Molecular properties and modifications of some respiratory and nutritional allergens

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info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172024/RS//

Molecular properties and modifications of some respiratory and nutritional allergens (en)
Молекуларне особине и модификације неких респираторних и нутритивних алергена (sr)
Molekularne osobine i modifikacije nekih respiratornih i nutritivnih alergena (sr_RS)
Authors

Publications

Drying methodology effect on the phenolic content, antioxidant activity of Myrtus communis L. leaves ethanol extracts and soybean oil oxidative stability

Snoussi, Ahmed; Essaidi, Ismahen; Ben Haj Koubaier, Hayet; Zrelli, Houda; Alsafari, Ibrahim; Tešić, Živoslav Lj.; Mihailovic, Jelena; Khan, Muhummadh; El Omri, Abdelfatteh; Ćirković-Veličković, Tanja; Bouzouita, Nabiha

(Springer Nature, 2021)

TY  - JOUR
AU  - Snoussi, Ahmed
AU  - Essaidi, Ismahen
AU  - Ben Haj Koubaier, Hayet
AU  - Zrelli, Houda
AU  - Alsafari, Ibrahim
AU  - Tešić, Živoslav Lj.
AU  - Mihailovic, Jelena
AU  - Khan, Muhummadh
AU  - El Omri, Abdelfatteh
AU  - Ćirković-Veličković, Tanja
AU  - Bouzouita, Nabiha
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4441
AB  - In this study, different drying methodologies (convective air, oven and microwave) of Myrtus communis L. (M. communis L.) leaves were conducted to investigate their effects on the levels of phenolic compounds, antioxidant capacity of ethanolic extracts (EEs) as well as the soybean oil oxidative stability. Drying methodology significantly influenced the extractability of phenolic compounds. Microwave drying led to an increase in the amounts of total phenols, flavonoids and proanthocyanidins followed by oven drying at 70 °C. Higher temperature of drying (100 and 120 °C) led to a significant reduction of their amounts (p < 0.05). An ultra-performance liquid chromatography method combined with high resolution mass spectroscopic detection was used to analyze the phenolic fraction of extracts. Higher amounts of the identified compounds were observed when leaves were heat treated. Furthermore, the evaluation of the antioxidant activity showed that the studied extracts possess in general high antioxidant capacities, significantly dependent on the employed drying methodology. The incorporation of the different extracts at 200 ppm in soybean oil showed that its oxidative stability was significantly improved. Extracts from leaves treated with microwave (EE_MW) and at 70 °C (EE_70) have better effect than BHT. The results of the present study suggest that microwave drying could be useful to enhance the extractability of phenolic compounds and the antioxidant capacity of M. communis L. leaf extract.
PB  - Springer Nature
T2  - BMC Chemistry
T2  - BMC ChemistryBMC Chemistry
T1  - Drying methodology effect on the phenolic content, antioxidant activity of Myrtus communis L. leaves ethanol extracts and soybean oil oxidative stability
VL  - 15
IS  - 1
SP  - 31
DO  - 10.1186/s13065-021-00753-2
ER  - 
@article{
author = "Snoussi, Ahmed and Essaidi, Ismahen and Ben Haj Koubaier, Hayet and Zrelli, Houda and Alsafari, Ibrahim and Tešić, Živoslav Lj. and Mihailovic, Jelena and Khan, Muhummadh and El Omri, Abdelfatteh and Ćirković-Veličković, Tanja and Bouzouita, Nabiha",
year = "2021",
abstract = "In this study, different drying methodologies (convective air, oven and microwave) of Myrtus communis L. (M. communis L.) leaves were conducted to investigate their effects on the levels of phenolic compounds, antioxidant capacity of ethanolic extracts (EEs) as well as the soybean oil oxidative stability. Drying methodology significantly influenced the extractability of phenolic compounds. Microwave drying led to an increase in the amounts of total phenols, flavonoids and proanthocyanidins followed by oven drying at 70 °C. Higher temperature of drying (100 and 120 °C) led to a significant reduction of their amounts (p < 0.05). An ultra-performance liquid chromatography method combined with high resolution mass spectroscopic detection was used to analyze the phenolic fraction of extracts. Higher amounts of the identified compounds were observed when leaves were heat treated. Furthermore, the evaluation of the antioxidant activity showed that the studied extracts possess in general high antioxidant capacities, significantly dependent on the employed drying methodology. The incorporation of the different extracts at 200 ppm in soybean oil showed that its oxidative stability was significantly improved. Extracts from leaves treated with microwave (EE_MW) and at 70 °C (EE_70) have better effect than BHT. The results of the present study suggest that microwave drying could be useful to enhance the extractability of phenolic compounds and the antioxidant capacity of M. communis L. leaf extract.",
publisher = "Springer Nature",
journal = "BMC Chemistry, BMC ChemistryBMC Chemistry",
title = "Drying methodology effect on the phenolic content, antioxidant activity of Myrtus communis L. leaves ethanol extracts and soybean oil oxidative stability",
volume = "15",
number = "1",
pages = "31",
doi = "10.1186/s13065-021-00753-2"
}
Snoussi, A., Essaidi, I., Ben Haj Koubaier, H., Zrelli, H., Alsafari, I., Tešić, Ž. Lj., Mihailovic, J., Khan, M., El Omri, A., Ćirković-Veličković, T.,& Bouzouita, N.. (2021). Drying methodology effect on the phenolic content, antioxidant activity of Myrtus communis L. leaves ethanol extracts and soybean oil oxidative stability. in BMC Chemistry
Springer Nature., 15(1), 31.
https://doi.org/10.1186/s13065-021-00753-2
Snoussi A, Essaidi I, Ben Haj Koubaier H, Zrelli H, Alsafari I, Tešić ŽL, Mihailovic J, Khan M, El Omri A, Ćirković-Veličković T, Bouzouita N. Drying methodology effect on the phenolic content, antioxidant activity of Myrtus communis L. leaves ethanol extracts and soybean oil oxidative stability. in BMC Chemistry. 2021;15(1):31.
doi:10.1186/s13065-021-00753-2 .
Snoussi, Ahmed, Essaidi, Ismahen, Ben Haj Koubaier, Hayet, Zrelli, Houda, Alsafari, Ibrahim, Tešić, Živoslav Lj., Mihailovic, Jelena, Khan, Muhummadh, El Omri, Abdelfatteh, Ćirković-Veličković, Tanja, Bouzouita, Nabiha, "Drying methodology effect on the phenolic content, antioxidant activity of Myrtus communis L. leaves ethanol extracts and soybean oil oxidative stability" in BMC Chemistry, 15, no. 1 (2021):31,
https://doi.org/10.1186/s13065-021-00753-2 . .

The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c

Stanić-Vučinić, Dragana; Nikolić, Stefan; Vlajić, Katarina; Radomirović, Mirjana Ž.; Mihailović, Jelena; Ćirković-Veličković, Tanja; Grgurić-Šipka, Sanja

(Springer, 2020)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Vlajić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić-Šipka, Sanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3859
AB  - The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.
PB  - Springer
T2  - Journal of Biological Inorganic Chemistry
T1  - The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c
VL  - 25
IS  - 2
SP  - 253
EP  - 265
DO  - 10.1007/s00775-020-01758-3
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Nikolić, Stefan and Vlajić, Katarina and Radomirović, Mirjana Ž. and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić-Šipka, Sanja",
year = "2020",
abstract = "The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.",
publisher = "Springer",
journal = "Journal of Biological Inorganic Chemistry",
title = "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c",
volume = "25",
number = "2",
pages = "253-265",
doi = "10.1007/s00775-020-01758-3"
}
Stanić-Vučinić, D., Nikolić, S., Vlajić, K., Radomirović, M. Ž., Mihailović, J., Ćirković-Veličković, T.,& Grgurić-Šipka, S.. (2020). The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. in Journal of Biological Inorganic Chemistry
Springer., 25(2), 253-265.
https://doi.org/10.1007/s00775-020-01758-3
Stanić-Vučinić D, Nikolić S, Vlajić K, Radomirović MŽ, Mihailović J, Ćirković-Veličković T, Grgurić-Šipka S. The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. in Journal of Biological Inorganic Chemistry. 2020;25(2):253-265.
doi:10.1007/s00775-020-01758-3 .
Stanić-Vučinić, Dragana, Nikolić, Stefan, Vlajić, Katarina, Radomirović, Mirjana Ž., Mihailović, Jelena, Ćirković-Veličković, Tanja, Grgurić-Šipka, Sanja, "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c" in Journal of Biological Inorganic Chemistry, 25, no. 2 (2020):253-265,
https://doi.org/10.1007/s00775-020-01758-3 . .
3
3
3

Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3

Stanić-Vučinić, Dragana; Nikolić, Stefan; Vlajić, Katarina; Radomirović, Mirjana Ž.; Mihailović, Jelena; Ćirković-Veličković, Tanja; Grgurić-Šipka, Sanja

(Springer, 2020)

TY  - DATA
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Vlajić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić-Šipka, Sanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3863
PB  - Springer
T2  - Journal of Biological Inorganic Chemistry
T1  - Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3
ER  - 
@misc{
author = "Stanić-Vučinić, Dragana and Nikolić, Stefan and Vlajić, Katarina and Radomirović, Mirjana Ž. and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić-Šipka, Sanja",
year = "2020",
publisher = "Springer",
journal = "Journal of Biological Inorganic Chemistry",
title = "Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3"
}
Stanić-Vučinić, D., Nikolić, S., Vlajić, K., Radomirović, M. Ž., Mihailović, J., Ćirković-Veličković, T.,& Grgurić-Šipka, S.. (2020). Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3. in Journal of Biological Inorganic Chemistry
Springer..
Stanić-Vučinić D, Nikolić S, Vlajić K, Radomirović MŽ, Mihailović J, Ćirković-Veličković T, Grgurić-Šipka S. Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3. in Journal of Biological Inorganic Chemistry. 2020;..
Stanić-Vučinić, Dragana, Nikolić, Stefan, Vlajić, Katarina, Radomirović, Mirjana Ž., Mihailović, Jelena, Ćirković-Veličković, Tanja, Grgurić-Šipka, Sanja, "Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3" in Journal of Biological Inorganic Chemistry (2020).

