TY  - JOUR
AU  - Đukić, Teodora
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Liu, Shu-Hua
AU  - Epstein, Michelle M.
AU  - van Hage, Marianne
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5781
AB  - : Post-translational modifications (PTMs) are covalent changes occurring on amino acid side
chains of proteins and yet are neglected structural and functional aspects of protein architecture. The
objective was to detect differences in PTM profiles that take place after roasting using open PTM
search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on
readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications
was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing
protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative
profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms
of modification versatility and extent. The most frequent PTM was methionine oxidation, especially
in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation
(Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ
in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study
provides a better understanding of how roasting impacts the PTM profile of major peanut allergens
and provides a good foundation for further exploration of PTMs
PB  - MDPI
T2  - Foods
T1  - Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting
VL  - 11
IS  - 24
SP  - 3993
DO  - 10.3390/foods11243993
ER  - 

@article{
author = "Đukić, Teodora and Smiljanić, Katarina and Mihailović, Jelena and Prodić, Ivana and Apostolović, Danijela and Liu, Shu-Hua and Epstein, Michelle M. and van Hage, Marianne and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2022",
abstract = ": Post-translational modifications (PTMs) are covalent changes occurring on amino acid side
chains of proteins and yet are neglected structural and functional aspects of protein architecture. The
objective was to detect differences in PTM profiles that take place after roasting using open PTM
search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on
readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications
was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing
protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative
profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms
of modification versatility and extent. The most frequent PTM was methionine oxidation, especially
in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation
(Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ
in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study
provides a better understanding of how roasting impacts the PTM profile of major peanut allergens
and provides a good foundation for further exploration of PTMs",
publisher = "MDPI",
journal = "Foods",
title = "Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting",
volume = "11",
number = "24",
pages = "3993",
doi = "10.3390/foods11243993"
}

Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S., Epstein, M. M., van Hage, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. in Foods
MDPI., 11(24), 3993.
https://doi.org/10.3390/foods11243993

Đukić T, Smiljanić K, Mihailović J, Prodić I, Apostolović D, Liu S, Epstein MM, van Hage M, Stanić-Vučinić D, Ćirković-Veličković T. Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. in Foods. 2022;11(24):3993.
doi:10.3390/foods11243993 .

Đukić, Teodora, Smiljanić, Katarina, Mihailović, Jelena, Prodić, Ivana, Apostolović, Danijela, Liu, Shu-Hua, Epstein, Michelle M., van Hage, Marianne, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting" in Foods, 11, no. 24 (2022):3993,
https://doi.org/10.3390/foods11243993 . .

TY  - DATA
AU  - Đukić, Teodora
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Liu, Shu-Hua
AU  - Epstein, Michelle M.
AU  - van Hage, Marianne
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5708
AB  - Post-translational modifications (PTMs) are covalent changes occurring on amino acid side chains of proteins and yet are neglected structural and functional aspects of protein architecture. The objective was to detect differences in PTM profiles that take place after roasting using open PTM search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms of modification versatility and extent. The most frequent PTM was methionine oxidation, especially in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation (Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study provides a better understanding of how roasting impacts the PTM profile of major peanut allergens and provides a good foundation for further exploration of PTMs.
PB  - MDPI
T2  - Foods
T1  - Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993
VL  - 11
IS  - 24
EP  - 3993
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5708
ER  - 

@misc{
author = "Đukić, Teodora and Smiljanić, Katarina and Mihailović, Jelena and Prodić, Ivana and Apostolović, Danijela and Liu, Shu-Hua and Epstein, Michelle M. and van Hage, Marianne and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Post-translational modifications (PTMs) are covalent changes occurring on amino acid side chains of proteins and yet are neglected structural and functional aspects of protein architecture. The objective was to detect differences in PTM profiles that take place after roasting using open PTM search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms of modification versatility and extent. The most frequent PTM was methionine oxidation, especially in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation (Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study provides a better understanding of how roasting impacts the PTM profile of major peanut allergens and provides a good foundation for further exploration of PTMs.",
publisher = "MDPI",
journal = "Foods",
title = "Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993",
volume = "11",
number = "24",
pages = "3993",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5708"
}

Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S., Epstein, M. M., van Hage, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2022). Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993. in Foods
MDPI., 11(24).
https://hdl.handle.net/21.15107/rcub_cherry_5708

Đukić T, Smiljanić K, Mihailović J, Prodić I, Apostolović D, Liu S, Epstein MM, van Hage M, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993. in Foods. 2022;11(24):null-3993.
https://hdl.handle.net/21.15107/rcub_cherry_5708 .

Đukić, Teodora, Smiljanić, Katarina, Mihailović, Jelena, Prodić, Ivana, Apostolović, Danijela, Liu, Shu-Hua, Epstein, Michelle M., van Hage, Marianne, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993" in Foods, 11, no. 24 (2022),
https://hdl.handle.net/21.15107/rcub_cherry_5708 .