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

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

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

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

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

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

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

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

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

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

TY  - CHAP
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Jovanović, Vesna B.
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5728
AB  - Post-translational modifications (PTMs) occur in many forms and shapes, widely influencing protein behavior. High-resolution tandem mass spectrometry (HRMS/MS), coupled with dedicated engines for the identification of unspecified PTMs, is a powerful method for their mapping. 
A majority of proteomic experiments utilize trypsin for digestion, which cleaves the C-terminal peptide bonds of arginine (Arg) and lysine (Lys) amino acids with high catalytic efficiency and selectivity, unless they are followed with proline. At the same time, Arg and Lys residues are frequently modified during food processing by heat and non-thermal treatments, causing oxidation, carbamylation, and various forms of side chain carbonylation, including the other common PTMs (methylation, acetylation, etc.). Consequently, we explored the possibility to re-assess already generated proteomic data (food protein/allergen tryptic peptides) with respect to the possible modulation of the tryptic intestinal digestion pattern caused by PTMs incorporated at Arg and Lys residues. However, most of the proteomic bottom-up experiments are run with porcine trypsin that has been reductively methylated to increase its stability and minimize autoproteolytic effects. Therefore, in this chapter, the utility of the aforementioned idea was explored, by reviewing the differences in structure, affinity, specificity, and catalytic efficiency of trypsin, primarily from porcine, bovine and human species. Porcine trypsin either from pancreas or in recombinant form showed superior performance compared to human and bovine tryptic counterparts. In addition, set of software tools for identification and analyses of PTMs was reviewed with the aim to isolate those capable of in-depth PTMs profiling and their simultaneous relative quantification, such as PEAKS PTM (PEAKS Studio, Bioinformatics Solution Inc., Ontario Canada). Based on our preliminary experimental results, conclusion is that the proposed idea is plausible, because if potential hindrance effects caused by PTMs are observed with porcine trypsin, then they can be just augmented within human intestinal digestion, with respect to inferior performance of human trypsin.
PB  - New York : Nova Science Publisher
T2  - A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era
T1  - Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications
VL  - 4
SP  - 158
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5728
ER  - 

@inbook{
author = "Smiljanić, Katarina and Mihailović, Jelena and Prodić, Ivana and Đukić, Teodora and Vasović, Tamara and Jovanović, Vesna B. and Ćirković-Veličković, Tanja",
year = "2020",
abstract = "Post-translational modifications (PTMs) occur in many forms and shapes, widely influencing protein behavior. High-resolution tandem mass spectrometry (HRMS/MS), coupled with dedicated engines for the identification of unspecified PTMs, is a powerful method for their mapping. 
A majority of proteomic experiments utilize trypsin for digestion, which cleaves the C-terminal peptide bonds of arginine (Arg) and lysine (Lys) amino acids with high catalytic efficiency and selectivity, unless they are followed with proline. At the same time, Arg and Lys residues are frequently modified during food processing by heat and non-thermal treatments, causing oxidation, carbamylation, and various forms of side chain carbonylation, including the other common PTMs (methylation, acetylation, etc.). Consequently, we explored the possibility to re-assess already generated proteomic data (food protein/allergen tryptic peptides) with respect to the possible modulation of the tryptic intestinal digestion pattern caused by PTMs incorporated at Arg and Lys residues. However, most of the proteomic bottom-up experiments are run with porcine trypsin that has been reductively methylated to increase its stability and minimize autoproteolytic effects. Therefore, in this chapter, the utility of the aforementioned idea was explored, by reviewing the differences in structure, affinity, specificity, and catalytic efficiency of trypsin, primarily from porcine, bovine and human species. Porcine trypsin either from pancreas or in recombinant form showed superior performance compared to human and bovine tryptic counterparts. In addition, set of software tools for identification and analyses of PTMs was reviewed with the aim to isolate those capable of in-depth PTMs profiling and their simultaneous relative quantification, such as PEAKS PTM (PEAKS Studio, Bioinformatics Solution Inc., Ontario Canada). Based on our preliminary experimental results, conclusion is that the proposed idea is plausible, because if potential hindrance effects caused by PTMs are observed with porcine trypsin, then they can be just augmented within human intestinal digestion, with respect to inferior performance of human trypsin.",
publisher = "New York : Nova Science Publisher",
journal = "A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era",
booktitle = "Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications",
volume = "4",
pages = "158",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5728"
}

Smiljanić, K., Mihailović, J., Prodić, I., Đukić, T., Vasović, T., Jovanović, V. B.,& Ćirković-Veličković, T.. (2020). Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications. in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era
New York : Nova Science Publisher., 4, 158.
https://hdl.handle.net/21.15107/rcub_cherry_5728

Smiljanić K, Mihailović J, Prodić I, Đukić T, Vasović T, Jovanović VB, Ćirković-Veličković T. Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications. in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era. 2020;4:158.
https://hdl.handle.net/21.15107/rcub_cherry_5728 .

Smiljanić, Katarina, Mihailović, Jelena, Prodić, Ivana, Đukić, Teodora, Vasović, Tamara, Jovanović, Vesna B., Ćirković-Veličković, Tanja, "Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications" in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era, 4 (2020):158,
https://hdl.handle.net/21.15107/rcub_cherry_5728 .

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  - https://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 . .

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  - https://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 . .

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  - https://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
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3863
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",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3863"
}

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..
https://hdl.handle.net/21.15107/rcub_cherry_3863

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;.
https://hdl.handle.net/21.15107/rcub_cherry_3863 .

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),
https://hdl.handle.net/21.15107/rcub_cherry_3863 .

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  - https://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
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3864
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",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3864"
}

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..
https://hdl.handle.net/21.15107/rcub_cherry_3864

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;.
https://hdl.handle.net/21.15107/rcub_cherry_3864 .

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),
https://hdl.handle.net/21.15107/rcub_cherry_3864 .

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  - https://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 . .

TY  - CONF
AU  - Mihailović, Jelena
AU  - Apostolović, Danijela
AU  - Smiljanić, Katarina
AU  - Đukić, Teodora
AU  - Prodić, Ivana
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5727
PB  - Medical University of Vienna - MUW
C3  - Abstract Book of the 2nd FoodEnTwin Workshop “Experimental Animal models for food and environment”, Vienna, February 6-7, 2020
T1  - Immunoproteomics study of raw and roasted major peanut allergen post translational modifications (PTMs)
SP  - 1
EP  - 7
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5727
ER  - 

@conference{
author = "Mihailović, Jelena and Apostolović, Danijela and Smiljanić, Katarina and Đukić, Teodora and Prodić, Ivana and Ćirković-Veličković, Tanja",
year = "2020",
publisher = "Medical University of Vienna - MUW",
journal = "Abstract Book of the 2nd FoodEnTwin Workshop “Experimental Animal models for food and environment”, Vienna, February 6-7, 2020",
title = "Immunoproteomics study of raw and roasted major peanut allergen post translational modifications (PTMs)",
pages = "1-7",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5727"
}

Mihailović, J., Apostolović, D., Smiljanić, K., Đukić, T., Prodić, I.,& Ćirković-Veličković, T.. (2020). Immunoproteomics study of raw and roasted major peanut allergen post translational modifications (PTMs). in Abstract Book of the 2nd FoodEnTwin Workshop “Experimental Animal models for food and environment”, Vienna, February 6-7, 2020
Medical University of Vienna - MUW., 1-7.
https://hdl.handle.net/21.15107/rcub_cherry_5727

Mihailović J, Apostolović D, Smiljanić K, Đukić T, Prodić I, Ćirković-Veličković T. Immunoproteomics study of raw and roasted major peanut allergen post translational modifications (PTMs). in Abstract Book of the 2nd FoodEnTwin Workshop “Experimental Animal models for food and environment”, Vienna, February 6-7, 2020. 2020;:1-7.
https://hdl.handle.net/21.15107/rcub_cherry_5727 .