The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c

Stanić-Vučinić, Dragana; Nikolić, Stefan; Vlajić, Katarina; Radomirović, Mirjana Ž.; Mihailović, Jelena; Ćirković-Veličković, Tanja; Grgurić-Šipka, Sanja

(Springer, 2020)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Vlajić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić-Šipka, Sanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3942
AB  - The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.
PB  - Springer
T2  - Journal of Biological Inorganic Chemistry
T1  - The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c
VL  - 25
IS  - 2
SP  - 253
EP  - 265
DO  - 10.1007/s00775-020-01758-3
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Nikolić, Stefan and Vlajić, Katarina and Radomirović, Mirjana Ž. and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić-Šipka, Sanja",
year = "2020",
abstract = "The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.",
publisher = "Springer",
journal = "Journal of Biological Inorganic Chemistry",
title = "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c",
volume = "25",
number = "2",
pages = "253-265",
doi = "10.1007/s00775-020-01758-3"
}
Stanić-Vučinić, D., Nikolić, S., Vlajić, K., Radomirović, M. Ž., Mihailović, J., Ćirković-Veličković, T.,& Grgurić-Šipka, S.. (2020). The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. in Journal of Biological Inorganic Chemistry
Springer., 25(2), 253-265.
https://doi.org/10.1007/s00775-020-01758-3
Stanić-Vučinić D, Nikolić S, Vlajić K, Radomirović MŽ, Mihailović J, Ćirković-Veličković T, Grgurić-Šipka S. The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. in Journal of Biological Inorganic Chemistry. 2020;25(2):253-265.
doi:10.1007/s00775-020-01758-3 .
Stanić-Vučinić, Dragana, Nikolić, Stefan, Vlajić, Katarina, Radomirović, Mirjana Ž., Mihailović, Jelena, Ćirković-Veličković, Tanja, Grgurić-Šipka, Sanja, "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c" in Journal of Biological Inorganic Chemistry, 25, no. 2 (2020):253-265,
https://doi.org/10.1007/s00775-020-01758-3 . .
3
3
3

Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy

Apostolović, Danijela; Mihailović, Jelena; Commins, Scott P.; Wijnveld, Michiel; Kazimirova, Maria; Starkhammar, Maria; Stockinger, Hannes; Platts-Mills, Thomas A. E.; Ćirković-Veličković, Tanja; Hamsten, Carl; van Hage, Marianne

(Wiley, 2020)

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Commins, Scott P.
AU  - Wijnveld, Michiel
AU  - Kazimirova, Maria
AU  - Starkhammar, Maria
AU  - Stockinger, Hannes
AU  - Platts-Mills, Thomas A. E.
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3860
PB  - Wiley
T2  - Allergy: European Journal of Allergy and Clinical Immunology
T1  - Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy
VL  - 75
IS  - 1
SP  - 217
EP  - 220
DO  - 10.1111/ALL.13978
ER  - 
@article{
author = "Apostolović, Danijela and Mihailović, Jelena and Commins, Scott P. and Wijnveld, Michiel and Kazimirova, Maria and Starkhammar, Maria and Stockinger, Hannes and Platts-Mills, Thomas A. E. and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2020",
publisher = "Wiley",
journal = "Allergy: European Journal of Allergy and Clinical Immunology",
title = "Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy",
volume = "75",
number = "1",
pages = "217-220",
doi = "10.1111/ALL.13978"
}
Apostolović, D., Mihailović, J., Commins, S. P., Wijnveld, M., Kazimirova, M., Starkhammar, M., Stockinger, H., Platts-Mills, T. A. E., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M.. (2020). Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy. in Allergy: European Journal of Allergy and Clinical Immunology
Wiley., 75(1), 217-220.
https://doi.org/10.1111/ALL.13978
Apostolović D, Mihailović J, Commins SP, Wijnveld M, Kazimirova M, Starkhammar M, Stockinger H, Platts-Mills TAE, Ćirković-Veličković T, Hamsten C, van Hage M. Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy. in Allergy: European Journal of Allergy and Clinical Immunology. 2020;75(1):217-220.
doi:10.1111/ALL.13978 .
Apostolović, Danijela, Mihailović, Jelena, Commins, Scott P., Wijnveld, Michiel, Kazimirova, Maria, Starkhammar, Maria, Stockinger, Hannes, Platts-Mills, Thomas A. E., Ćirković-Veličković, Tanja, Hamsten, Carl, van Hage, Marianne, "Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy" in Allergy: European Journal of Allergy and Clinical Immunology, 75, no. 1 (2020):217-220,
https://doi.org/10.1111/ALL.13978 . .
10
21
20
20

Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy

Apostolović, Danijela; Mihailović, Jelena; Commins, Scott P.; Wijnveld, Michiel; Kazimirova, Maria; Starkhammar, Maria; Stockinger, Hannes; Platts-Mills, Thomas A. E.; Ćirković-Veličković, Tanja; Hamsten, Carl; van Hage, Marianne

(Wiley, 2020)

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Commins, Scott P.
AU  - Wijnveld, Michiel
AU  - Kazimirova, Maria
AU  - Starkhammar, Maria
AU  - Stockinger, Hannes
AU  - Platts-Mills, Thomas A. E.
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3853
PB  - Wiley
T2  - Allergy: European Journal of Allergy and Clinical Immunology
T1  - Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy
VL  - 75
IS  - 1
SP  - 217
EP  - 220
DO  - 10.1111/all.13978
ER  - 
@article{
author = "Apostolović, Danijela and Mihailović, Jelena and Commins, Scott P. and Wijnveld, Michiel and Kazimirova, Maria and Starkhammar, Maria and Stockinger, Hannes and Platts-Mills, Thomas A. E. and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2020",
publisher = "Wiley",
journal = "Allergy: European Journal of Allergy and Clinical Immunology",
title = "Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy",
volume = "75",
number = "1",
pages = "217-220",
doi = "10.1111/all.13978"
}
Apostolović, D., Mihailović, J., Commins, S. P., Wijnveld, M., Kazimirova, M., Starkhammar, M., Stockinger, H., Platts-Mills, T. A. E., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M.. (2020). Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy. in Allergy: European Journal of Allergy and Clinical Immunology
Wiley., 75(1), 217-220.
https://doi.org/10.1111/all.13978
Apostolović D, Mihailović J, Commins SP, Wijnveld M, Kazimirova M, Starkhammar M, Stockinger H, Platts-Mills TAE, Ćirković-Veličković T, Hamsten C, van Hage M. Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy. in Allergy: European Journal of Allergy and Clinical Immunology. 2020;75(1):217-220.
doi:10.1111/all.13978 .
Apostolović, Danijela, Mihailović, Jelena, Commins, Scott P., Wijnveld, Michiel, Kazimirova, Maria, Starkhammar, Maria, Stockinger, Hannes, Platts-Mills, Thomas A. E., Ćirković-Veličković, Tanja, Hamsten, Carl, van Hage, Marianne, "Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy" in Allergy: European Journal of Allergy and Clinical Immunology, 75, no. 1 (2020):217-220,
https://doi.org/10.1111/all.13978 . .
10
21
20
20

Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978

Apostolović, Danijela; Mihailović, Jelena; Commins, Scott P.; Wijnveld, Michiel; Kazimirova, Maria; Starkhammar, Maria; Stockinger, Hannes; Platts-Mills, Thomas A. E.; Ćirković-Veličković, Tanja; Hamsten, Carl; van Hage, Marianne

(Wiley, 2020)

TY  - DATA
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Commins, Scott P.
AU  - Wijnveld, Michiel
AU  - Kazimirova, Maria
AU  - Starkhammar, Maria
AU  - Stockinger, Hannes
AU  - Platts-Mills, Thomas A. E.
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3864
PB  - Wiley
T2  - Allergy: European Journal of Allergy and Clinical Immunology
T1  - Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978
ER  - 
@misc{
author = "Apostolović, Danijela and Mihailović, Jelena and Commins, Scott P. and Wijnveld, Michiel and Kazimirova, Maria and Starkhammar, Maria and Stockinger, Hannes and Platts-Mills, Thomas A. E. and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2020",
publisher = "Wiley",
journal = "Allergy: European Journal of Allergy and Clinical Immunology",
title = "Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978"
}
Apostolović, D., Mihailović, J., Commins, S. P., Wijnveld, M., Kazimirova, M., Starkhammar, M., Stockinger, H., Platts-Mills, T. A. E., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M.. (2020). Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978. in Allergy: European Journal of Allergy and Clinical Immunology
Wiley..
Apostolović D, Mihailović J, Commins SP, Wijnveld M, Kazimirova M, Starkhammar M, Stockinger H, Platts-Mills TAE, Ćirković-Veličković T, Hamsten C, van Hage M. Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978. in Allergy: European Journal of Allergy and Clinical Immunology. 2020;..
Apostolović, Danijela, Mihailović, Jelena, Commins, Scott P., Wijnveld, Michiel, Kazimirova, Maria, Starkhammar, Maria, Stockinger, Hannes, Platts-Mills, Thomas A. E., Ćirković-Veličković, Tanja, Hamsten, Carl, van Hage, Marianne, "Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978" in Allergy: European Journal of Allergy and Clinical Immunology (2020).

Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis

Moons, Jens; de Azambuja, Francisco; Mihailović, Jelena; Kozma, Karoly; Smiljanić, Katarina; Amiri, Mehran; Ćirković-Veličković, Tanja; Nyman, May; Parac-Vogt, Tatjana

(Wiley, 2020)

TY  - JOUR
AU  - Moons, Jens
AU  - de Azambuja, Francisco
AU  - Mihailović, Jelena
AU  - Kozma, Karoly
AU  - Smiljanić, Katarina
AU  - Amiri, Mehran
AU  - Ćirković-Veličković, Tanja
AU  - Nyman, May
AU  - Parac-Vogt, Tatjana
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3917
AB  - The selective hydrolysis of proteins by non‐enzymatic catalysis is difficult to achieve, yet it is crucial for applications in biotechnology and proteomics. Herein, we report that discrete hafnium metal‐oxo cluster [Hf18O10(OH)26(SO4)13⋅(H2O)33] (Hf18), which is centred by the same hexamer motif found in many MOFs, acts as a heterogeneous catalyst for the efficient hydrolysis of horse heart myoglobin (HHM) in low buffer concentrations. Among 154 amino acids present in the sequence of HHM, strictly selective cleavage at only 6 solvent accessible aspartate residues was observed. Mechanistic experiments suggest that the hydrolytic activity is likely derived from the actuation of HfIV Lewis acidic sites and the Brønsted acidic surface of Hf18. X‐ray scattering and ESI‐MS revealed that Hf18 is completely insoluble in these conditions, confirming the HHM hydrolysis is caused by a heterogeneous reaction of the solid Hf18 cluster, and not from smaller, soluble Hf species that could leach into solution.
PB  - Wiley
T2  - Angewandte Chemie (International Edition)
T1  - Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis
VL  - 59
IS  - 17
SP  - 1
EP  - 9
DO  - 10.1002/anie.202001036
ER  - 
@article{
author = "Moons, Jens and de Azambuja, Francisco and Mihailović, Jelena and Kozma, Karoly and Smiljanić, Katarina and Amiri, Mehran and Ćirković-Veličković, Tanja and Nyman, May and Parac-Vogt, Tatjana",
year = "2020",
abstract = "The selective hydrolysis of proteins by non‐enzymatic catalysis is difficult to achieve, yet it is crucial for applications in biotechnology and proteomics. Herein, we report that discrete hafnium metal‐oxo cluster [Hf18O10(OH)26(SO4)13⋅(H2O)33] (Hf18), which is centred by the same hexamer motif found in many MOFs, acts as a heterogeneous catalyst for the efficient hydrolysis of horse heart myoglobin (HHM) in low buffer concentrations. Among 154 amino acids present in the sequence of HHM, strictly selective cleavage at only 6 solvent accessible aspartate residues was observed. Mechanistic experiments suggest that the hydrolytic activity is likely derived from the actuation of HfIV Lewis acidic sites and the Brønsted acidic surface of Hf18. X‐ray scattering and ESI‐MS revealed that Hf18 is completely insoluble in these conditions, confirming the HHM hydrolysis is caused by a heterogeneous reaction of the solid Hf18 cluster, and not from smaller, soluble Hf species that could leach into solution.",
publisher = "Wiley",
journal = "Angewandte Chemie (International Edition)",
title = "Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis",
volume = "59",
number = "17",
pages = "1-9",
doi = "10.1002/anie.202001036"
}
Moons, J., de Azambuja, F., Mihailović, J., Kozma, K., Smiljanić, K., Amiri, M., Ćirković-Veličković, T., Nyman, M.,& Parac-Vogt, T.. (2020). Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis. in Angewandte Chemie (International Edition)
Wiley., 59(17), 1-9.
https://doi.org/10.1002/anie.202001036
Moons J, de Azambuja F, Mihailović J, Kozma K, Smiljanić K, Amiri M, Ćirković-Veličković T, Nyman M, Parac-Vogt T. Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis. in Angewandte Chemie (International Edition). 2020;59(17):1-9.
doi:10.1002/anie.202001036 .
Moons, Jens, de Azambuja, Francisco, Mihailović, Jelena, Kozma, Karoly, Smiljanić, Katarina, Amiri, Mehran, Ćirković-Veličković, Tanja, Nyman, May, Parac-Vogt, Tatjana, "Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis" in Angewandte Chemie (International Edition), 59, no. 17 (2020):1-9,
https://doi.org/10.1002/anie.202001036 . .
22
11
10
12

