Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity
2016
Аутори
Apostolovic, DanijelaStanić-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
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
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.
Извор:
Scientific Reports, 2016, 6Издавач:
- Nature Publishing Group, London
Финансирање / пројекти:
- Молекуларне особине и модификације неких респираторних и нутритивних алергена (RS-MESTD-Basic Research (BR or ON)-172024)
- Моделирање и нумеричке симулације сложених вишечестичних система (RS-MESTD-Basic Research (BR or ON)-171017)
- Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-FP7-256716)
DOI: 10.1038/srep29249
ISSN: 2045-2322
PubMed: 27377129
WoS: 000379265400001
Scopus: 2-s2.0-84977267167
Институција/група
IHTMTY - 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 . .