Mihailović, Jelena, Apostolović, Danijela, Smiljanić, Katarina, Đukić, Teodora, Prodić, Ivana, Ćirković-Veličković, Tanja, "Immunoproteomics study of raw and roasted major peanut allergen post translational modifications (PTMs)" in Abstract Book of the 2nd FoodEnTwin Workshop “Experimental Animal models for food and environment”, Vienna, February 6-7, 2020 (2020):1-7,
https://hdl.handle.net/21.15107/rcub_cherry_5727 .

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  - https://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 . .

TY  - DATA
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/123456789/4851
PB  - Wiley
T2  - Angewandte Chemie (International Edition)
T1  - Supplementary data for the article: 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. Angewandte Chemie (International Edition) 2020, 59 (17), 1–9. https://doi.org/10.1002/anie.202001036.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4851
ER  - 

@misc{
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",
publisher = "Wiley",
journal = "Angewandte Chemie (International Edition)",
title = "Supplementary data for the article: 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. Angewandte Chemie (International Edition) 2020, 59 (17), 1–9. https://doi.org/10.1002/anie.202001036.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4851"
}

Moons, J., de Azambuja, F., Mihailović, J., Kozma, K., Smiljanić, K., Amiri, M., Ćirković-Veličković, T., Nyman, M.,& Parac-Vogt, T.. (2020). Supplementary data for the article: 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. Angewandte Chemie (International Edition) 2020, 59 (17), 1–9. https://doi.org/10.1002/anie.202001036.. in Angewandte Chemie (International Edition)
Wiley..
https://hdl.handle.net/21.15107/rcub_cherry_4851

Moons J, de Azambuja F, Mihailović J, Kozma K, Smiljanić K, Amiri M, Ćirković-Veličković T, Nyman M, Parac-Vogt T. Supplementary data for the article: 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. Angewandte Chemie (International Edition) 2020, 59 (17), 1–9. https://doi.org/10.1002/anie.202001036.. in Angewandte Chemie (International Edition). 2020;.
https://hdl.handle.net/21.15107/rcub_cherry_4851 .

Moons, Jens, de Azambuja, Francisco, Mihailović, Jelena, Kozma, Karoly, Smiljanić, Katarina, Amiri, Mehran, Ćirković-Veličković, Tanja, Nyman, May, Parac-Vogt, Tatjana, "Supplementary data for the article: 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. Angewandte Chemie (International Edition) 2020, 59 (17), 1–9. https://doi.org/10.1002/anie.202001036." in Angewandte Chemie (International Edition) (2020),
https://hdl.handle.net/21.15107/rcub_cherry_4851 .

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/123456789/4850
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 . .

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  - https://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 . .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić Šipka, Sanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6037
AB  - The ruthenium-based antitumour compounds act more via protein targets involved in carcinogenesis, in contrast to platinum-based compounds. Also, after intravenous administration of antitumour complexes proteins are the first binding targets in circulation. Therefore, interactions of anticancer compounds with proteins are important for elucidation of their pharmacokinetic pathways. Four half-sandwich ruthenium(II)-cymene complexes (C1, C2, C3 and C4), developed earlier and with promising cytotoxic activity, are investigated for their interactions with cytochrome c (Cyt). Complexes  were incubated with Cyt for 48 h at 37 °C and high-resolution LTQ-Orbitrap ESI MS was used to monitor the formed adducts. The changes in heme state and tertiary structure around the heme were monitored by CD and UV-VIS spectra in the presence of oxygen. The complexes containing two chloride ligands (C2 and C3) were more reactive toward Cyt than those with only one (C1 and C4). The complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). All complexes reduced heme iron of Cyt, but the extent of reduction was inverse to the order of their reactivity to Cyt (C1>C4>>C2>C3). CD spectra in Soret region indicated that Cyt reduction was accompanied with slight tertiary structure change, the rupture of ferro-Met-80 and occupation of this heme coordination site by His-33/His-26. Extent of  heme reduction by complexes inverse with respect to their reactivity implies that initially noncovalent binding of complexes occures, causing heme reduction, followed by comlex coordination to protein. In the presence of less reactive complexes more intensive reduction of heme leaves less available histidine residues (main targets for Ru coordination), leading to less efficient formation of adducts.
C3  - 1st FoodEnTwin Workshop “Food and Environmental –Omics”, Belgrade, Serbia, 20th-21st June, 2019. In: Book of Abstracts
T1  - Interactions of ruthenium(II)-cymene complexes with cytochrome c
SP  - 24
EP  - 24
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6037
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Stanić-Vučinić, Dragana and Nikolić, Stefan and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić Šipka, Sanja",
year = "2019",
abstract = "The ruthenium-based antitumour compounds act more via protein targets involved in carcinogenesis, in contrast to platinum-based compounds. Also, after intravenous administration of antitumour complexes proteins are the first binding targets in circulation. Therefore, interactions of anticancer compounds with proteins are important for elucidation of their pharmacokinetic pathways. Four half-sandwich ruthenium(II)-cymene complexes (C1, C2, C3 and C4), developed earlier and with promising cytotoxic activity, are investigated for their interactions with cytochrome c (Cyt). Complexes  were incubated with Cyt for 48 h at 37 °C and high-resolution LTQ-Orbitrap ESI MS was used to monitor the formed adducts. The changes in heme state and tertiary structure around the heme were monitored by CD and UV-VIS spectra in the presence of oxygen. The complexes containing two chloride ligands (C2 and C3) were more reactive toward Cyt than those with only one (C1 and C4). The complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). All complexes reduced heme iron of Cyt, but the extent of reduction was inverse to the order of their reactivity to Cyt (C1>C4>>C2>C3). CD spectra in Soret region indicated that Cyt reduction was accompanied with slight tertiary structure change, the rupture of ferro-Met-80 and occupation of this heme coordination site by His-33/His-26. Extent of  heme reduction by complexes inverse with respect to their reactivity implies that initially noncovalent binding of complexes occures, causing heme reduction, followed by comlex coordination to protein. In the presence of less reactive complexes more intensive reduction of heme leaves less available histidine residues (main targets for Ru coordination), leading to less efficient formation of adducts.",
journal = "1st FoodEnTwin Workshop “Food and Environmental –Omics”, Belgrade, Serbia, 20th-21st June, 2019. In: Book of Abstracts",
title = "Interactions of ruthenium(II)-cymene complexes with cytochrome c",
pages = "24-24",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6037"
}

Radomirović, M. Ž., Stanić-Vučinić, D., Nikolić, S., Mihailović, J., Ćirković-Veličković, T.,& Grgurić Šipka, S.. (2019). Interactions of ruthenium(II)-cymene complexes with cytochrome c. in 1st FoodEnTwin Workshop “Food and Environmental –Omics”, Belgrade, Serbia, 20th-21st June, 2019. In: Book of Abstracts, 24-24.
https://hdl.handle.net/21.15107/rcub_cherry_6037

Radomirović MŽ, Stanić-Vučinić D, Nikolić S, Mihailović J, Ćirković-Veličković T, Grgurić Šipka S. Interactions of ruthenium(II)-cymene complexes with cytochrome c. in 1st FoodEnTwin Workshop “Food and Environmental –Omics”, Belgrade, Serbia, 20th-21st June, 2019. In: Book of Abstracts. 2019;:24-24.
https://hdl.handle.net/21.15107/rcub_cherry_6037 .