Thermal Processing of Peanut Grains Impairs Their Mimicked Gastrointestinal Digestion While Downstream Defatting Treatments Affect Digestomic Profiles

Prodić, Ivana; Smiljanić, Katarina; Simović, Ana; Radosavljević, Jelena; Ćirković-Veličković, Tanja

(MDPI, 2019)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Simović, Ana
AU  - Radosavljević, Jelena
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3682
AB  - Resistance to digestion by digestive proteases represents a critical property of many food allergens. Recently, a harmonized INFOGEST protocol was proposed for solid food digestion. The protocol proposes digestion conditions suitable for all kinds of solid and liquid foods. However, peanuts, as a lipid-rich food, represent a challenge for downstream analyses of the digestome. This is particularly reflected in the methodological difficulties in analyzing proteins and peptides in the presence of lipids. Therefore, the removal of the lipids seems to be a prerequisite for the downstream analysis of digestomes of lipid-rich foods. Here, we aimed to compare the digestomes of raw and thermally treated (boiled and roasted) peanuts, resulting from the INFOGEST digestion protocol for solid food, upon defatting the digests in two different manners. The most reproducible results of peanut digests were obtained in downstream analyses on TCA/acetone defatting. Unfortunately, defatting, even with an optimized TCA/acetone procedure, leads to the loss of proteins and peptides. The results of our study reveal that different thermal treatments of peanuts affect protein extraction and gastric/gastrointestinal digestion. Roasting of peanuts seems to enhance the extraction of proteins during intestinal digestion to a notable extent. The increased intestinal digestion is a consequence of the delayed extraction of thermally treated peanut proteins, which are poorly soluble in acidic gastric digestion juice but are easily extracted when the pH of the media is raised as in the subsequent intestinal phase of the digestion. Thermal processing of peanuts impaired the gastrointestinal digestion of the peanut proteins, especially in the case of roasted samples
PB  - MDPI
T2  - Foods
T1  - Thermal Processing of Peanut Grains Impairs Their Mimicked Gastrointestinal Digestion While Downstream Defatting Treatments Affect Digestomic Profiles
VL  - 8
IS  - 10
SP  - 1
EP  - 18
DO  - https://doi.org/10.3390/foods8100463
ER  - 
@article{
author = "Prodić, Ivana and Smiljanić, Katarina and Simović, Ana and Radosavljević, Jelena and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Resistance to digestion by digestive proteases represents a critical property of many food allergens. Recently, a harmonized INFOGEST protocol was proposed for solid food digestion. The protocol proposes digestion conditions suitable for all kinds of solid and liquid foods. However, peanuts, as a lipid-rich food, represent a challenge for downstream analyses of the digestome. This is particularly reflected in the methodological difficulties in analyzing proteins and peptides in the presence of lipids. Therefore, the removal of the lipids seems to be a prerequisite for the downstream analysis of digestomes of lipid-rich foods. Here, we aimed to compare the digestomes of raw and thermally treated (boiled and roasted) peanuts, resulting from the INFOGEST digestion protocol for solid food, upon defatting the digests in two different manners. The most reproducible results of peanut digests were obtained in downstream analyses on TCA/acetone defatting. Unfortunately, defatting, even with an optimized TCA/acetone procedure, leads to the loss of proteins and peptides. The results of our study reveal that different thermal treatments of peanuts affect protein extraction and gastric/gastrointestinal digestion. Roasting of peanuts seems to enhance the extraction of proteins during intestinal digestion to a notable extent. The increased intestinal digestion is a consequence of the delayed extraction of thermally treated peanut proteins, which are poorly soluble in acidic gastric digestion juice but are easily extracted when the pH of the media is raised as in the subsequent intestinal phase of the digestion. Thermal processing of peanuts impaired the gastrointestinal digestion of the peanut proteins, especially in the case of roasted samples",
publisher = "MDPI",
journal = "Foods",
title = "Thermal Processing of Peanut Grains Impairs Their Mimicked Gastrointestinal Digestion While Downstream Defatting Treatments Affect Digestomic Profiles",
volume = "8",
number = "10",
pages = "1-18",
doi = "https://doi.org/10.3390/foods8100463"
}
Prodić, I., Smiljanić, K., Simović, A., Radosavljević, J.,& Ćirković-Veličković, T.. (2019). Thermal Processing of Peanut Grains Impairs Their Mimicked Gastrointestinal Digestion While Downstream Defatting Treatments Affect Digestomic Profiles. in Foods
MDPI., 8(10), 1-18.
https://doi.org/https://doi.org/10.3390/foods8100463
Prodić I, Smiljanić K, Simović A, Radosavljević J, Ćirković-Veličković T. Thermal Processing of Peanut Grains Impairs Their Mimicked Gastrointestinal Digestion While Downstream Defatting Treatments Affect Digestomic Profiles. in Foods. 2019;8(10):1-18.
doi:https://doi.org/10.3390/foods8100463 .
Prodić, Ivana, Smiljanić, Katarina, Simović, Ana, Radosavljević, Jelena, Ćirković-Veličković, Tanja, "Thermal Processing of Peanut Grains Impairs Their Mimicked Gastrointestinal Digestion While Downstream Defatting Treatments Affect Digestomic Profiles" in Foods, 8, no. 10 (2019):1-18,
https://doi.org/https://doi.org/10.3390/foods8100463 . .
1
2

Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu

Mihailović, Jelena

(Универзитет у Београду, Хемијски факултет, 2019)

TY  - THES
AU  - Mihailović, Jelena
PY  - 2019
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=7675
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:22858/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=24146185
UR  - https://nardus.mpn.gov.rs/handle/123456789/17611
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4381
AB  - Alergija na hranu je reakcija preosetljivosti imunskog sistema na hranu koja dovodi dostvaranja IgE antitela. Ne postoji efikasan tretman i izbegavanje namirnica koje izazivajusimptome je jedini način za sprečavanje ozbiljnih posledica. Cilj ove teze je izučavanjeposttranslacionih i hemijskih modifikacija (PTM i HM) i interakcija alergena hrane sabiološki aktivnim polifenolom biljnog porekla.Alergija na crveno meso je novootkriveni tip odložene reakcije, sa PTM galaktozil-α-1,3-galaktozom (α-Gal) kao epitopom. Ispitani su podložnost model proteina - tiroglobulina(TG) digestiji pepsinom, prisustvo α-Gal na rezultujućim peptidima i pretpostavljenomesto vezivanja α-Gal za TG. Pokazano je da je α-Gal celim tokom simulirane želudačnedigestije vezan za nastale peptide TG, koji zadržavaju sposobnost da vežu IgE.Alergija na kikiriki je među najopasnijim zbog učestalosti, postojanosti i ozbiljnostisimptoma. Postoje razlike u alergenosti između sirovog i pečenog kikirikija, koje mogupoticati od razlika u modifikacijama alergena. U ovoj disertaciji je proučena razlika umodifikacijama glavnih alergena iz sirovog i pečenog kikirikija. Detektovano je 27modifikacija, od kojih 4 isključivo na proteinima pečenog kikirikija. Pokazane su razlikeu profilima modifikacija proteina između ekstrakata, koje mogu uticati na alergenost.2S albumini kikirikija su zbog kompaktne strukture otporni na delovanje digestivnihenzima, što se povezuje sa njihovom alergenošću. Ispitane su interakcije između njih iepigalokatehin-3-galata (EGCG), katehina zelenog čaja sa imunomodulatornimsvojstvima koji pospešuje digestiju proteina pepsinom. Vezivanje EGCG-a za alergeneizaziva promene u njihovoj strukturi (entalpijski povoljan proces), sa konstantamavezivanja reda veličine 104 M-1.
AB  - Food allergy is an immune system reaction to certain foods that results in IgE antibodygeneration. Efficient treatment does not exist, so avoidance of trigger foods is the onlyway to prevent serious consequences. The aim of this thesis was to study posttranslationaland chemical modifications (PTM and CM) of food allergens and their interactions withbiologically active plant polyphenol.Red meat allergy is a newly discovered type of allergy with delayed symptoms and aPTM - galactose-α-1,3-galactose (α-Gal) as an epitope. Digestibility of a model protein -thyroglobulin (TG) by pepsin and presence of α-Gal on resulting peptides was studied,and the position of α-Gal containing glycan on TG was proposed. It was shown thatthroughout simulated gastric digestion α-Gal remains bound to IgE reactive TG peptides.Peanut allergy is among most dangerous types of food allergies due to prevalence,persistence and symptom severity. Differences in allergenicity between raw and roastedpeanuts were previously shown and might stem from differences in protein modifications.Differences in major allergen modifications between raw and roasted peanut werestudied. Twenty-seven modifications were detected, 4 of which exclusively on allergensfrom roasted peanuts. Differences in modification profiling were found between the twoprotein preparations that can affect their allergenicity.Peanut 2S albumins are compact digestion-resistant proteins, which attributes to theirallergenicity. Their interactions with epigallocatechin-3-gallate (EGCG), animmunomodulatory green tea catechin that facilitates pepsin digestion of proteins werestudied. The results show that binding of EGCG to these allergens induces conformationalchanges, and is enthalpy favorable with binding constants of 104 M-1.
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu
ER  - 
@phdthesis{
author = "Mihailović, Jelena",
year = "2019",
abstract = "Alergija na hranu je reakcija preosetljivosti imunskog sistema na hranu koja dovodi dostvaranja IgE antitela. Ne postoji efikasan tretman i izbegavanje namirnica koje izazivajusimptome je jedini način za sprečavanje ozbiljnih posledica. Cilj ove teze je izučavanjeposttranslacionih i hemijskih modifikacija (PTM i HM) i interakcija alergena hrane sabiološki aktivnim polifenolom biljnog porekla.Alergija na crveno meso je novootkriveni tip odložene reakcije, sa PTM galaktozil-α-1,3-galaktozom (α-Gal) kao epitopom. Ispitani su podložnost model proteina - tiroglobulina(TG) digestiji pepsinom, prisustvo α-Gal na rezultujućim peptidima i pretpostavljenomesto vezivanja α-Gal za TG. Pokazano je da je α-Gal celim tokom simulirane želudačnedigestije vezan za nastale peptide TG, koji zadržavaju sposobnost da vežu IgE.Alergija na kikiriki je među najopasnijim zbog učestalosti, postojanosti i ozbiljnostisimptoma. Postoje razlike u alergenosti između sirovog i pečenog kikirikija, koje mogupoticati od razlika u modifikacijama alergena. U ovoj disertaciji je proučena razlika umodifikacijama glavnih alergena iz sirovog i pečenog kikirikija. Detektovano je 27modifikacija, od kojih 4 isključivo na proteinima pečenog kikirikija. Pokazane su razlikeu profilima modifikacija proteina između ekstrakata, koje mogu uticati na alergenost.2S albumini kikirikija su zbog kompaktne strukture otporni na delovanje digestivnihenzima, što se povezuje sa njihovom alergenošću. Ispitane su interakcije između njih iepigalokatehin-3-galata (EGCG), katehina zelenog čaja sa imunomodulatornimsvojstvima koji pospešuje digestiju proteina pepsinom. Vezivanje EGCG-a za alergeneizaziva promene u njihovoj strukturi (entalpijski povoljan proces), sa konstantamavezivanja reda veličine 104 M-1., Food allergy is an immune system reaction to certain foods that results in IgE antibodygeneration. Efficient treatment does not exist, so avoidance of trigger foods is the onlyway to prevent serious consequences. The aim of this thesis was to study posttranslationaland chemical modifications (PTM and CM) of food allergens and their interactions withbiologically active plant polyphenol.Red meat allergy is a newly discovered type of allergy with delayed symptoms and aPTM - galactose-α-1,3-galactose (α-Gal) as an epitope. Digestibility of a model protein -thyroglobulin (TG) by pepsin and presence of α-Gal on resulting peptides was studied,and the position of α-Gal containing glycan on TG was proposed. It was shown thatthroughout simulated gastric digestion α-Gal remains bound to IgE reactive TG peptides.Peanut allergy is among most dangerous types of food allergies due to prevalence,persistence and symptom severity. Differences in allergenicity between raw and roastedpeanuts were previously shown and might stem from differences in protein modifications.Differences in major allergen modifications between raw and roasted peanut werestudied. Twenty-seven modifications were detected, 4 of which exclusively on allergensfrom roasted peanuts. Differences in modification profiling were found between the twoprotein preparations that can affect their allergenicity.Peanut 2S albumins are compact digestion-resistant proteins, which attributes to theirallergenicity. Their interactions with epigallocatechin-3-gallate (EGCG), animmunomodulatory green tea catechin that facilitates pepsin digestion of proteins werestudied. The results show that binding of EGCG to these allergens induces conformationalchanges, and is enthalpy favorable with binding constants of 104 M-1.",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu"
}
Mihailović, J.. (2019). Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
Mihailović J. Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu. in Универзитет у Београду. 2019;..
Mihailović, Jelena, "Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu" in Универзитет у Београду (2019).

Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu

Prodić, Ivana

(Универзитет у Београду, Хемијски факултет, 2019)

TY  - THES
AU  - Prodić, Ivana
PY  - 2019
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=7705
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:22917/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=23935753
UR  - https://nardus.mpn.gov.rs/handle/123456789/17617
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4384
AB  - INFOGEST metoda predstavlja standardizovani protokol za in vitro simulacijudigestije kompletne hrane, zasnovanom na fiziološki relevantnim uslovima. Predmetrada ove disertacije je ispitivanje digestibilnosti alergena kikirikija iz celog zrnaprimenom INFOGEST metode, kao i karakterizacija njihovih fragmenata otpornih naproteolizu.Za odstranjivanje lipida primenjena je metoda taloženja proteina, koja se pokazala kaosuperiornija u odnosu ekstrakciju lipida organskim rastvaračem, usled manjegkvalitativnog i kvantitativnog gubitka proteina.U ovoj tezi je pokazano da termički tretmani kikirikija, pored matriksa hrane, dodatnootežavaju oslobađanje proteina iz zrna, što čini glavne alergene kikirikija Ara h 1, Ara h2 Ara h 3 i Ara h 6 nedostupnijim za pepsinsku hidrolizu. Oslobađanje proteinakikirikija, kao i digestibilnost, u gastričnoj fazi se pokazala znatno izraženijom, uodnosu na intestinalnu fazu, s tim da je digestija kod pečenog kikirikija otežana uodnosu na sirovi. Nakon oralno-gastrične digestije celog zrna sirovog kikirikija, glavnialergeni kikirikija u velikoj meri ostaju intaktni, a njihovi peptidi otporni na digestijuzadržavaju alergeni kapacitet. Pokazano je da većina Ara h 2 i Ara h 6 alergena ostajerezistentna na digestiju. Ara h 1 i Ara h 3 kaskadno podležu pepsinolizi, do fragmenatakoji i dalje zadržavaju IgE vezujući potencijal. Mali peptidi koji potiču od Ara h 2alergena, su se pokazali kao najpotentniji inhibitori vezivanja IgE iz seruma pacijenataalergičnih na kikiriki, u odnosu na male Ara h 1 i Ara h 3 peptide.U ovoj disertaciji je pokazana izuzetno važna uloga efekata matriksa hrane, kao i njenetermičke obrade, na digestiju proteina hrane, koji mogu povećati stabilnost alergenahrane tokom digestije, i time omogućiti zadržavanje potencijala aktivacije alergijskereakcije nakon oralno-gastrične faze digestije.
AB  - INFOGEST method is standardized protocol for in vitro simulation of complete fooddigestion, based on physiologicaly relevant conditions. The objective of thisdissertation was to investigate digestibility of peanut allergens from whole peanutkernel by INFOGEST method, as well as to characterize their fragments resistant toproteolysis.For delipidation, protein precipitation approach was applied, showing to be superior incomparison to delipidation by organic solevent, due to lower qualitative andquantitative protein loss.In this thesis it was shown that peanut thermal processing, in addition to effect of foodmatix, further complicates the extractability and digestibility of proteins from the grain,making peanut allergens Ara h 1, 2, 3 and 6, less accessible for pepsin hydrolysis.Extractability and digestibility of peanut proteins in the gastric phase have shown to besignificantly more pronounced, in comparison to intestinal phase, and roasted peanutdigestion was impaired compared to the raw. It was shown that after oral and gastricdigestion of whole raw peanut grains peanut allergens largely remain intact, and theirdigestion resistant peptides retain allergenic capacity. The most Ara h 2 and Ara h 6allergens have been shown to remain resistant to digestion. Ara h 1 and Ara h 3undergo pepsinolysis with cascade pattern to consequently smaller peptide fragmentswith retained IgE binding capacity. Small peptides from Ara h 2 allergens were themost potent inhibitors of IgE binding from sera of peanut allergic patients, compared tosmall peptides from Ara h 1 and Ara h 3.This thesis points to the great importance of the effects of food matrix, as well as foodthermal processing, on protein digestibility, which can create additional stability offood allergens during digestion, and thus enable retaining of their potential for thesensitization or triggering of allergic reactions.
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu
ER  - 
@phdthesis{
author = "Prodić, Ivana",
year = "2019",
abstract = "INFOGEST metoda predstavlja standardizovani protokol za in vitro simulacijudigestije kompletne hrane, zasnovanom na fiziološki relevantnim uslovima. Predmetrada ove disertacije je ispitivanje digestibilnosti alergena kikirikija iz celog zrnaprimenom INFOGEST metode, kao i karakterizacija njihovih fragmenata otpornih naproteolizu.Za odstranjivanje lipida primenjena je metoda taloženja proteina, koja se pokazala kaosuperiornija u odnosu ekstrakciju lipida organskim rastvaračem, usled manjegkvalitativnog i kvantitativnog gubitka proteina.U ovoj tezi je pokazano da termički tretmani kikirikija, pored matriksa hrane, dodatnootežavaju oslobađanje proteina iz zrna, što čini glavne alergene kikirikija Ara h 1, Ara h2 Ara h 3 i Ara h 6 nedostupnijim za pepsinsku hidrolizu. Oslobađanje proteinakikirikija, kao i digestibilnost, u gastričnoj fazi se pokazala znatno izraženijom, uodnosu na intestinalnu fazu, s tim da je digestija kod pečenog kikirikija otežana uodnosu na sirovi. Nakon oralno-gastrične digestije celog zrna sirovog kikirikija, glavnialergeni kikirikija u velikoj meri ostaju intaktni, a njihovi peptidi otporni na digestijuzadržavaju alergeni kapacitet. Pokazano je da većina Ara h 2 i Ara h 6 alergena ostajerezistentna na digestiju. Ara h 1 i Ara h 3 kaskadno podležu pepsinolizi, do fragmenatakoji i dalje zadržavaju IgE vezujući potencijal. Mali peptidi koji potiču od Ara h 2alergena, su se pokazali kao najpotentniji inhibitori vezivanja IgE iz seruma pacijenataalergičnih na kikiriki, u odnosu na male Ara h 1 i Ara h 3 peptide.U ovoj disertaciji je pokazana izuzetno važna uloga efekata matriksa hrane, kao i njenetermičke obrade, na digestiju proteina hrane, koji mogu povećati stabilnost alergenahrane tokom digestije, i time omogućiti zadržavanje potencijala aktivacije alergijskereakcije nakon oralno-gastrične faze digestije., INFOGEST method is standardized protocol for in vitro simulation of complete fooddigestion, based on physiologicaly relevant conditions. The objective of thisdissertation was to investigate digestibility of peanut allergens from whole peanutkernel by INFOGEST method, as well as to characterize their fragments resistant toproteolysis.For delipidation, protein precipitation approach was applied, showing to be superior incomparison to delipidation by organic solevent, due to lower qualitative andquantitative protein loss.In this thesis it was shown that peanut thermal processing, in addition to effect of foodmatix, further complicates the extractability and digestibility of proteins from the grain,making peanut allergens Ara h 1, 2, 3 and 6, less accessible for pepsin hydrolysis.Extractability and digestibility of peanut proteins in the gastric phase have shown to besignificantly more pronounced, in comparison to intestinal phase, and roasted peanutdigestion was impaired compared to the raw. It was shown that after oral and gastricdigestion of whole raw peanut grains peanut allergens largely remain intact, and theirdigestion resistant peptides retain allergenic capacity. The most Ara h 2 and Ara h 6allergens have been shown to remain resistant to digestion. Ara h 1 and Ara h 3undergo pepsinolysis with cascade pattern to consequently smaller peptide fragmentswith retained IgE binding capacity. Small peptides from Ara h 2 allergens were themost potent inhibitors of IgE binding from sera of peanut allergic patients, compared tosmall peptides from Ara h 1 and Ara h 3.This thesis points to the great importance of the effects of food matrix, as well as foodthermal processing, on protein digestibility, which can create additional stability offood allergens during digestion, and thus enable retaining of their potential for thesensitization or triggering of allergic reactions.",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu"
}
Prodić, I.. (2019). Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
Prodić I. Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu. in Универзитет у Београду. 2019;..
Prodić, Ivana, "Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu" in Универзитет у Београду (2019).

