de Jong, Govardus A. H.

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  • de Jong, Govardus A. H. (3)
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Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249

Apostolović, Danijela; Stanić-Vučinić, Dragana; de Jongh, Harmen H. J.; de Jong, Govardus A. H.; Mihailović-Vesić, Jelena; Radosavljević, Jelena; Radibratović, Milica; Nordlee, Julie A.; Baumert, Joseph L.; Milčić, Miloš K.; Taylor, Steve L.; Clua, Nuria Garrido; Ćirković-Veličković, Tanja; Koppelman, Stef J.

(Nature Publishing Group, London, 2016)

TY  - BOOK
AU  - Apostolović, Danijela
AU  - Stanić-Vučinić, Dragana
AU  - de Jongh, Harmen H. J.
AU  - de Jong, Govardus A. H.
AU  - Mihailović-Vesić, Jelena
AU  - Radosavljević, Jelena
AU  - Radibratović, Milica
AU  - Nordlee, Julie A.
AU  - Baumert, Joseph L.
AU  - Milčić, Miloš K.
AU  - Taylor, Steve L.
AU  - Clua, Nuria Garrido
AU  - Ćirković-Veličković, Tanja
AU  - Koppelman, Stef J.
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3415
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249
ER  - 
@book{
author = "Apostolović, Danijela and Stanić-Vučinić, Dragana and de Jongh, Harmen H. J. and de Jong, Govardus A. H. and Mihailović-Vesić, Jelena and Radosavljević, Jelena and Radibratović, Milica and Nordlee, Julie A. and Baumert, Joseph L. and Milčić, Miloš K. and Taylor, Steve L. and Clua, Nuria Garrido and Ćirković-Veličković, Tanja and Koppelman, Stef J.",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3415",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249"
}
Apostolović, D., Stanić-Vučinić, D., de Jongh, H. H. J., de Jong, G. A. H., Mihailović-Vesić, J., Radosavljević, J., Radibratović, M., Nordlee, J. A., Baumert, J. L., Milčić, M. K., Taylor, S. L., Clua, N. G., Ćirković-Veličković, T.,& Koppelman, S. J. (2016). Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249.
Scientific Reports
Nature Publishing Group, London..
Apostolović D, Stanić-Vučinić D, de Jongh HHJ, de Jong GAH, Mihailović-Vesić J, Radosavljević J, Radibratović M, Nordlee JA, Baumert JL, Milčić MK, Taylor SL, Clua NG, Ćirković-Veličković T, Koppelman SJ. Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249. Scientific Reports. 2016;
Apostolović Danijela, Stanić-Vučinić Dragana, de Jongh Harmen H. J., de Jong Govardus A. H., Mihailović-Vesić Jelena, Radosavljević Jelena, Radibratović Milica, Nordlee Julie A., Baumert Joseph L., Milčić Miloš K., Taylor Steve L., Clua Nuria Garrido, Ćirković-Veličković Tanja, Koppelman Stef J., "Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249" Scientific Reports (2016)

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

Apostolović, Danijela; Stanić-Vučinić, Dragana; de Jongh, Harmen H. J.; de Jong, Govardus A. H.; Mihailović-Vesić, Jelena; Radosavljević, Jelena; Radibratović, Milica; Nordlee, Julie A.; Baumert, Joseph L.; Milčić, Miloš K.; Taylor, Steve L.; Clua, Nuria Garrido; Ćirković-Veličković, Tanja; Koppelman, Stef J.

(Nature Publishing Group, London, 2016)

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Stanić-Vučinić, Dragana
AU  - de Jongh, Harmen H. J.
AU  - de Jong, Govardus A. H.
AU  - Mihailović-Vesić, Jelena
AU  - Radosavljević, Jelena
AU  - Radibratović, Milica
AU  - Nordlee, Julie A.
AU  - Baumert, Joseph L.
AU  - Milčić, Miloš K.
AU  - Taylor, Steve L.
AU  - Clua, Nuria Garrido
AU  - Ćirković-Veličković, Tanja
AU  - Koppelman, Stef J.
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2273
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 = "Apostolović, Danijela and Stanić-Vučinić, Dragana and de Jongh, Harmen H. J. and de Jong, Govardus A. H. and Mihailović-Vesić, Jelena and Radosavljević, Jelena and Radibratović, Milica and Nordlee, Julie A. and Baumert, Joseph L. and Milčić, Miloš K. and Taylor, Steve L. and Clua, Nuria Garrido and Ćirković-Veličković, Tanja and Koppelman, Stef J.",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2273",
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"
}
Apostolović, D., Stanić-Vučinić, D., de Jongh, H. H. J., de Jong, G. A. H., Mihailović-Vesić, J., Radosavljević, J., Radibratović, M., Nordlee, J. A., Baumert, J. L., Milčić, M. K., 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.
Scientific Reports
Nature Publishing Group, London., 6.
https://doi.org/10.1038/srep29249
Apostolović D, Stanić-Vučinić D, de Jongh HHJ, de Jong GAH, Mihailović-Vesić J, Radosavljević J, Radibratović M, Nordlee JA, Baumert JL, Milčić MK, 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. Scientific Reports. 2016;6
Apostolović Danijela, Stanić-Vučinić Dragana, de Jongh Harmen H. J., de Jong Govardus A. H., Mihailović-Vesić Jelena, Radosavljević Jelena, Radibratović Milica, Nordlee Julie A., Baumert Joseph L., Milčić Miloš K., 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" Scientific Reports, 6 (2016),
https://doi.org/10.1038/srep29249 .
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Reduction and alkylation of peanut allergen isoforms Ara h 2 and Ara h 6 characterization of intermediate- and end products

Apostolović, Danijela; Luykx, Dion; Warmenhoven, Hans; Verbart, Dennis; Stanić-Vučinić, Dragana; de Jong, Govardus A. H.; Ćirković-Veličković, Tanja; Koppelman, Stef J.