Radomirović, Mirjana Ž., Stanić-Vučinić, Dragana, Nikolić, Stefan, Mihailović, Jelena, Ćirković-Veličković, Tanja, Grgurić Šipka, Sanja, "Interactions of ruthenium(II)-cymene complexes with cytochrome c" in 1st FoodEnTwin Workshop “Food and Environmental –Omics”, Belgrade, Serbia, 20th-21st June, 2019. In: Book of Abstracts (2019):24-24,
https://hdl.handle.net/21.15107/rcub_cherry_6037 .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić Šipka, Sanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6038
AB  - Objective. In contrast to platinum-based antitumour compounds, the mode of action of ruthenium-based compounds is via protein targets involved in cellular signaling pathways and the histone proteins. As proteins are the first potential binding targets for the complexes in the bloodstream after their intravenous administration, interactions of anticancer therapeutics with proteins are very important to be investigated with aim to elucidate their pharmacokinetic pathways. Four half-sandwich ruthenium(II)-cymene complexes, developed earlier and with promising cytotoxic activity, are investigated  for their interactions with proteins, cytochrome c and lysozyme.

Material and Methods. Ruthenium(II)-cymene complexes were incubated for 24 and 48 h at 37 °C in the presence of cytochrome c and lysozyme, both in 20 mM ammonium hydrogen carbonate pH 7.4 and water. High-resolution LTQ-Orbitrap ESI MS was used to monitor the adducts formed between ruthenium complexes and proteins.

Results. The complexes with two Cl- ligands have shown higher reactivity to proteins than those with only one, and were more reactive toward cytochrome c in comparison to lysozyme. The complex with S,N-chelating ligand was less reactive to proteins than one with O,N-chelating ligand. Species initially coordinating the proteins are most likely dehalogenated complexes. During the time, vivid ligand exchange of non-arene organic ligand L with CO32- and OH- takes place after initial formation of protein adducts. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could be expected generating different intermediate protein species. 

Conclusions. Protein reactivity toward Ru(II) complexes is determined by protein structure and ligands in Ru(II) coordination sphere, but this reactivity should be described from both kinetics, as well as stability aspect. In extracellular or intracellular milieu, ability of metal binding ligands (such as carbonate ions) to bind and to leave, determinate both the extent and mechanism of the binding of ruthenium complexes to the target biomacromolecules for cancer therapy.
PB  - Faculty of Sciences
PB  - University of Novi Sad
PB  - Serbian Proteomics Assosication
C3  - V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad, Serbia, 31st May, 2019. In: The Book of Abstracts
T1  - Lysozyme and Cytochrome C adducts of ruthenium(II)-cymene complexes
SP  - P2
EP  - P2
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6038
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Stanić-Vučinić, Dragana and Nikolić, Stefan and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić Šipka, Sanja",
year = "2019",
abstract = "Objective. In contrast to platinum-based antitumour compounds, the mode of action of ruthenium-based compounds is via protein targets involved in cellular signaling pathways and the histone proteins. As proteins are the first potential binding targets for the complexes in the bloodstream after their intravenous administration, interactions of anticancer therapeutics with proteins are very important to be investigated with aim to elucidate their pharmacokinetic pathways. Four half-sandwich ruthenium(II)-cymene complexes, developed earlier and with promising cytotoxic activity, are investigated  for their interactions with proteins, cytochrome c and lysozyme.

Material and Methods. Ruthenium(II)-cymene complexes were incubated for 24 and 48 h at 37 °C in the presence of cytochrome c and lysozyme, both in 20 mM ammonium hydrogen carbonate pH 7.4 and water. High-resolution LTQ-Orbitrap ESI MS was used to monitor the adducts formed between ruthenium complexes and proteins.

Results. The complexes with two Cl- ligands have shown higher reactivity to proteins than those with only one, and were more reactive toward cytochrome c in comparison to lysozyme. The complex with S,N-chelating ligand was less reactive to proteins than one with O,N-chelating ligand. Species initially coordinating the proteins are most likely dehalogenated complexes. During the time, vivid ligand exchange of non-arene organic ligand L with CO32- and OH- takes place after initial formation of protein adducts. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could be expected generating different intermediate protein species. 

Conclusions. Protein reactivity toward Ru(II) complexes is determined by protein structure and ligands in Ru(II) coordination sphere, but this reactivity should be described from both kinetics, as well as stability aspect. In extracellular or intracellular milieu, ability of metal binding ligands (such as carbonate ions) to bind and to leave, determinate both the extent and mechanism of the binding of ruthenium complexes to the target biomacromolecules for cancer therapy.",
publisher = "Faculty of Sciences, University of Novi Sad, Serbian Proteomics Assosication",
journal = "V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad, Serbia, 31st May, 2019. In: The Book of Abstracts",
title = "Lysozyme and Cytochrome C adducts of ruthenium(II)-cymene complexes",
pages = "P2-P2",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6038"
}

Radomirović, M. Ž., Stanić-Vučinić, D., Nikolić, S., Mihailović, J., Ćirković-Veličković, T.,& Grgurić Šipka, S.. (2019). Lysozyme and Cytochrome C adducts of ruthenium(II)-cymene complexes. in V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad, Serbia, 31st May, 2019. In: The Book of Abstracts
Faculty of Sciences., P2-P2.
https://hdl.handle.net/21.15107/rcub_cherry_6038

Radomirović MŽ, Stanić-Vučinić D, Nikolić S, Mihailović J, Ćirković-Veličković T, Grgurić Šipka S. Lysozyme and Cytochrome C adducts of ruthenium(II)-cymene complexes. in V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad, Serbia, 31st May, 2019. In: The Book of Abstracts. 2019;:P2-P2.
https://hdl.handle.net/21.15107/rcub_cherry_6038 .

Radomirović, Mirjana Ž., Stanić-Vučinić, Dragana, Nikolić, Stefan, Mihailović, Jelena, Ćirković-Veličković, Tanja, Grgurić Šipka, Sanja, "Lysozyme and Cytochrome C adducts of ruthenium(II)-cymene complexes" in V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad, Serbia, 31st May, 2019. In: The Book of Abstracts (2019):P2-P2,
https://hdl.handle.net/21.15107/rcub_cherry_6038 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5721
AB  - Brief introduction: Stability to gastric digestion represents a very important parameter of food protein allergenicity. Usually digestion experiments are carried out on purified proteins or protein extracts; however, use of solid food is far closer to the in vivo situation, taking into account food protein interactions with other food components, such as polyphenols and lipids.
Objective: The aim of this study was to investigate and compare digestion stability and allergenicity of large and small peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under standardized and physiologically relevant in vitro conditions.
Methodology: In vitro simulated oral and gastric phase digestion was carried out with ground raw and roasted hazelnut kernels. Digested proteins were extracted from the mixture and analyzed by SDS-PAGE, 2D-PAGE, and compared with Image Master 2D Platinum 7.0. Western blot probed with allergic patients’ sera and specific antibodies for Cor a 8.
Main findings: Several important hazelnut seed storage digestion resistant proteins and peptides have been identified and characterized. Most abundant hazelnut allergens were resolved on a 2DE map, for instance acidic and basic chains of Cor a 9, and Cor a
11. Digestion-resistant peptides of Cor a 11 and Cor a 9 were able to bind IgE. Lipid transfer protein (Cor a 8) was highly resistant to gastric proteolysis. Conclusion: To conclude, roasted hazelnut is more prone to gastric digestion than raw, and cause milder IgE response in patients. Gastric phase digestion of raw and roasted hazelnut kernels results in partial extraction and digestion of Cor a 11 and Cor a 9 into digestion- resistant peptides with preserved IgE-binding epitopes. These results demonstrate substantial resistance of raw and roasted hazelnut allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion and retained their allergenicity.
PB  - Univerzitet u Beogradu - Hemijski fakultet
C3  - Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019
T1  - Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products
SP  - 25
EP  - 25
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5721
ER  - 