Struktura i funkcija proteina mleka modifikovanih u Majarovoj reakciji

Peruško, Marija

(Универзитет у Београду, Хемијски факултет, 2019)

TY  - THES
AU  - Peruško, Marija
PY  - 2019
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=7689
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:22883/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=24283145
UR  - https://nardus.mpn.gov.rs/handle/123456789/17612
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4385
AB  - Majarova reakcija (MR) je spontana reakcija izmeĊu karbonilne i amino grupe iod velikog je znaĉaja u hemiji hrane. Proteini modifikovani u MR imaju poboljšanetehno-funkcionalne osobine i nalaze primenu u prehrambenoj industriji. TakoĊe,strukture Majarovih proizvoda modifikovanih proteina imaju brojne efekte naalergenost proteina hrane.Predmet rada ove disertacije bilo je ispitivanje efekata MR indukovaneultrazvukom ili sušenjem raspršivanjem na fiziĉko-hemijske i tehno-funkcionalneosobine kravlje surutke i kamiljeg mleka, kao i efekata intenzivnog glikovanja u MR naimunološke osobine glavnog alergena kravljeg mleka, β-laktoglobulina (BLG).Kombinovana primena ultrazvuka i makromolekulskog nagomilavanja jeznaĉajnije ubrzala MR i glikovanje proteina nego sam ultrazvuĉni tretman.Makromolekulsko nagomilavanje, preko ubrzavanja MR, povećava oksidativnepromene na proteinima i formiranje struktura sliĉnih amiloidima. Visoko glikovaniproteini surutke su pokazali poboljšanu rastvorljivost u širokom pH i temperaturnomopsegu, kao i povećanu antioksidativnu moć.U kamiljem mleku u prahu sušenom raspršivanjem više temperature (230 °C –250 °C) su rezultirale većim stepenom MR u odnosu na niže temperature sušenja (190°C – 210 °C). Poboljšanje tehno-funkcionalnih osobina proteina kamiljeg mleka uprahu, kao što su antioksidativna moć i rastvorljivost, je pozitivno koreliralo sastepenom MR.Glikovanje BLG u MR, dovelo je do njegovog smanjenog transporta kroz modelsistem intestinalne barijere, povećanog preuzimanja od strane dendritskih ćelija,smanjenog luĉenja citokina u mešovitoj kulturi dendritskih ćelija sa CD4+ T-ćelijama, ido smanjene aktivacije bazofila, ukazujući da modifikovanje BLG u MR znaĉajnomenja njegovu sudbinu u procesima koji odreĊuju alergenost proteina mleka.
AB  - Maillard reaction (MR) is a spontaneous reaction between carbonil and aminogroup, and it is of high importance in food chemistry. Proteins modified in MR possessimproved techno-functional properties and they have application in food industry. MRproducts of food proteins exert numerous effects on food proteins allergenicity.The subject of this doctoral dissertation was to examine the effects of MRinduced by ultrasound or spray-drying on phisyco-chemical and techno-functionalproperties of cow whey proteins and camel milk proteins, as well as the effects of MRon immunologic properties of major cow milk allergen, β-lactoglobulin (BLG).Combined application of ultrasound and macromolecular crowding enhancedMR to a greater extent than ultrasound treatment alone. Macromolecular crowdingindirectly, by enhancing MR, intensified oxidative modifications of whey proteins andformation of amyloid-like structures. Highly glycated proteins exhibited improvedsolubility in wide pH range, thermal stability and antioxidative power.Upon spray-drying treatment of camel milk, higher temperatures (230 °C – 250°C) induced higher degree of MR compared to lower drying temperatures (190 °C – 210°C). Improvement of techno-functional properties of camel milk proteins, such asantioxidative power and solubility, strongly correlated with the degree of MR.Intensive glycation of BLG in MR reduced its transport through the modelsystem of intestinal barrier, increased uptake by dendritic cells and decreased cytokineproduction in dendritic cells/CD4+ T-cells coculture, as well as reduced basophilactivation, indicating that modification of BLG in MR alters its fate in processescrucially involved in allergenicity of milk proteins.
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Struktura i funkcija proteina mleka modifikovanih u Majarovoj reakciji
ER  - 
@phdthesis{
author = "Peruško, Marija",
year = "2019",
abstract = "Majarova reakcija (MR) je spontana reakcija izmeĊu karbonilne i amino grupe iod velikog je znaĉaja u hemiji hrane. Proteini modifikovani u MR imaju poboljšanetehno-funkcionalne osobine i nalaze primenu u prehrambenoj industriji. TakoĊe,strukture Majarovih proizvoda modifikovanih proteina imaju brojne efekte naalergenost proteina hrane.Predmet rada ove disertacije bilo je ispitivanje efekata MR indukovaneultrazvukom ili sušenjem raspršivanjem na fiziĉko-hemijske i tehno-funkcionalneosobine kravlje surutke i kamiljeg mleka, kao i efekata intenzivnog glikovanja u MR naimunološke osobine glavnog alergena kravljeg mleka, β-laktoglobulina (BLG).Kombinovana primena ultrazvuka i makromolekulskog nagomilavanja jeznaĉajnije ubrzala MR i glikovanje proteina nego sam ultrazvuĉni tretman.Makromolekulsko nagomilavanje, preko ubrzavanja MR, povećava oksidativnepromene na proteinima i formiranje struktura sliĉnih amiloidima. Visoko glikovaniproteini surutke su pokazali poboljšanu rastvorljivost u širokom pH i temperaturnomopsegu, kao i povećanu antioksidativnu moć.U kamiljem mleku u prahu sušenom raspršivanjem više temperature (230 °C –250 °C) su rezultirale većim stepenom MR u odnosu na niže temperature sušenja (190°C – 210 °C). Poboljšanje tehno-funkcionalnih osobina proteina kamiljeg mleka uprahu, kao što su antioksidativna moć i rastvorljivost, je pozitivno koreliralo sastepenom MR.Glikovanje BLG u MR, dovelo je do njegovog smanjenog transporta kroz modelsistem intestinalne barijere, povećanog preuzimanja od strane dendritskih ćelija,smanjenog luĉenja citokina u mešovitoj kulturi dendritskih ćelija sa CD4+ T-ćelijama, ido smanjene aktivacije bazofila, ukazujući da modifikovanje BLG u MR znaĉajnomenja njegovu sudbinu u procesima koji odreĊuju alergenost proteina mleka., Maillard reaction (MR) is a spontaneous reaction between carbonil and aminogroup, and it is of high importance in food chemistry. Proteins modified in MR possessimproved techno-functional properties and they have application in food industry. MRproducts of food proteins exert numerous effects on food proteins allergenicity.The subject of this doctoral dissertation was to examine the effects of MRinduced by ultrasound or spray-drying on phisyco-chemical and techno-functionalproperties of cow whey proteins and camel milk proteins, as well as the effects of MRon immunologic properties of major cow milk allergen, β-lactoglobulin (BLG).Combined application of ultrasound and macromolecular crowding enhancedMR to a greater extent than ultrasound treatment alone. Macromolecular crowdingindirectly, by enhancing MR, intensified oxidative modifications of whey proteins andformation of amyloid-like structures. Highly glycated proteins exhibited improvedsolubility in wide pH range, thermal stability and antioxidative power.Upon spray-drying treatment of camel milk, higher temperatures (230 °C – 250°C) induced higher degree of MR compared to lower drying temperatures (190 °C – 210°C). Improvement of techno-functional properties of camel milk proteins, such asantioxidative power and solubility, strongly correlated with the degree of MR.Intensive glycation of BLG in MR reduced its transport through the modelsystem of intestinal barrier, increased uptake by dendritic cells and decreased cytokineproduction in dendritic cells/CD4+ T-cells coculture, as well as reduced basophilactivation, indicating that modification of BLG in MR alters its fate in processescrucially involved in allergenicity of milk proteins.",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Struktura i funkcija proteina mleka modifikovanih u Majarovoj reakciji"
}
Peruško, M.. (2019). Struktura i funkcija proteina mleka modifikovanih u Majarovoj reakciji. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
Peruško M. Struktura i funkcija proteina mleka modifikovanih u Majarovoj reakciji. in Универзитет у Београду. 2019;..
Peruško, Marija, "Struktura i funkcija proteina mleka modifikovanih u Majarovoj reakciji" in Универзитет у Београду (2019).

Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija M.; Ćirković-Veličković, Tanja

(Belgrade : Faculty of Chemistry, 2019)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3742
AB  - Field-realistic exposure studies provide the most relevant assessment of the
effects of the intensity and diversity of urban and industrial contamination on
pollen structure and allergenicity. The significance of in-depth post-translational
modification (PTM) studies of pollen proteomes, when compared with studies on
other aspects of pollution and altered pollen allergenicity, has not yet been
determined; hence, little progress has been made within this field.
PB  - Belgrade : Faculty of Chemistry
C3  - 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia
T1  - Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments
SP  - 6
EP  - 7
ER  - 
@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Field-realistic exposure studies provide the most relevant assessment of the
effects of the intensity and diversity of urban and industrial contamination on
pollen structure and allergenicity. The significance of in-depth post-translational
modification (PTM) studies of pollen proteomes, when compared with studies on
other aspects of pollution and altered pollen allergenicity, has not yet been
determined; hence, little progress has been made within this field.",
publisher = "Belgrade : Faculty of Chemistry",
journal = "1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia",
title = "Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments",
pages = "6-7"
}
Smiljanić, K., Prodić, I., Apostolović, D., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2019). Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments. in 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia
Belgrade : Faculty of Chemistry., 6-7.
Smiljanić K, Prodić I, Apostolović D, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments. in 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia. 2019;:6-7..
Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija M., Ćirković-Veličković, Tanja, "Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments" in 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia (2019):6-7.

Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija M.; Ćirković-Veličković, Tanja

(2019)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3763
AB  - The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. 
Therefore, we created a comprehensive approach for the comparison of pollen from polluted and environmentally preserved areas. To examine the effects of long-term, in vivo pollen exposure to multiple source pollutants, Phleum pratense (Timothy grass) pollen samples were collected along a regional road in Kruševac, central Serbia and were compared with pollen samples from rural, environmentally preserved area over two consecutive pollination seasons. We combined the quantitative comparison of proteome expression profiles from in-solution and 2D-gels with unrestrictive in-depth quantitative PTM profiling using high resolution tandem mass spectrometry and the PEAKS 8.5 Suite platform.
An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, and significantly higher content of mercury, cadmium, and manganese. Antioxidative defense-related enzymes were significantly upregulated. Seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected pollen allergens, especially Phl p 6, with several different oxidative modifications. 
Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach was used for the first time to map extensive modifications in the pollen proteome, reflecting increased environmental oxidative stress, primarily caused by increased content of heavy metals in pollen.
C3  - XIV Italian Proteomics Association Annual Meeting with HPS, 2019.
T1  - Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution
SP  - 38
EP  - 38
ER  - 
@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. 
Therefore, we created a comprehensive approach for the comparison of pollen from polluted and environmentally preserved areas. To examine the effects of long-term, in vivo pollen exposure to multiple source pollutants, Phleum pratense (Timothy grass) pollen samples were collected along a regional road in Kruševac, central Serbia and were compared with pollen samples from rural, environmentally preserved area over two consecutive pollination seasons. We combined the quantitative comparison of proteome expression profiles from in-solution and 2D-gels with unrestrictive in-depth quantitative PTM profiling using high resolution tandem mass spectrometry and the PEAKS 8.5 Suite platform.
An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, and significantly higher content of mercury, cadmium, and manganese. Antioxidative defense-related enzymes were significantly upregulated. Seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected pollen allergens, especially Phl p 6, with several different oxidative modifications. 
Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach was used for the first time to map extensive modifications in the pollen proteome, reflecting increased environmental oxidative stress, primarily caused by increased content of heavy metals in pollen.",
journal = "XIV Italian Proteomics Association Annual Meeting with HPS, 2019.",
title = "Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution",
pages = "38-38"
}
Smiljanić, K., Prodić, I., Apostolović, D., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2019). Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution. in XIV Italian Proteomics Association Annual Meeting with HPS, 2019., 38-38.
Smiljanić K, Prodić I, Apostolović D, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution. in XIV Italian Proteomics Association Annual Meeting with HPS, 2019.. 2019;:38-38..
Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija M., Ćirković-Veličković, Tanja, "Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution" in XIV Italian Proteomics Association Annual Meeting with HPS, 2019. (2019):38-38.

