Mihailović, Jelena and Radosavljević, Jelena and Radibratović, Milica and Nordlee, Julie A and Baumert, Joseph L and Milčić, Miloš and Taylor, Steve L and Clua, Nuria Garrido and Ćirković Veličković, Tanja and Koppelman, Stef J",
year = "2016",
abstract = "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.",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity",
volume = "6",
doi = "10.1038/srep29249"
}
Apostolovic, D., Stanić-Vučinić, D., de, J. H. H. J., de, J. G. A. H., Mihailović, J., Radosavljević, J., Radibratović, M., Nordlee, J. A., Baumert, J. L., Milčić, M., Taylor, S. L., Clua, N. G., Ćirković Veličković, T.,& Koppelman, S. J.. (2016). Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity. in Scientific Reports
Nature Publishing Group, London., 6.
https://doi.org/10.1038/srep29249
Apostolovic D, Stanić-Vučinić D, de JHHJ, de JGAH, Mihailović J, Radosavljević J, Radibratović M, Nordlee JA, Baumert JL, Milčić M, Taylor SL, Clua NG, Ćirković Veličković T, Koppelman SJ. Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity. in Scientific Reports. 2016;6.
doi:10.1038/srep29249 .
Apostolovic, Danijela, Stanić-Vučinić, Dragana, de, Jongh Harmen H J, de, Jong Govardus A H, Mihailović, Jelena, Radosavljević, Jelena, Radibratović, Milica, Nordlee, Julie A, Baumert, Joseph L, Milčić, Miloš, Taylor, Steve L, Clua, Nuria Garrido, Ćirković Veličković, Tanja, Koppelman, Stef J, "Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity" in Scientific Reports, 6 (2016),
https://doi.org/10.1038/srep29249 . .