@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Mihailović, Jelena and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Brief introduction: Stability to gastric digestion represents a very important parameter of food protein allergenicity. Usually digestion experiments are carried out on purified proteins or protein extracts; however, use of solid food is far closer to the in vivo situation, taking into account food protein interactions with other food components, such as polyphenols and lipids.
Objective: The aim of this study was to investigate and compare digestion stability and allergenicity of large and small peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under standardized and physiologically relevant in vitro conditions.
Methodology: In vitro simulated oral and gastric phase digestion was carried out with ground raw and roasted hazelnut kernels. Digested proteins were extracted from the mixture and analyzed by SDS-PAGE, 2D-PAGE, and compared with Image Master 2D Platinum 7.0. Western blot probed with allergic patients’ sera and specific antibodies for Cor a 8.
Main findings: Several important hazelnut seed storage digestion resistant proteins and peptides have been identified and characterized. Most abundant hazelnut allergens were resolved on a 2DE map, for instance acidic and basic chains of Cor a 9, and Cor a
11. Digestion-resistant peptides of Cor a 11 and Cor a 9 were able to bind IgE. Lipid transfer protein (Cor a 8) was highly resistant to gastric proteolysis. Conclusion: To conclude, roasted hazelnut is more prone to gastric digestion than raw, and cause milder IgE response in patients. Gastric phase digestion of raw and roasted hazelnut kernels results in partial extraction and digestion of Cor a 11 and Cor a 9 into digestion- resistant peptides with preserved IgE-binding epitopes. These results demonstrate substantial resistance of raw and roasted hazelnut allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion and retained their allergenicity.",
publisher = "Univerzitet u Beogradu - Hemijski fakultet",
journal = "Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019",
title = "Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products",
pages = "25-25",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5721"
}

Prodić, I., Smiljanić, K., Mihailović, J., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2019). Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products. in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019
Univerzitet u Beogradu - Hemijski fakultet., 25-25.
https://hdl.handle.net/21.15107/rcub_cherry_5721

Prodić I, Smiljanić K, Mihailović J, Hoffmann-Sommergruber K, Ćirković-Veličković T. Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products. in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019. 2019;:25-25.
https://hdl.handle.net/21.15107/rcub_cherry_5721 .

Prodić, Ivana, Smiljanić, Katarina, Mihailović, Jelena, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products" in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019 (2019):25-25,
https://hdl.handle.net/21.15107/rcub_cherry_5721 .

TY  - CONF
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5722
AB  - Introduction. Peanut allergy affects a large portion of world population causing reactions ranging from mild to severe. Major peanut allergen IgE epitopes are well characterized but little is known about their post-translational modifications (PTM) and how they are affected by thermal treatment. PTM profile may differ between raw and thermally treated peanut, which could affect its allergic potential depending on type, size and position of modifications.
Objective. Our aim was to analyse and compare PTM profiles of 4 major peanut allergens - Ara h 1, Ara h 2, Ara h 3 and Ara h 6, as well as their amounts in raw and roasted samples using bottom-up proteomics methods.
Methodology. Full peanut protein extracts (both thermally treated and non-treated) were digested in gel and in solution, and analysed by a Top10 nLC-MS/MS method by LTQ Orbitrap XL (Thermo Fisher Scientific Inc., Germany). Within the extracts major allergens - Ara h 1, Ara h 2, Ara h 3 and Ara h 6 were identified, label free quantified (LFQ) and searched for PTMs by Peaks X software (Bioinformatics solutions Inc.I, Canada). Epitope sequences were acquired from the Immune Epitope Database (IEDB www.iedb.org).
Main findings. LFQ results show that there is no significant change in the amounts of any of the studied allergens between raw and roasted extracts. Out of the 4 allergens Ara h 6 is modified in the highest portion, with respect to the protein size: 15% and 12% of its positions are modified in raw and roasted sample, respectively. Total of 21 modifications were quantified between the two preparations, with oxidation (M), methylation (K,R) and dethiomethylation affecting the largest number of peptides.
Conclusions. Peanut allergen epitopes are indeed carriers of PTMs that differ in pattern and quantity between treated and non-treated extracts. The in silico discovered PTMs could affect protein digestibility and allergenicity. Further investigation is necessary in order to fully understand the impact protein modifications could have on their allergenic potential.
PB  - Univerzitet u Beogradu - Hemijski fakultet
C3  - Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019
T1  - Investigation of raw and thermally treated peanut major allergen post- translational modifications (PTMs)
IS  - 26
EP  - 26
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5722
ER  - 

@conference{
author = "Mihailović, Jelena and Prodić, Ivana and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Introduction. Peanut allergy affects a large portion of world population causing reactions ranging from mild to severe. Major peanut allergen IgE epitopes are well characterized but little is known about their post-translational modifications (PTM) and how they are affected by thermal treatment. PTM profile may differ between raw and thermally treated peanut, which could affect its allergic potential depending on type, size and position of modifications.
Objective. Our aim was to analyse and compare PTM profiles of 4 major peanut allergens - Ara h 1, Ara h 2, Ara h 3 and Ara h 6, as well as their amounts in raw and roasted samples using bottom-up proteomics methods.
Methodology. Full peanut protein extracts (both thermally treated and non-treated) were digested in gel and in solution, and analysed by a Top10 nLC-MS/MS method by LTQ Orbitrap XL (Thermo Fisher Scientific Inc., Germany). Within the extracts major allergens - Ara h 1, Ara h 2, Ara h 3 and Ara h 6 were identified, label free quantified (LFQ) and searched for PTMs by Peaks X software (Bioinformatics solutions Inc.I, Canada). Epitope sequences were acquired from the Immune Epitope Database (IEDB www.iedb.org).
Main findings. LFQ results show that there is no significant change in the amounts of any of the studied allergens between raw and roasted extracts. Out of the 4 allergens Ara h 6 is modified in the highest portion, with respect to the protein size: 15% and 12% of its positions are modified in raw and roasted sample, respectively. Total of 21 modifications were quantified between the two preparations, with oxidation (M), methylation (K,R) and dethiomethylation affecting the largest number of peptides.
Conclusions. Peanut allergen epitopes are indeed carriers of PTMs that differ in pattern and quantity between treated and non-treated extracts. The in silico discovered PTMs could affect protein digestibility and allergenicity. Further investigation is necessary in order to fully understand the impact protein modifications could have on their allergenic potential.",
publisher = "Univerzitet u Beogradu - Hemijski fakultet",
journal = "Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019",
title = "Investigation of raw and thermally treated peanut major allergen post- translational modifications (PTMs)",
number = "26",
pages = "26",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5722"
}

Mihailović, J., Prodić, I., Smiljanić, K.,& Ćirković-Veličković, T.. (2019). Investigation of raw and thermally treated peanut major allergen post- translational modifications (PTMs). in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019
Univerzitet u Beogradu - Hemijski fakultet.(26).
https://hdl.handle.net/21.15107/rcub_cherry_5722

Mihailović J, Prodić I, Smiljanić K, Ćirković-Veličković T. Investigation of raw and thermally treated peanut major allergen post- translational modifications (PTMs). in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019. 2019;(26):null-26.
https://hdl.handle.net/21.15107/rcub_cherry_5722 .