Hypersensitivity reactions to antiepileptic drugs in children

Atanasković-Marković, Marina; Janković, Jelena; Tmušić, Vladimir; Gavrović-Jankulović, Marija; Ćirković-Veličković, Tanja; Nikolić, Dimitrije; Škorić, Dejan

(John Wiley and Sons Ltd., 2019)

TY  - JOUR
AU  - Atanasković-Marković, Marina
AU  - Janković, Jelena
AU  - Tmušić, Vladimir
AU  - Gavrović-Jankulović, Marija
AU  - Ćirković-Veličković, Tanja
AU  - Nikolić, Dimitrije
AU  - Škorić, Dejan
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3704
AB  - Background: Antiepileptic drugs (AEDs) can cause hypersensitivity reactions in children. These reactions are mainly cutaneous, self-limiting, and benign, but life-threatening severe cutaneous adverse reactions can occur. Infections can lead to skin eruptions and mimic drug hypersensitivity reactions, if a drug is taken at the same time. The aims of our study were to confirm or rule out the diagnosis of hypersensitivity reactions to AEDs in children and to detect an infection which mimics these reactions. Methods: A prospective survey was conducted in a group of 100 children with histories of hypersensitivity reactions to AEDs by performing patch tests, delayed-reading intradermal test, and, in case of negative results, challenge test. In all children, a study was performed to detect infections by viruses or Mycoplasma pneumoniae. Results: Maculopapular exanthema and delayed-appearing urticaria were the most reported hypersensitivity reactions to AEDs. Sixty-six (66%) of 100 children had confirmed hypersensitivity reactions to AEDs. Fifty-nine children had positive patch test. No children had positive challenge tests. The most common AEDs causing hypersensitivity reactions were carbamazepine (45.4%) and lamotrigine (43.6%). Thirty-two children had positive tests for viruses or M pneumoniae, and nine of them had also a positive allergy work-up. Conclusion: Considering that there are no specific tests to distinguish between a viral infection and hypersensitivity reactions to AEDs in the acute phase, a diagnostic work-up should be performed in all children with suspected hypersensitivity reactions to AEDs, as well as infectious agent study, to remove a false label of hypersensitivity.
PB  - John Wiley and Sons Ltd.
T2  - Pediatric Allergy and Immunology
T1  - Hypersensitivity reactions to antiepileptic drugs in children
VL  - 30
IS  - 5
SP  - 547
EP  - 552
DO  - 10.1111/pai.13055
ER  - 
@article{
author = "Atanasković-Marković, Marina and Janković, Jelena and Tmušić, Vladimir and Gavrović-Jankulović, Marija and Ćirković-Veličković, Tanja and Nikolić, Dimitrije and Škorić, Dejan",
year = "2019",
abstract = "Background: Antiepileptic drugs (AEDs) can cause hypersensitivity reactions in children. These reactions are mainly cutaneous, self-limiting, and benign, but life-threatening severe cutaneous adverse reactions can occur. Infections can lead to skin eruptions and mimic drug hypersensitivity reactions, if a drug is taken at the same time. The aims of our study were to confirm or rule out the diagnosis of hypersensitivity reactions to AEDs in children and to detect an infection which mimics these reactions. Methods: A prospective survey was conducted in a group of 100 children with histories of hypersensitivity reactions to AEDs by performing patch tests, delayed-reading intradermal test, and, in case of negative results, challenge test. In all children, a study was performed to detect infections by viruses or Mycoplasma pneumoniae. Results: Maculopapular exanthema and delayed-appearing urticaria were the most reported hypersensitivity reactions to AEDs. Sixty-six (66%) of 100 children had confirmed hypersensitivity reactions to AEDs. Fifty-nine children had positive patch test. No children had positive challenge tests. The most common AEDs causing hypersensitivity reactions were carbamazepine (45.4%) and lamotrigine (43.6%). Thirty-two children had positive tests for viruses or M pneumoniae, and nine of them had also a positive allergy work-up. Conclusion: Considering that there are no specific tests to distinguish between a viral infection and hypersensitivity reactions to AEDs in the acute phase, a diagnostic work-up should be performed in all children with suspected hypersensitivity reactions to AEDs, as well as infectious agent study, to remove a false label of hypersensitivity.",
publisher = "John Wiley and Sons Ltd.",
journal = "Pediatric Allergy and Immunology",
title = "Hypersensitivity reactions to antiepileptic drugs in children",
volume = "30",
number = "5",
pages = "547-552",
doi = "10.1111/pai.13055"
}
Atanasković-Marković, M., Janković, J., Tmušić, V., Gavrović-Jankulović, M., Ćirković-Veličković, T., Nikolić, D.,& Škorić, D.. (2019). Hypersensitivity reactions to antiepileptic drugs in children. in Pediatric Allergy and Immunology
John Wiley and Sons Ltd.., 30(5), 547-552.
https://doi.org/10.1111/pai.13055
Atanasković-Marković M, Janković J, Tmušić V, Gavrović-Jankulović M, Ćirković-Veličković T, Nikolić D, Škorić D. Hypersensitivity reactions to antiepileptic drugs in children. in Pediatric Allergy and Immunology. 2019;30(5):547-552.
doi:10.1111/pai.13055 .
Atanasković-Marković, Marina, Janković, Jelena, Tmušić, Vladimir, Gavrović-Jankulović, Marija, Ćirković-Veličković, Tanja, Nikolić, Dimitrije, Škorić, Dejan, "Hypersensitivity reactions to antiepileptic drugs in children" in Pediatric Allergy and Immunology, 30, no. 5 (2019):547-552,
https://doi.org/10.1111/pai.13055 . .
1
7
7
7

Characterisation and the effects of bilirubin binding to human fibrinogen

Gligorijević, Nikola; Minić, Simeon L.; Robajac, Dragana B.; Nikolić, Milan; Ćirković-Veličković, Tanja; Nedić, Olgica

(2019)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Robajac, Dragana B.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
AU  - Nedić, Olgica
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2824
AB  - Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventing its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction.
T2  - International Journal of Biological Macromolecules
T1  - Characterisation and the effects of bilirubin binding to human fibrinogen
VL  - 128
SP  - 74
EP  - 79
DO  - 10.1016/j.ijbiomac.2019.01.124
ER  - 
@article{
author = "Gligorijević, Nikola and Minić, Simeon L. and Robajac, Dragana B. and Nikolić, Milan and Ćirković-Veličković, Tanja and Nedić, Olgica",
year = "2019",
abstract = "Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventing its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction.",
journal = "International Journal of Biological Macromolecules",
title = "Characterisation and the effects of bilirubin binding to human fibrinogen",
volume = "128",
pages = "74-79",
doi = "10.1016/j.ijbiomac.2019.01.124"
}
Gligorijević, N., Minić, S. L., Robajac, D. B., Nikolić, M., Ćirković-Veličković, T.,& Nedić, O.. (2019). Characterisation and the effects of bilirubin binding to human fibrinogen. in International Journal of Biological Macromolecules, 128, 74-79.
https://doi.org/10.1016/j.ijbiomac.2019.01.124
Gligorijević N, Minić SL, Robajac DB, Nikolić M, Ćirković-Veličković T, Nedić O. Characterisation and the effects of bilirubin binding to human fibrinogen. in International Journal of Biological Macromolecules. 2019;128:74-79.
doi:10.1016/j.ijbiomac.2019.01.124 .
Gligorijević, Nikola, Minić, Simeon L., Robajac, Dragana B., Nikolić, Milan, Ćirković-Veličković, Tanja, Nedić, Olgica, "Characterisation and the effects of bilirubin binding to human fibrinogen" in International Journal of Biological Macromolecules, 128 (2019):74-79,
https://doi.org/10.1016/j.ijbiomac.2019.01.124 . .
6
6
6

Characterisation and the effects of bilirubin binding to human fibrinogen

Gligorijević, Nikola; Minić, Simeon L.; Robajac, Dragana B.; Nikolić, Milan; Ćirković-Veličković, Tanja; Nedić, Olgica

(2019)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Robajac, Dragana B.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
AU  - Nedić, Olgica
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2825
AB  - Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventing its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction.
T2  - International Journal of Biological Macromolecules
T1  - Characterisation and the effects of bilirubin binding to human fibrinogen
VL  - 128
SP  - 74
EP  - 79
DO  - 10.1016/j.ijbiomac.2019.01.124
ER  - 
@article{
author = "Gligorijević, Nikola and Minić, Simeon L. and Robajac, Dragana B. and Nikolić, Milan and Ćirković-Veličković, Tanja and Nedić, Olgica",
year = "2019",
abstract = "Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventing its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction.",
journal = "International Journal of Biological Macromolecules",
title = "Characterisation and the effects of bilirubin binding to human fibrinogen",
volume = "128",
pages = "74-79",
doi = "10.1016/j.ijbiomac.2019.01.124"
}
Gligorijević, N., Minić, S. L., Robajac, D. B., Nikolić, M., Ćirković-Veličković, T.,& Nedić, O.. (2019). Characterisation and the effects of bilirubin binding to human fibrinogen. in International Journal of Biological Macromolecules, 128, 74-79.
https://doi.org/10.1016/j.ijbiomac.2019.01.124
Gligorijević N, Minić SL, Robajac DB, Nikolić M, Ćirković-Veličković T, Nedić O. Characterisation and the effects of bilirubin binding to human fibrinogen. in International Journal of Biological Macromolecules. 2019;128:74-79.
doi:10.1016/j.ijbiomac.2019.01.124 .
Gligorijević, Nikola, Minić, Simeon L., Robajac, Dragana B., Nikolić, Milan, Ćirković-Veličković, Tanja, Nedić, Olgica, "Characterisation and the effects of bilirubin binding to human fibrinogen" in International Journal of Biological Macromolecules, 128 (2019):74-79,
https://doi.org/10.1016/j.ijbiomac.2019.01.124 . .
6
6
6

Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124

Gligorijević, Nikola; Minić, Simeon L.; Robajac, Dragana B.; Nikolić, Milan; Ćirković-Veličković, Tanja; Nedić, Olgica

(2019)

TY  - DATA
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Robajac, Dragana B.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
AU  - Nedić, Olgica
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2937
T2  - International Journal of Biological Macromolecules
T1  - Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124
ER  - 
@misc{
author = "Gligorijević, Nikola and Minić, Simeon L. and Robajac, Dragana B. and Nikolić, Milan and Ćirković-Veličković, Tanja and Nedić, Olgica",
year = "2019",
journal = "International Journal of Biological Macromolecules",
title = "Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124"
}
Gligorijević, N., Minić, S. L., Robajac, D. B., Nikolić, M., Ćirković-Veličković, T.,& Nedić, O.. (2019). Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124. in International Journal of Biological Macromolecules.
Gligorijević N, Minić SL, Robajac DB, Nikolić M, Ćirković-Veličković T, Nedić O. Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124. in International Journal of Biological Macromolecules. 2019;..
Gligorijević, Nikola, Minić, Simeon L., Robajac, Dragana B., Nikolić, Milan, Ćirković-Veličković, Tanja, Nedić, Olgica, "Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124" in International Journal of Biological Macromolecules (2019).

Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study

Radibratović, Milica; Al-Hanish, Ayah; Minić, Simeon L.; Radomirović, Mirjana Ž.; Milčić, Miloš K.; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier, 2019)

TY  - JOUR
AU  - Radibratović, Milica
AU  - Al-Hanish, Ayah
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3733
AB  - α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. 

EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.
PB  - Elsevier
T2  - Food Chemistry
T1  - Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study
VL  - 278
SP  - 388
EP  - 395
DO  - 10.1016/j.foodchem.2018.11.038
ER  - 
@article{
author = "Radibratović, Milica and Al-Hanish, Ayah and Minić, Simeon L. and Radomirović, Mirjana Ž. and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. 

EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study",
volume = "278",
pages = "388-395",
doi = "10.1016/j.foodchem.2018.11.038"
}
Radibratović, M., Al-Hanish, A., Minić, S. L., Radomirović, M. Ž., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2019). Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. in Food Chemistry
Elsevier., 278, 388-395.
https://doi.org/10.1016/j.foodchem.2018.11.038
Radibratović M, Al-Hanish A, Minić SL, Radomirović MŽ, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. in Food Chemistry. 2019;278:388-395.
doi:10.1016/j.foodchem.2018.11.038 .
Radibratović, Milica, Al-Hanish, Ayah, Minić, Simeon L., Radomirović, Mirjana Ž., Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study" in Food Chemistry, 278 (2019):388-395,
https://doi.org/10.1016/j.foodchem.2018.11.038 . .
5
3
5

Fatty acids composition of the most common bivalves in Korean diet

Krstić-Ristivojević, Maja; Jovanović, Vesna B.; Ristivojević, Petar; Ćirković-Veličković, Tanja

(Portugal : Sociedade Portuguesa de Química, 2019)

TY  - CONF
AU  - Krstić-Ristivojević, Maja
AU  - Jovanović, Vesna B.
AU  - Ristivojević, Petar
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3777
AB  - Consumption of bivalve molluscs, such as oysters, mussels, clams and scallops, makes a significant part of the daily Korean diet. Bivalves provide high quality proteins with all the dietary-essential amino acids, lipids, vitamins, minerals and other bioactive nutrients, which offer a variety of health benefits to the consumer [1]. This food contains less than 5 percent of total fat, so it is considered a low-fat food. Beside the amount of total fat, the proportions of saturated, monounsaturated and polyunsaturated fatty acids (FA) (S, M and P, respectively), as well as ratio of n-3 (ω-3) and n-6 (ω-6) P in food are very important for the health diet [2].
Fourteen species of bivalves Anadara broughtonii (AB), Ruditapes philippinarum (Manila clam (RP)), Tegillarca granosa (TG), Pecten yessoensis (Yesso scallop (YS), Argopecten spp. (small scallop (SS), Chlamys farreri farreri (CF), Cyclina sinensis (CS), Leukoma jedoensis (LJ), Mytilus califorianus (MCa) Mytilus galloprovancialis (MG), Maretrix lusoria (ML), Mactra quadrangularis (MQ), Sinovacula constricta (SC) and Crassostrea gigas (Pacific oyster (PC)) were bought in two fish markets in Incheon, Korea, in order to determine FA composition using GC/EI-MS of fatty acid methyl esters (FAME). The FAME were identified by comparing their retention times with those of the FAME standards or by comparing their mass spectra with those stored in the NIST Mass Spectral Library.
In the bivalve samples, 43 different FA were identified, of which 10 were S, 12 M and 13 P, other FA were 7 methyl-FA and 1 hydroxyl-FA. The P/S ratio and ω-6/ω-3 P ratio are the most significant markers of lipid composition in a healthy diet and both should be close to 1 [3]. Among analysed species, only YS and SS have P/S ratio close to 1 (1,20 and 1.16, respectively), while other species have value between 0.07 and 0.73. The obtained values for ω-6/ω-3 P ratio were from 0.008 to 0.55, which indicates that bivalve molluscs are the valuable source of ω-3 P (EPA and DHA). These ω-3 P play important roles in growth, development, and maintenance of health.
PB  - Portugal : Sociedade Portuguesa de Química
C3  - Book of Abstracts of the XX EuroFoodChem Congress
T1  - Fatty acids composition of the most common bivalves in Korean diet
ER  - 
@conference{
author = "Krstić-Ristivojević, Maja and Jovanović, Vesna B. and Ristivojević, Petar and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Consumption of bivalve molluscs, such as oysters, mussels, clams and scallops, makes a significant part of the daily Korean diet. Bivalves provide high quality proteins with all the dietary-essential amino acids, lipids, vitamins, minerals and other bioactive nutrients, which offer a variety of health benefits to the consumer [1]. This food contains less than 5 percent of total fat, so it is considered a low-fat food. Beside the amount of total fat, the proportions of saturated, monounsaturated and polyunsaturated fatty acids (FA) (S, M and P, respectively), as well as ratio of n-3 (ω-3) and n-6 (ω-6) P in food are very important for the health diet [2].
Fourteen species of bivalves Anadara broughtonii (AB), Ruditapes philippinarum (Manila clam (RP)), Tegillarca granosa (TG), Pecten yessoensis (Yesso scallop (YS), Argopecten spp. (small scallop (SS), Chlamys farreri farreri (CF), Cyclina sinensis (CS), Leukoma jedoensis (LJ), Mytilus califorianus (MCa) Mytilus galloprovancialis (MG), Maretrix lusoria (ML), Mactra quadrangularis (MQ), Sinovacula constricta (SC) and Crassostrea gigas (Pacific oyster (PC)) were bought in two fish markets in Incheon, Korea, in order to determine FA composition using GC/EI-MS of fatty acid methyl esters (FAME). The FAME were identified by comparing their retention times with those of the FAME standards or by comparing their mass spectra with those stored in the NIST Mass Spectral Library.
In the bivalve samples, 43 different FA were identified, of which 10 were S, 12 M and 13 P, other FA were 7 methyl-FA and 1 hydroxyl-FA. The P/S ratio and ω-6/ω-3 P ratio are the most significant markers of lipid composition in a healthy diet and both should be close to 1 [3]. Among analysed species, only YS and SS have P/S ratio close to 1 (1,20 and 1.16, respectively), while other species have value between 0.07 and 0.73. The obtained values for ω-6/ω-3 P ratio were from 0.008 to 0.55, which indicates that bivalve molluscs are the valuable source of ω-3 P (EPA and DHA). These ω-3 P play important roles in growth, development, and maintenance of health.",
publisher = "Portugal : Sociedade Portuguesa de Química",
journal = "Book of Abstracts of the XX EuroFoodChem Congress",
title = "Fatty acids composition of the most common bivalves in Korean diet"
}
Krstić-Ristivojević, M., Jovanović, V. B., Ristivojević, P.,& Ćirković-Veličković, T.. (2019). Fatty acids composition of the most common bivalves in Korean diet. in Book of Abstracts of the XX EuroFoodChem Congress
Portugal : Sociedade Portuguesa de Química..
Krstić-Ristivojević M, Jovanović VB, Ristivojević P, Ćirković-Veličković T. Fatty acids composition of the most common bivalves in Korean diet. in Book of Abstracts of the XX EuroFoodChem Congress. 2019;..
Krstić-Ristivojević, Maja, Jovanović, Vesna B., Ristivojević, Petar, Ćirković-Veličković, Tanja, "Fatty acids composition of the most common bivalves in Korean diet" in Book of Abstracts of the XX EuroFoodChem Congress (2019).

In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Cvetković, Anka; Veljović, Đorđe; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija M.; Ćirković-Veličković, Tanja

(Elsevier, 2019)

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Cvetković, Anka
AU  - Veljović, Đorđe
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2857
AB  - An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.
PB  - Elsevier
T2  - Environment International
T1  - In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress
VL  - 126
SP  - 644
EP  - 658
DO  - 10.1016/j.envint.2019.03.001
ER  - 
@article{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Cvetković, Anka and Veljović, Đorđe and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.",
publisher = "Elsevier",
journal = "Environment International",
title = "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress",
volume = "126",
pages = "644-658",
doi = "10.1016/j.envint.2019.03.001"
}
Smiljanić, K., Prodić, I., Apostolović, D., Cvetković, A., Veljović, Đ., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2019). In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress. in Environment International
Elsevier., 126, 644-658.
https://doi.org/10.1016/j.envint.2019.03.001
Smiljanić K, Prodić I, Apostolović D, Cvetković A, Veljović Đ, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress. in Environment International. 2019;126:644-658.
doi:10.1016/j.envint.2019.03.001 .
Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Cvetković, Anka, Veljović, Đorđe, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija M., Ćirković-Veličković, Tanja, "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress" in Environment International, 126 (2019):644-658,
https://doi.org/10.1016/j.envint.2019.03.001 . .
2
5
4
5

Novel insights into the allergenic relationship between red meat and bovine milk

Peruško, Marija; Apostolović, Danijela; Starkhammar, Maria; Ćirković-Veličković, Tanja; van Hage, Marianne

(Wiley, 2019)

TY  - CONF
AU  - Peruško, Marija
AU  - Apostolović, Danijela
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - van Hage, Marianne
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3735
AB  - Novel insights into the allergenic relationship between red meat and bovine milk
Marija Perusko1, Danijela Apostolovic2, Maria Starkhammar3, Tanja Cirkovic Velickovic4,5,6,7, Marianne van Hage2
1Innovation Center of the Faculty of Chemistry, Belgrade, Serbia
2Department of Medicine, Solna, Immunology and Allergy Unit, Karolinska Institutet and University Hospital, Stockholm, Sweden
3Department of Internal Medicine, Sodersjukhuset, Stockholm, Sweden
4Serbian Academy of Sciences and Arts, Belgrade, Serbia
5Center of Excellence for Molecular Food Sciences & Department of Biochemistry, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia
6Ghent University Global Campus, Yeonsu-gu, Incheon, South Korea
7Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium
 