(Elsevier Science Bv, Amsterdam, 2013)

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Luykx, Dion
AU  - Warmenhoven, Hans
AU  - Verbart, Dennis
AU  - Stanić-Vučinić, Dragana
AU  - de Jong, Govardus A. H.
AU  - Ćirković-Veličković, Tanja
AU  - Koppelman, Stef J.
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1463
AB  - Conglutins, the major peanut allergens, Ara h 2 and Ara h 6, are highly structured proteins stabilized by multiple disulfide bridges and are stable towards heat-denaturation and digestion. We sought a way to reduce their potent allergenicity in view of the development of immunotherapy for peanut allergy. Isoforms of conglutin were purified, reduced with dithiothreitol and subsequently allcylated with iodoacetamide. The effect of this modification was assessed on protein folding and IgE-binding. We found that all disulfide bridges were reduced and alkylated. As a result, the secondary structure lost a-helix and gained some beta-structure content, and the tertiary structure stability was reduced. On a functional level, the modification led to a strongly decreased IgE-binding. Using conditions for limited reduction and alkylation, partially reduced and alkylated proteins were found with rearranged disulfide bridges and, in some cases, intermolecular cross-links were found. Peptide mass finger printing was applied to control progress of the modification reaction and to map novel disulfide bonds. There was no preference for the order in which disulfides were reduced, and disulfide rearrangement occurred in a non-specific way. Only minor differences in kinetics of reduction and alkylation were found between the different conglutin isoforms. We conclude that the peanut conglutins Ara h 2 and Ara h 6 can be chemically modified by reduction and alkylation, such that they substantially unfold and that their allergenic potency decreases.
PB  - Elsevier Science Bv, Amsterdam
T2  - Biochimica et Biophysica Acta: Proteins and Proteomics
T1  - Reduction and alkylation of peanut allergen isoforms Ara h 2 and Ara h 6 characterization of intermediate- and end products
VL  - 1834
IS  - 12
SP  - 2832
EP  - 2842
DO  - 10.1016/j.bbapap.2013.10.004
ER  - 
@article{
author = "Apostolović, Danijela and Luykx, Dion and Warmenhoven, Hans and Verbart, Dennis and Stanić-Vučinić, Dragana and de Jong, Govardus A. H. and Ćirković-Veličković, Tanja and Koppelman, Stef J.",
year = "2013",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1463",
abstract = "Conglutins, the major peanut allergens, Ara h 2 and Ara h 6, are highly structured proteins stabilized by multiple disulfide bridges and are stable towards heat-denaturation and digestion. We sought a way to reduce their potent allergenicity in view of the development of immunotherapy for peanut allergy. Isoforms of conglutin were purified, reduced with dithiothreitol and subsequently allcylated with iodoacetamide. The effect of this modification was assessed on protein folding and IgE-binding. We found that all disulfide bridges were reduced and alkylated. As a result, the secondary structure lost a-helix and gained some beta-structure content, and the tertiary structure stability was reduced. On a functional level, the modification led to a strongly decreased IgE-binding. Using conditions for limited reduction and alkylation, partially reduced and alkylated proteins were found with rearranged disulfide bridges and, in some cases, intermolecular cross-links were found. Peptide mass finger printing was applied to control progress of the modification reaction and to map novel disulfide bonds. There was no preference for the order in which disulfides were reduced, and disulfide rearrangement occurred in a non-specific way. Only minor differences in kinetics of reduction and alkylation were found between the different conglutin isoforms. We conclude that the peanut conglutins Ara h 2 and Ara h 6 can be chemically modified by reduction and alkylation, such that they substantially unfold and that their allergenic potency decreases.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Biochimica et Biophysica Acta: Proteins and Proteomics",
title = "Reduction and alkylation of peanut allergen isoforms Ara h 2 and Ara h 6 characterization of intermediate- and end products",
volume = "1834",
number = "12",
pages = "2832-2842",
doi = "10.1016/j.bbapap.2013.10.004"
}
Apostolović, D., Luykx, D., Warmenhoven, H., Verbart, D., Stanić-Vučinić, D., de Jong, G. A. H., Ćirković-Veličković, T.,& Koppelman, S. J. (2013). Reduction and alkylation of peanut allergen isoforms Ara h 2 and Ara h 6 characterization of intermediate- and end products.
Biochimica et Biophysica Acta: Proteins and Proteomics
Elsevier Science Bv, Amsterdam., 1834(12), 2832-2842.
https://doi.org/10.1016/j.bbapap.2013.10.004
Apostolović D, Luykx D, Warmenhoven H, Verbart D, Stanić-Vučinić D, de Jong GAH, Ćirković-Veličković T, Koppelman SJ. Reduction and alkylation of peanut allergen isoforms Ara h 2 and Ara h 6 characterization of intermediate- and end products. Biochimica et Biophysica Acta: Proteins and Proteomics. 2013;1834(12):2832-2842
Apostolović Danijela, Luykx Dion, Warmenhoven Hans, Verbart Dennis, Stanić-Vučinić Dragana, de Jong Govardus A. H., Ćirković-Veličković Tanja, Koppelman Stef J., "Reduction and alkylation of peanut allergen isoforms Ara h 2 and Ara h 6 characterization of intermediate- and end products" Biochimica et Biophysica Acta: Proteins and Proteomics, 1834, no. 12 (2013):2832-2842,
https://doi.org/10.1016/j.bbapap.2013.10.004 .
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