Mihailović, Jelena, Prodić, Ivana, Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Investigation of raw and thermally treated peanut major allergen post- translational modifications (PTMs)" in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019, no. 26 (2019),
https://hdl.handle.net/21.15107/rcub_cherry_5722 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
AU  - Mihailović, Jelena
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5723
AB  - Introduction
Stability to gastric digestion represents a very important parameter of food protein allergenicity. Usu-
ally digestion experiments are carried out on purified proteins or protein extracts; however, use of
solid food is far closer to the in vivo situation, taking into account food protein interactions with other
food components, such as polyphenols and lipids.
Objective
The aim of this study was to investigate and compare digestion stability and allergenicity of large
and small peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under
standardized and physiologically relevant in vitro conditions.
Methodology
In vitro simulated oral and gastric phase digestion was carried out with ground raw and roasted
hazelnut kernels. Digested proteins were extracted from the mixture and analyzed by SDS-PAGE,
2D-PAGE, and compared with Image Master 2D Platinum 7.0. Western blot probed with allergic
patients’ sera and specific antibodies for Cor a 8.
Main findings
Several important hazelnut seed storage digestion resistant proteins and peptides have been identi-
fied and characterized. Most abundant hazelnut allergens were resolved on a 2DE map, for instance,
acidic and basic chains of Cor a 9, and Cor a 11. Digestion-resistant peptides of Cor a 11 and Cor
a 9 were able to bind IgE. Lipid transfer protein (Cor a 8) was highly resistant to gastric proteolysis.
Conclusion
To conclude, roasted hazelnut is more prone to gastric digestion than raw, and cause milder IgE
response in patients. Gastric phase digestion of raw and roasted hazelnut kernels results in partial
extraction and digestion of Cor a 11 and Cor a 9 into digestion-resistant peptides with preserved
IgE-binding epitopes. These results demonstrate substantial resistance of raw and roasted hazelnut
allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion
and retained their allergenicity.
PB  - INFOGEST Cost action FA1402
C3  - Proceedings of the 6th International Conference on Food Digestion 2019
T1  - Digestomics of raw and roasted hazelnut according to harmonized static digestion method suitable for solid food and characterization of gastric-phase products
SP  - 191
EP  - 191
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5723
ER  - 

@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja and Mihailović, Jelena",
year = "2019",
abstract = "Introduction
Stability to gastric digestion represents a very important parameter of food protein allergenicity. Usu-
ally digestion experiments are carried out on purified proteins or protein extracts; however, use of
solid food is far closer to the in vivo situation, taking into account food protein interactions with other
food components, such as polyphenols and lipids.
Objective
The aim of this study was to investigate and compare digestion stability and allergenicity of large
and small peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under
standardized and physiologically relevant in vitro conditions.
Methodology
In vitro simulated oral and gastric phase digestion was carried out with ground raw and roasted
hazelnut kernels. Digested proteins were extracted from the mixture and analyzed by SDS-PAGE,
2D-PAGE, and compared with Image Master 2D Platinum 7.0. Western blot probed with allergic
patients’ sera and specific antibodies for Cor a 8.
Main findings
Several important hazelnut seed storage digestion resistant proteins and peptides have been identi-
fied and characterized. Most abundant hazelnut allergens were resolved on a 2DE map, for instance,
acidic and basic chains of Cor a 9, and Cor a 11. Digestion-resistant peptides of Cor a 11 and Cor
a 9 were able to bind IgE. Lipid transfer protein (Cor a 8) was highly resistant to gastric proteolysis.
Conclusion
To conclude, roasted hazelnut is more prone to gastric digestion than raw, and cause milder IgE
response in patients. Gastric phase digestion of raw and roasted hazelnut kernels results in partial
extraction and digestion of Cor a 11 and Cor a 9 into digestion-resistant peptides with preserved
IgE-binding epitopes. These results demonstrate substantial resistance of raw and roasted hazelnut
allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion
and retained their allergenicity.",
publisher = "INFOGEST Cost action FA1402",
journal = "Proceedings of the 6th International Conference on Food Digestion 2019",
title = "Digestomics of raw and roasted hazelnut according to harmonized static digestion method suitable for solid food and characterization of gastric-phase products",
pages = "191-191",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5723"
}

Prodić, I., Smiljanić, K., Hoffmann-Sommergruber, K., Ćirković-Veličković, T.,& Mihailović, J.. (2019). Digestomics of raw and roasted hazelnut according to harmonized static digestion method suitable for solid food and characterization of gastric-phase products. in Proceedings of the 6th International Conference on Food Digestion 2019
INFOGEST Cost action FA1402., 191-191.
https://hdl.handle.net/21.15107/rcub_cherry_5723

Prodić I, Smiljanić K, Hoffmann-Sommergruber K, Ćirković-Veličković T, Mihailović J. Digestomics of raw and roasted hazelnut according to harmonized static digestion method suitable for solid food and characterization of gastric-phase products. in Proceedings of the 6th International Conference on Food Digestion 2019. 2019;:191-191.
https://hdl.handle.net/21.15107/rcub_cherry_5723 .

Prodić, Ivana, Smiljanić, Katarina, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, Mihailović, Jelena, "Digestomics of raw and roasted hazelnut according to harmonized static digestion method suitable for solid food and characterization of gastric-phase products" in Proceedings of the 6th International Conference on Food Digestion 2019 (2019):191-191,
https://hdl.handle.net/21.15107/rcub_cherry_5723 .

TY  - CONF
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5725
AB  - Introduction. Peanut allergy affects a large portion of world population causing reactions ranging
from mild to severe. Major peanut allergen IgE epitopes are well characterized but little is known
about their post-translational modifications (PTM) and how they are affected by thermal
treatment. PTM profile may differ between raw and thermally treated peanut, which could affect
its allergic potential depending on type, size and position of modifications.
Objective. Our aim was to analyse and compare PTM profiles of 4 major peanut allergens - Ara h 1,
Ara h 2, Ara h 3 and Ara h 6, as well as their amounts in raw and roasted samples using bottom-up
proteomics methods.
Methodology. Full peanut protein extracts (both thermally treated and non-treated) were digested
in gel and in solution, and analysed by a Top10 nLC-MS/MS method by LTQ Orbitrap XL (Thermo
Fisher Scientific Inc., Germany). Within the extracts major allergens - Ara h 1, Ara h 2, Ara h 3 and
Ara h 6 were identified, label free quantified (LFQ) and searched for PTMs by Peaks X software
(Bioinformatics solutions Inc.I, Canada). Epitope sequences were acquired from the Immune
Epitope Database (IEDB www.iedb.org).
Main findings. LFQ results show that there is no significant change in the amountsof any of the
studied allergens between raw and roasted extracts.Out of the 4 allergens Ara h 6 is modified in the
highest portion, with respect to the protein size: 15% and 12% of its positions are modified in raw
and roasted sample, respectively. Total of 21 modifications were quantified between the two
preparations, with oxidation (M), methylation (K,R) and dethiomethylation affecting the largest
number of peptides.
Conclusions. Peanut allergen epitopes are indeed carriers of PTMs that differ in pattern and
quantity between treated and non-treated extracts. The in silico discovered PTMs could affect
protein digestibility and allergenicity. Further investigation is necessary in order to fully understand
the impact protein modifications could have on their allergenic potential.
PB  - Serbian Proteomic Association - SePA
C3  - Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019
T1  - Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs)
SP  - 16/L10
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5725
ER  - 

@conference{
author = "Mihailović, Jelena and Prodić, Ivana and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Introduction. Peanut allergy affects a large portion of world population causing reactions ranging
from mild to severe. Major peanut allergen IgE epitopes are well characterized but little is known
about their post-translational modifications (PTM) and how they are affected by thermal
treatment. PTM profile may differ between raw and thermally treated peanut, which could affect
its allergic potential depending on type, size and position of modifications.
Objective. Our aim was to analyse and compare PTM profiles of 4 major peanut allergens - Ara h 1,
Ara h 2, Ara h 3 and Ara h 6, as well as their amounts in raw and roasted samples using bottom-up
proteomics methods.
Methodology. Full peanut protein extracts (both thermally treated and non-treated) were digested
in gel and in solution, and analysed by a Top10 nLC-MS/MS method by LTQ Orbitrap XL (Thermo
Fisher Scientific Inc., Germany). Within the extracts major allergens - Ara h 1, Ara h 2, Ara h 3 and
Ara h 6 were identified, label free quantified (LFQ) and searched for PTMs by Peaks X software
(Bioinformatics solutions Inc.I, Canada). Epitope sequences were acquired from the Immune
Epitope Database (IEDB www.iedb.org).
Main findings. LFQ results show that there is no significant change in the amountsof any of the
studied allergens between raw and roasted extracts.Out of the 4 allergens Ara h 6 is modified in the
highest portion, with respect to the protein size: 15% and 12% of its positions are modified in raw
and roasted sample, respectively. Total of 21 modifications were quantified between the two
preparations, with oxidation (M), methylation (K,R) and dethiomethylation affecting the largest
number of peptides.
Conclusions. Peanut allergen epitopes are indeed carriers of PTMs that differ in pattern and
quantity between treated and non-treated extracts. The in silico discovered PTMs could affect
protein digestibility and allergenicity. Further investigation is necessary in order to fully understand
the impact protein modifications could have on their allergenic potential.",
publisher = "Serbian Proteomic Association - SePA",
journal = "Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019",
title = "Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs)",
pages = "16/L10",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5725"
}

Mihailović, J., Prodić, I., Smiljanić, K.,& Ćirković-Veličković, T.. (2019). Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs). in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019
Serbian Proteomic Association - SePA., 16/L10.
https://hdl.handle.net/21.15107/rcub_cherry_5725

Mihailović J, Prodić I, Smiljanić K, Ćirković-Veličković T. Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs). in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019. 2019;:16/L10.
https://hdl.handle.net/21.15107/rcub_cherry_5725 .