Background
Red meat allergy is a severe form of food allergy with delayed symptoms including anaphylaxis where the IgE antibodies are directed against a carbohydrate epitope, galactose-α-1,3-galactose (α-Gal). Many red meat allergic patients report allergic symptoms upon consumption of milk or dairy products. The aim of the project was to investigate the allergenic relationship between bovine milk and red meat at a molecular level.
Methods
Adults with diagnosed red meat allergy (n = 27) were recruited and their specific IgE levels to α-Gal, beef and milk were analyzed by ImmunoCAP. Milk proteins were assayed by immunoblot and inhibition ELISA for the presence of the α-Gal epitope and for the binding to red meat allergic patients’ IgE. The involvement of the carbohydrate epitope in the IgE binding to milk proteins was assessed by an inhibition assay with thyroglobulin. Basophil activation test was performed with milk and milk proteins in samples from 11 red meat allergic patients and 2 controls.
Results
All patients were IgE positive to milk, but the IgE levels to milk were lower than those to α-Gal or beef. Significant correlations between IgE levels to milk and α-Gal (rs=0.64, P < 0.01), as well as between milk and beef (rs=0.90, P < 0.01) were observed. Immunoblot analysis of milk proteins revealed bovine γ-globulin (BGG) as α-Gal carrier. Other milk proteins, α-lactalbumin, β-lactoglobulin, α-casein, β-casein and κ-casein were negative for the presence of α-Gal epitope. BGG was also shown to bind IgE antibodies of red meat allergic patients. Inhibition immunoblot with thyroglobulin resulted in the loss of IgE binding to BGG. Additionally, ELISA experiments showed that BGG, as well as whey proteins exert a dose-dependent inhibition of red meat allergic patients’ IgE binding to -Gal. Inhibition with raw milk and commercially available milk preparations showed that raw milk exerted a slightly higher inhibition of the IgE binding to the α-Gal epitope than the commercially available milks. Importantly, activation of red meat allergic patient’s basophils by BGG and milk was demonstrated.
Conclusion
BGG was identified as a major milk carrier of the -Gal epitope that bound IgE antibodies and furthermore activated basophils of red meat allergic patients. This study highlights the importance of milk as allergenic food source among the meat allergic population.
PB  - Wiley
C3  - Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)
T1  - Novel insights into the allergenic relationship between red meat and bovine milk
VL  - 74
VL  - supp. 106
SP  - 596
EP  - 596
ER  - 
@conference{
author = "Peruško, Marija and Apostolović, Danijela and Starkhammar, Maria and Ćirković-Veličković, Tanja and van Hage, Marianne",
year = "2019",
abstract = "Novel insights into the allergenic relationship between red meat and bovine milk
Marija Perusko1, Danijela Apostolovic2, Maria Starkhammar3, Tanja Cirkovic Velickovic4,5,6,7, Marianne van Hage2
1Innovation Center of the Faculty of Chemistry, Belgrade, Serbia
2Department of Medicine, Solna, Immunology and Allergy Unit, Karolinska Institutet and University Hospital, Stockholm, Sweden
3Department of Internal Medicine, Sodersjukhuset, Stockholm, Sweden
4Serbian Academy of Sciences and Arts, Belgrade, Serbia
5Center of Excellence for Molecular Food Sciences & Department of Biochemistry, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia
6Ghent University Global Campus, Yeonsu-gu, Incheon, South Korea
7Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium
 
Background
Red meat allergy is a severe form of food allergy with delayed symptoms including anaphylaxis where the IgE antibodies are directed against a carbohydrate epitope, galactose-α-1,3-galactose (α-Gal). Many red meat allergic patients report allergic symptoms upon consumption of milk or dairy products. The aim of the project was to investigate the allergenic relationship between bovine milk and red meat at a molecular level.
Methods
Adults with diagnosed red meat allergy (n = 27) were recruited and their specific IgE levels to α-Gal, beef and milk were analyzed by ImmunoCAP. Milk proteins were assayed by immunoblot and inhibition ELISA for the presence of the α-Gal epitope and for the binding to red meat allergic patients’ IgE. The involvement of the carbohydrate epitope in the IgE binding to milk proteins was assessed by an inhibition assay with thyroglobulin. Basophil activation test was performed with milk and milk proteins in samples from 11 red meat allergic patients and 2 controls.
Results
All patients were IgE positive to milk, but the IgE levels to milk were lower than those to α-Gal or beef. Significant correlations between IgE levels to milk and α-Gal (rs=0.64, P < 0.01), as well as between milk and beef (rs=0.90, P < 0.01) were observed. Immunoblot analysis of milk proteins revealed bovine γ-globulin (BGG) as α-Gal carrier. Other milk proteins, α-lactalbumin, β-lactoglobulin, α-casein, β-casein and κ-casein were negative for the presence of α-Gal epitope. BGG was also shown to bind IgE antibodies of red meat allergic patients. Inhibition immunoblot with thyroglobulin resulted in the loss of IgE binding to BGG. Additionally, ELISA experiments showed that BGG, as well as whey proteins exert a dose-dependent inhibition of red meat allergic patients’ IgE binding to -Gal. Inhibition with raw milk and commercially available milk preparations showed that raw milk exerted a slightly higher inhibition of the IgE binding to the α-Gal epitope than the commercially available milks. Importantly, activation of red meat allergic patient’s basophils by BGG and milk was demonstrated.
Conclusion
BGG was identified as a major milk carrier of the -Gal epitope that bound IgE antibodies and furthermore activated basophils of red meat allergic patients. This study highlights the importance of milk as allergenic food source among the meat allergic population.",
publisher = "Wiley",
journal = "Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)",
title = "Novel insights into the allergenic relationship between red meat and bovine milk",
volume = "74, supp. 106",
pages = "596-596"
}
Peruško, M., Apostolović, D., Starkhammar, M., Ćirković-Veličković, T.,& van Hage, M.. (2019). Novel insights into the allergenic relationship between red meat and bovine milk. in Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)
Wiley., 74, 596-596.
Peruško M, Apostolović D, Starkhammar M, Ćirković-Veličković T, van Hage M. Novel insights into the allergenic relationship between red meat and bovine milk. in Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI). 2019;74:596-596..
Peruško, Marija, Apostolović, Danijela, Starkhammar, Maria, Ćirković-Veličković, Tanja, van Hage, Marianne, "Novel insights into the allergenic relationship between red meat and bovine milk" in Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI), 74 (2019):596-596.

Spray drying of camel milk induces protein aggregates and Maillard reaction products formation

(Beograd : Srpsko hemijsko društvo, 2019)

TY  - CONF
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3761
AB  - Camel milk (CM) powders are nutritious food with many health benefits. We investigated physicochemical properties of CM proteins upon spray drying at six inlet temperatures (190°C - 250°C). Electrophoretic and spectrophotometric analysis revealed occurrence of Maillard reaction upon spray drying. Size exclusion chromatography showed increase in protein Mw and aggregates formation. Spray drying inlet temperatures exerted significant effects on the properties of CM powder proteins. Project was supported by the GA No.172024 of Ministry of Education, Science and Technological Development.
AB  - Kamilje mleko (KM) u prahu je visoko nutritivno sa brojnim zdravstvenim učincima. U ovoj studiji smo ispitivali fizičko-hemijske osobine proteina KM nakon sušenja raspršivanjem na šest ulaznih temperatura (190°C - 250°C). Elektroforetske i spektrofotometrijske analize su pokazale odigravanje Majarove reakcije tokom sušenja raspršivanjem. Ekskluziona hromatografija je pokazala povećanje Mw proteina i formiranje proteinskih agregata. Ulazna temperatura kod sušenja raspršivanjem ima značajne efekte na fizičko-hemijske osobine proteina KM u prahu.
PB  - Beograd : Srpsko hemijsko društvo
C3  - Kratki izvodi radova / 56. savetovanje Srpskog hemijskog društva , Niš 7. i 8. juni 2019.
T1  - Spray drying of camel milk induces protein aggregates and Maillard reaction products formation
T1  - Sušenje kamiljeg mleka raspršivanjem indukuje formiranje proteinskih agregata i Majarovih proizvoda
ER  - 
@conference{
year = "2019",
abstract = "Camel milk (CM) powders are nutritious food with many health benefits. We investigated physicochemical properties of CM proteins upon spray drying at six inlet temperatures (190°C - 250°C). Electrophoretic and spectrophotometric analysis revealed occurrence of Maillard reaction upon spray drying. Size exclusion chromatography showed increase in protein Mw and aggregates formation. Spray drying inlet temperatures exerted significant effects on the properties of CM powder proteins. Project was supported by the GA No.172024 of Ministry of Education, Science and Technological Development., Kamilje mleko (KM) u prahu je visoko nutritivno sa brojnim zdravstvenim učincima. U ovoj studiji smo ispitivali fizičko-hemijske osobine proteina KM nakon sušenja raspršivanjem na šest ulaznih temperatura (190°C - 250°C). Elektroforetske i spektrofotometrijske analize su pokazale odigravanje Majarove reakcije tokom sušenja raspršivanjem. Ekskluziona hromatografija je pokazala povećanje Mw proteina i formiranje proteinskih agregata. Ulazna temperatura kod sušenja raspršivanjem ima značajne efekte na fizičko-hemijske osobine proteina KM u prahu.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "Kratki izvodi radova / 56. savetovanje Srpskog hemijskog društva , Niš 7. i 8. juni 2019.",
title = "Spray drying of camel milk induces protein aggregates and Maillard reaction products formation, Sušenje kamiljeg mleka raspršivanjem indukuje formiranje proteinskih agregata i Majarovih proizvoda"
}
(2019). Spray drying of camel milk induces protein aggregates and Maillard reaction products formation. in Kratki izvodi radova / 56. savetovanje Srpskog hemijskog društva , Niš 7. i 8. juni 2019.
Beograd : Srpsko hemijsko društvo..
Spray drying of camel milk induces protein aggregates and Maillard reaction products formation. in Kratki izvodi radova / 56. savetovanje Srpskog hemijskog društva , Niš 7. i 8. juni 2019.. 2019;..
"Spray drying of camel milk induces protein aggregates and Maillard reaction products formation" in Kratki izvodi radova / 56. savetovanje Srpskog hemijskog društva , Niš 7. i 8. juni 2019. (2019).

Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović-Vesić, Jelena; Radibratović, Milica; Radosavljević, Jelena; Burazer, Lidija M.; Milčić, Miloš K.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2155
AB  - BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
VL  - 48
IS  - 6
SP  - 731
EP  - 740
DO  - 10.1111/cea.13113
UR  - Kon_3486
ER  - 
@article{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
volume = "48",
number = "6",
pages = "731-740",
doi = "10.1111/cea.13113",
url = "Kon_3486"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T.. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy
Wiley, Hoboken., 48(6), 731-740.
https://doi.org/10.1111/cea.13113
Kon_3486
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, Ćirković-Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy. 2018;48(6):731-740.
doi:10.1111/cea.13113
Kon_3486 .
Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Mihailović-Vesić, Jelena, Radibratović, Milica, Radosavljević, Jelena, Burazer, Lidija M., Milčić, Miloš K., Smiljanić, Katarina, van Hage, Marianne, Ćirković-Veličković, Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" in Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 .,
Kon_3486 .
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Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović-Vesić, Jelena; Radibratović, Milica; Radosavljević, Jelena; Burazer, Lidija M.; Milčić, Miloš K.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3224
AB  - BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
VL  - 48
IS  - 6
SP  - 731
EP  - 740
DO  - 10.1111/cea.13113
UR  - Kon_3486
ER  - 
@article{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
volume = "48",
number = "6",
pages = "731-740",
doi = "10.1111/cea.13113",
url = "Kon_3486"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T.. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy
Wiley, Hoboken., 48(6), 731-740.
https://doi.org/10.1111/cea.13113
Kon_3486
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, Ćirković-Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy. 2018;48(6):731-740.
doi:10.1111/cea.13113
Kon_3486 .
Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Mihailović-Vesić, Jelena, Radibratović, Milica, Radosavljević, Jelena, Burazer, Lidija M., Milčić, Miloš K., Smiljanić, Katarina, van Hage, Marianne, Ćirković-Veličković, Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" in Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 .,
Kon_3486 .
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