Mihailović, Jelena, Prodić, Ivana, Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs)" in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019 (2019):16/L10,
https://hdl.handle.net/21.15107/rcub_cherry_5725 .

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  - https://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
UR  - https://hdl.handle.net/21.15107/rcub_nardus_17611
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",
url = "https://hdl.handle.net/21.15107/rcub_nardus_17611"
}

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..
https://hdl.handle.net/21.15107/rcub_nardus_17611

Mihailović J. Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu. in Универзитет у Београду. 2019;.
https://hdl.handle.net/21.15107/rcub_nardus_17611 .

Mihailović, Jelena, "Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu" in Универзитет у Београду (2019),
https://hdl.handle.net/21.15107/rcub_nardus_17611 .

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Đukić, Teodora
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3745
C3  - Book of Abstracts,4th Edition of Global Conference on Plant Science and Molecular Biology
T1  - Impact of oxidative stress on plant proteins modifications: relevance for plant allergens
SP  - 130
EP  - 130
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3745
ER  - 

@conference{
author = "Smiljanić, Katarina and Mihailović, Jelena and Đukić, Teodora and Ćirković-Veličković, Tanja",
year = "2019",
journal = "Book of Abstracts,4th Edition of Global Conference on Plant Science and Molecular Biology",
title = "Impact of oxidative stress on plant proteins modifications: relevance for plant allergens",
pages = "130-130",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3745"
}

Smiljanić, K., Mihailović, J., Đukić, T.,& Ćirković-Veličković, T.. (2019). Impact of oxidative stress on plant proteins modifications: relevance for plant allergens. in Book of Abstracts,4th Edition of Global Conference on Plant Science and Molecular Biology, 130-130.
https://hdl.handle.net/21.15107/rcub_cherry_3745

Smiljanić K, Mihailović J, Đukić T, Ćirković-Veličković T. Impact of oxidative stress on plant proteins modifications: relevance for plant allergens. in Book of Abstracts,4th Edition of Global Conference on Plant Science and Molecular Biology. 2019;:130-130.
https://hdl.handle.net/21.15107/rcub_cherry_3745 .

Smiljanić, Katarina, Mihailović, Jelena, Đukić, Teodora, Ćirković-Veličković, Tanja, "Impact of oxidative stress on plant proteins modifications: relevance for plant allergens" in Book of Abstracts,4th Edition of Global Conference on Plant Science and Molecular Biology (2019):130-130,
https://hdl.handle.net/21.15107/rcub_cherry_3745 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Dubiela, Pawel
AU  - Mihailović, Jelena
AU  - Stanić-Vučinić, Dragana
AU  - Smiljanić, Katarina
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5719
AB  - Background: Sensitization to non-specific lipid transfer protein (ns-LTPs) in plant foods is regarded as a risk factor for generalized allergic reactions. Stability to gastric digestion represents very important parameter of food proteins allergenicity. Usually studies of digestion were carried out on purified proteins, but has never been examined the influence of different food matrices on different allergens. Allergens from the nsLTP family are known to share a characteristic structure which is highly resistant to proteolysis, and therefore, IgE cross-reactivity of nsLTPs needs to be investigated in the environment such as complex food matrix.
Objective: The aim of this research project is to reveal how proteins are digested (by Minekus protocol) within the natural food matrix and possible consequences on their allergenicity, with the special focus on ns-LTP.
Methods: Pure nsLTPs from walnut were labelled with Alexa 633 and added to whole grain of grounded raw walnuts, incubated with human α-amylase, and pepsin, therefore mimicking the effects of oral and gastric digestion, in total duration of 2h. Proteins extracted from the mixture were analyzed by one-dimensional (1D) and two-dimensional SDS-PAGe, and respective 1D and 2D immunoblots.
Results: Most proteins from pepsin digested walnut sample were more resistant to digestion according to 1D SDS PAGE. Pepsin digested raw walnut sample with nsLTP were assessed by 2D PAGE to compare profiles of the digested and control sample (no pepsin added). 2D SDSPAGE of digested and control walnut samples showed almost identical profiles, especially in the context of fluorescently labelled nsLTP allergens. These results demonstrate substantial resistance of nsLTP allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion.
Conclusion: Further research is needed to be able to grade stability/resistance of selected food allergens to gastric digestion as a consequence of food matrix modulating effects. We propose that certain combinations of foods and allergens could provide additional protection or on the contrary ease the digestion, by comparing trends between control and digested samples and between different digested combinations as well.
PB  - IMPARAS Cost Action FA1402
C3  - Proceedings of the 4th International ImpARAS 
Conference, Portici (Naples), Italy, June 19-21, 2018
T1  - Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion
SP  - 59
EP  - 59
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5719
ER  - 

@conference{
author = "Prodić, Ivana and Dubiela, Pawel and Mihailović, Jelena and Stanić-Vučinić, Dragana and Smiljanić, Katarina and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Background: Sensitization to non-specific lipid transfer protein (ns-LTPs) in plant foods is regarded as a risk factor for generalized allergic reactions. Stability to gastric digestion represents very important parameter of food proteins allergenicity. Usually studies of digestion were carried out on purified proteins, but has never been examined the influence of different food matrices on different allergens. Allergens from the nsLTP family are known to share a characteristic structure which is highly resistant to proteolysis, and therefore, IgE cross-reactivity of nsLTPs needs to be investigated in the environment such as complex food matrix.
Objective: The aim of this research project is to reveal how proteins are digested (by Minekus protocol) within the natural food matrix and possible consequences on their allergenicity, with the special focus on ns-LTP.
Methods: Pure nsLTPs from walnut were labelled with Alexa 633 and added to whole grain of grounded raw walnuts, incubated with human α-amylase, and pepsin, therefore mimicking the effects of oral and gastric digestion, in total duration of 2h. Proteins extracted from the mixture were analyzed by one-dimensional (1D) and two-dimensional SDS-PAGe, and respective 1D and 2D immunoblots.
Results: Most proteins from pepsin digested walnut sample were more resistant to digestion according to 1D SDS PAGE. Pepsin digested raw walnut sample with nsLTP were assessed by 2D PAGE to compare profiles of the digested and control sample (no pepsin added). 2D SDSPAGE of digested and control walnut samples showed almost identical profiles, especially in the context of fluorescently labelled nsLTP allergens. These results demonstrate substantial resistance of nsLTP allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion.
Conclusion: Further research is needed to be able to grade stability/resistance of selected food allergens to gastric digestion as a consequence of food matrix modulating effects. We propose that certain combinations of foods and allergens could provide additional protection or on the contrary ease the digestion, by comparing trends between control and digested samples and between different digested combinations as well.",
publisher = "IMPARAS Cost Action FA1402",
journal = "Proceedings of the 4th International ImpARAS 
Conference, Portici (Naples), Italy, June 19-21, 2018",
title = "Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion",
pages = "59-59",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5719"
}

Prodić, I., Dubiela, P., Mihailović, J., Stanić-Vučinić, D., Smiljanić, K., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2018). Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion. in Proceedings of the 4th International ImpARAS 
Conference, Portici (Naples), Italy, June 19-21, 2018
IMPARAS Cost Action FA1402., 59-59.
https://hdl.handle.net/21.15107/rcub_cherry_5719

Prodić I, Dubiela P, Mihailović J, Stanić-Vučinić D, Smiljanić K, Hoffmann-Sommergruber K, Ćirković-Veličković T. Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion. in Proceedings of the 4th International ImpARAS 
Conference, Portici (Naples), Italy, June 19-21, 2018. 2018;:59-59.
https://hdl.handle.net/21.15107/rcub_cherry_5719 .

Prodić, Ivana, Dubiela, Pawel, Mihailović, Jelena, Stanić-Vučinić, Dragana, Smiljanić, Katarina, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion" in Proceedings of the 4th International ImpARAS 
Conference, Portici (Naples), Italy, June 19-21, 2018 (2018):59-59,
https://hdl.handle.net/21.15107/rcub_cherry_5719 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Radosavljević, Jelena
AU  - Mihailović, Jelena
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5714
AB  - Objective: Major peanut allergens, Ara h 2 and Ara h 6, are known to be resistant to pepsin
digestion, and they sensitize individual via the gastrointestinal tract. Mikenus et al. published a
standardized static digestion method for food, based on physiological conditions emphasizing the
impact of food matrices. Immunoreactive proteins (large fragments) and peptides (short digestion
resistant peptides SDRPs; <10 kDa), to which the immune system of the gastrointestinal tract is
exposed during digestion of peanut proteins, has not been investigated under pure physiological
conditions suggested by this protocol.
Matherial and methods: Whole grain of grounded raw peanut was incubated with human α-
amylase, and pepsin, mimicking the effects of oral and gastric digestion, in total duration of 2h.
Bottom up proteomic approach, immunoblotting with allergen-specific antibodies from peanut-
sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, were
used to identify and characterize peanut digesta.
Results: After 2h of oral/gastric phase we got, intact proteins, large, digestion resistant peptides
(DRP) and SDRPs, as well. Ara h 2 and Ara h 6 remained mostly intact, and short DRPs from Ara h
2 and Ara h 6 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h
3 showed preserved allergenic capacity, as well. Almost all of identified short DRPs from Ara h 1,
Ara h 2 and Ara h 3, with preserved allergenic potential, were constituents of continuous epitope
sequences found via Immune Epitope Database (www.iedb.org).
Conclusion: Processes of protein extraction from the matrix and their enzymatic digestion occur
simultaneously. Oral and gastric phase digestion products of raw peanut are intact proteins, large
and short digestion resistant peptides. Under these conditions Ara h 2 and Ara h 6 are expectedly
PB  - Srpsko Udruženje za Proteomiku; IBISS
C3  - IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
T1  - Gastric digestome of whole peanut grains from the aspect of immunoproteomics: Characterization of digested allergens in the real food matrix
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5714
ER  - 

@conference{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Radosavljević, Jelena and Mihailović, Jelena and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Objective: Major peanut allergens, Ara h 2 and Ara h 6, are known to be resistant to pepsin
digestion, and they sensitize individual via the gastrointestinal tract. Mikenus et al. published a
standardized static digestion method for food, based on physiological conditions emphasizing the
impact of food matrices. Immunoreactive proteins (large fragments) and peptides (short digestion
resistant peptides SDRPs; <10 kDa), to which the immune system of the gastrointestinal tract is
exposed during digestion of peanut proteins, has not been investigated under pure physiological
conditions suggested by this protocol.
Matherial and methods: Whole grain of grounded raw peanut was incubated with human α-
amylase, and pepsin, mimicking the effects of oral and gastric digestion, in total duration of 2h.
Bottom up proteomic approach, immunoblotting with allergen-specific antibodies from peanut-
sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, were
used to identify and characterize peanut digesta.
Results: After 2h of oral/gastric phase we got, intact proteins, large, digestion resistant peptides
(DRP) and SDRPs, as well. Ara h 2 and Ara h 6 remained mostly intact, and short DRPs from Ara h
2 and Ara h 6 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h
3 showed preserved allergenic capacity, as well. Almost all of identified short DRPs from Ara h 1,
Ara h 2 and Ara h 3, with preserved allergenic potential, were constituents of continuous epitope
sequences found via Immune Epitope Database (www.iedb.org).
Conclusion: Processes of protein extraction from the matrix and their enzymatic digestion occur
simultaneously. Oral and gastric phase digestion products of raw peanut are intact proteins, large
and short digestion resistant peptides. Under these conditions Ara h 2 and Ara h 6 are expectedly",
publisher = "Srpsko Udruženje za Proteomiku; IBISS",
journal = "IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija",
title = "Gastric digestome of whole peanut grains from the aspect of immunoproteomics: Characterization of digested allergens in the real food matrix",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5714"
}

Prodić, I., Stanić-Vučinić, D., Apostolović, D., Radosavljević, J., Mihailović, J., Smiljanić, K.,& Ćirković-Veličković, T.. (2018). Gastric digestome of whole peanut grains from the aspect of immunoproteomics: Characterization of digested allergens in the real food matrix. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
Srpsko Udruženje za Proteomiku; IBISS..
https://hdl.handle.net/21.15107/rcub_cherry_5714

Prodić I, Stanić-Vučinić D, Apostolović D, Radosavljević J, Mihailović J, Smiljanić K, Ćirković-Veličković T. Gastric digestome of whole peanut grains from the aspect of immunoproteomics: Characterization of digested allergens in the real food matrix. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija. 2018;.
https://hdl.handle.net/21.15107/rcub_cherry_5714 .

Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Radosavljević, Jelena, Mihailović, Jelena, Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Gastric digestome of whole peanut grains from the aspect of immunoproteomics: Characterization of digested allergens in the real food matrix" in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija (2018),
https://hdl.handle.net/21.15107/rcub_cherry_5714 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Khulal, Urmila
AU  - Mutić, Jelena
AU  - Mihailović, Jelena
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5710
AB  - Objective: Haliotis discus (Japanese abalone), mollusks among various shellfish, is a highly
nutritive food resource in the world, but also among the eight allergic food groups accounting for
approximately 90% of all immunoglobulin E food allergies worldwide. The general objective of our
research is to comprehensively investigate stability and structures of pepsin-resistant allergens, of
their larger fragments, and of short digestion resistant peptides (SDRPs) released by pepsin
digestion of whole raw and extract of shellfish, under standardized and physiologically relevant
gastric conditions.
Materials and Methods: Extract of raw whole shellfish (eRSS) and whole raw shellfish (wRSS),
were pepsin digested according to standardized static digestion protocol. Controls were treated in a
same manner without adding pepsin. Supernatant of samples and its counterpart controls were
precipitated with TCA/acetone. Obtained proteins were assessed by 2D SDS PAGE and 1D SDS-
PAGE, under reducing and non-reducing conditions. 1D SDS-PAGE of RSS were analyzed by
ncLC-MS/MS (Orbitrap LTQ) shot-gun proteomics. Relative quantification was performed by LFQ
algorithm within Peaks 8.5 software package Bioinformatics Solutions Inc. (BSI), Waterloo,
Canada.
Results and Conclusion: 1D SDS-PAGE analysis of eRSS and wRSS, and its controls showed a
range of proteins in varied concentrations between 10-250 kDa. In extracted and whole raw
shellfish, approximately 22 prominent protein bands were observed including the distinct bands
corresponding with the molecular weights of recognized shellfish allergen, tropomyosin (37-
39kDa). Fewer high molecular weight proteins were observed followed by protein smearing,
specifically around the low molecular weight protein bands. The smearing could possibly be due to
the breakdown products and the glycation. There were slight differences between the protein
profiles under reducing and non-reducing conditions as well. Nevertheless, there was the retention
of a band in the 37kDa molecular weight marker in all 4 samples, likely consistent with heat stable
tropomyosin (TM). Mass spectrometry showed allergens that are characterized (Hal d 1 and Hal di
1), with 90% of sequence homology with main tropomyosin allergens from seafood.
Scientific impact and relevance: The results will highlight effects of food matrix on shellfish
allergens digestibility proving its relevancy in molecular allergology. Moreover, an insight will be
obtained on the differences in digestibility of allergenic versus non-allergenic tropomyosins in the
real food matrix.
PB  - Srpsko Udruženje za Proteomiku, SePA; IBISS
C3  - IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
T1  - Digestomics of Japanese abalone in real food matrix
SP  - 10
EP  - 10
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5710
ER  - 

@conference{
author = "Prodić, Ivana and Khulal, Urmila and Mutić, Jelena and Mihailović, Jelena and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Objective: Haliotis discus (Japanese abalone), mollusks among various shellfish, is a highly
nutritive food resource in the world, but also among the eight allergic food groups accounting for
approximately 90% of all immunoglobulin E food allergies worldwide. The general objective of our
research is to comprehensively investigate stability and structures of pepsin-resistant allergens, of
their larger fragments, and of short digestion resistant peptides (SDRPs) released by pepsin
digestion of whole raw and extract of shellfish, under standardized and physiologically relevant
gastric conditions.
Materials and Methods: Extract of raw whole shellfish (eRSS) and whole raw shellfish (wRSS),
were pepsin digested according to standardized static digestion protocol. Controls were treated in a
same manner without adding pepsin. Supernatant of samples and its counterpart controls were
precipitated with TCA/acetone. Obtained proteins were assessed by 2D SDS PAGE and 1D SDS-
PAGE, under reducing and non-reducing conditions. 1D SDS-PAGE of RSS were analyzed by
ncLC-MS/MS (Orbitrap LTQ) shot-gun proteomics. Relative quantification was performed by LFQ
algorithm within Peaks 8.5 software package Bioinformatics Solutions Inc. (BSI), Waterloo,
Canada.
Results and Conclusion: 1D SDS-PAGE analysis of eRSS and wRSS, and its controls showed a
range of proteins in varied concentrations between 10-250 kDa. In extracted and whole raw
shellfish, approximately 22 prominent protein bands were observed including the distinct bands
corresponding with the molecular weights of recognized shellfish allergen, tropomyosin (37-
39kDa). Fewer high molecular weight proteins were observed followed by protein smearing,
specifically around the low molecular weight protein bands. The smearing could possibly be due to
the breakdown products and the glycation. There were slight differences between the protein
profiles under reducing and non-reducing conditions as well. Nevertheless, there was the retention
of a band in the 37kDa molecular weight marker in all 4 samples, likely consistent with heat stable
tropomyosin (TM). Mass spectrometry showed allergens that are characterized (Hal d 1 and Hal di
1), with 90% of sequence homology with main tropomyosin allergens from seafood.
Scientific impact and relevance: The results will highlight effects of food matrix on shellfish
allergens digestibility proving its relevancy in molecular allergology. Moreover, an insight will be
obtained on the differences in digestibility of allergenic versus non-allergenic tropomyosins in the
real food matrix.",
publisher = "Srpsko Udruženje za Proteomiku, SePA; IBISS",
journal = "IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija",
title = "Digestomics of Japanese abalone in real food matrix",
pages = "10-10",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5710"
}

Prodić, I., Khulal, U., Mutić, J., Mihailović, J., Smiljanić, K.,& Ćirković-Veličković, T.. (2018). Digestomics of Japanese abalone in real food matrix. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
Srpsko Udruženje za Proteomiku, SePA; IBISS., 10-10.
https://hdl.handle.net/21.15107/rcub_cherry_5710

Prodić I, Khulal U, Mutić J, Mihailović J, Smiljanić K, Ćirković-Veličković T. Digestomics of Japanese abalone in real food matrix. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija. 2018;:10-10.
https://hdl.handle.net/21.15107/rcub_cherry_5710 .

Prodić, Ivana, Khulal, Urmila, Mutić, Jelena, Mihailović, Jelena, Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Digestomics of Japanese abalone in real food matrix" in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija (2018):10-10,
https://hdl.handle.net/21.15107/rcub_cherry_5710 .

TY  - CONF
AU  - Mihailović, Jelena
AU  - Apostolović, Danijela
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5713
AB  - Peanut allergy affects a large portion of world population causing reactions ranging from
mild to severe. Seed storage proteins Ara h 1, Ara h 2, Ara h 3 and Ara h 6 are peanut
allergens, with well characterized IgE epitopes but little is known about PTMs effect on their
properties. Our aim was to investigate PTMs present on known epitopes of said purified
proteins using bottom-up proteomcs methods.
Out of the 4 allergens, Ara h 2 has the highest number of PTMs (14), while the most common
are hydroxylation Pro, dehydration and deamidation (N, Q). Peanut allergen epitopes are
indeed carriers of PTMs that could affect protein allergenicity and digestibility. Further
investigation on peanut extracts prepared in different ways is necessary in order to fully
understand the impact protein modifications could have on their allergenic potential.
PB  - Beograd : Srpsko hemijsko društvo
C3  - 55. savetovanje Srpskog hemijskog društva, Kratki izvodi radova
T1  - Post-translational modifications (PTMs) of major peanut allergen epitopes occurring as a result of purification process
SP  - 66
EP  - 66
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5713
ER  - 

@conference{
author = "Mihailović, Jelena and Apostolović, Danijela and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Peanut allergy affects a large portion of world population causing reactions ranging from
mild to severe. Seed storage proteins Ara h 1, Ara h 2, Ara h 3 and Ara h 6 are peanut
allergens, with well characterized IgE epitopes but little is known about PTMs effect on their
properties. Our aim was to investigate PTMs present on known epitopes of said purified
proteins using bottom-up proteomcs methods.
Out of the 4 allergens, Ara h 2 has the highest number of PTMs (14), while the most common
are hydroxylation Pro, dehydration and deamidation (N, Q). Peanut allergen epitopes are
indeed carriers of PTMs that could affect protein allergenicity and digestibility. Further
investigation on peanut extracts prepared in different ways is necessary in order to fully
understand the impact protein modifications could have on their allergenic potential.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "55. savetovanje Srpskog hemijskog društva, Kratki izvodi radova",
title = "Post-translational modifications (PTMs) of major peanut allergen epitopes occurring as a result of purification process",
pages = "66-66",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5713"
}

Mihailović, J., Apostolović, D., Smiljanić, K.,& Ćirković-Veličković, T.. (2018). Post-translational modifications (PTMs) of major peanut allergen epitopes occurring as a result of purification process. in 55. savetovanje Srpskog hemijskog društva, Kratki izvodi radova
Beograd : Srpsko hemijsko društvo., 66-66.
https://hdl.handle.net/21.15107/rcub_cherry_5713

Mihailović J, Apostolović D, Smiljanić K, Ćirković-Veličković T. Post-translational modifications (PTMs) of major peanut allergen epitopes occurring as a result of purification process. in 55. savetovanje Srpskog hemijskog društva, Kratki izvodi radova. 2018;:66-66.
https://hdl.handle.net/21.15107/rcub_cherry_5713 .

Mihailović, Jelena, Apostolović, Danijela, Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Post-translational modifications (PTMs) of major peanut allergen epitopes occurring as a result of purification process" in 55. savetovanje Srpskog hemijskog društva, Kratki izvodi radova (2018):66-66,
https://hdl.handle.net/21.15107/rcub_cherry_5713 .