TY  - DATA
AU  - Smiljanić, Katarina
PY  - 2024
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6462
AB  - This research dataset encompasess the post-translational and protein modificatrion profiles of raw and roasted shrimpts done with tandem mass spectroscopy (Orbitrap Exploris 240) and processed with PEAKS X pro Studio, with its PTM engine. From these level of results (PEAKS PTM) an ptm profiling was extracted and presented here. An .rar file was created containing ptm profile of raw shirmp and prtm profile of the roasted shrimp in an excel format.
PB  - Univerzitet u Beogradu - Hemijski fakultet
T2  - Journal of Functional Foods
T1  - Research data for: Khulal, U., Đukić, T., Smiljanić, K., Vasović, T., Aćimović, J., Rajković, A.,& Ćirković-Veličković, T.. (2024). Protein modifications screening of raw and thermally treated meat gastrointestinal digesta. in Journal of Functional Foods Elsevier., 113, 106052. https://doi.org/10.1016/j.jff.2024.106052
VL  - 113
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6462
ER  - 

@misc{
author = "Smiljanić, Katarina",
year = "2024",
abstract = "This research dataset encompasess the post-translational and protein modificatrion profiles of raw and roasted shrimpts done with tandem mass spectroscopy (Orbitrap Exploris 240) and processed with PEAKS X pro Studio, with its PTM engine. From these level of results (PEAKS PTM) an ptm profiling was extracted and presented here. An .rar file was created containing ptm profile of raw shirmp and prtm profile of the roasted shrimp in an excel format.",
publisher = "Univerzitet u Beogradu - Hemijski fakultet",
journal = "Journal of Functional Foods",
title = "Research data for: Khulal, U., Đukić, T., Smiljanić, K., Vasović, T., Aćimović, J., Rajković, A.,& Ćirković-Veličković, T.. (2024). Protein modifications screening of raw and thermally treated meat gastrointestinal digesta. in Journal of Functional Foods Elsevier., 113, 106052. https://doi.org/10.1016/j.jff.2024.106052",
volume = "113",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6462"
}

Smiljanić, K.. (2024). Research data for: Khulal, U., Đukić, T., Smiljanić, K., Vasović, T., Aćimović, J., Rajković, A.,& Ćirković-Veličković, T.. (2024). Protein modifications screening of raw and thermally treated meat gastrointestinal digesta. in Journal of Functional Foods Elsevier., 113, 106052. https://doi.org/10.1016/j.jff.2024.106052. in Journal of Functional Foods
Univerzitet u Beogradu - Hemijski fakultet., 113.
https://hdl.handle.net/21.15107/rcub_cherry_6462

Smiljanić K. Research data for: Khulal, U., Đukić, T., Smiljanić, K., Vasović, T., Aćimović, J., Rajković, A.,& Ćirković-Veličković, T.. (2024). Protein modifications screening of raw and thermally treated meat gastrointestinal digesta. in Journal of Functional Foods Elsevier., 113, 106052. https://doi.org/10.1016/j.jff.2024.106052. in Journal of Functional Foods. 2024;113.
https://hdl.handle.net/21.15107/rcub_cherry_6462 .

Smiljanić, Katarina, "Research data for: Khulal, U., Đukić, T., Smiljanić, K., Vasović, T., Aćimović, J., Rajković, A.,& Ćirković-Veličković, T.. (2024). Protein modifications screening of raw and thermally treated meat gastrointestinal digesta. in Journal of Functional Foods Elsevier., 113, 106052. https://doi.org/10.1016/j.jff.2024.106052" in Journal of Functional Foods, 113 (2024),
https://hdl.handle.net/21.15107/rcub_cherry_6462 .

TY  - JOUR
AU  - Khulal, Urmila
AU  - Đukić, Teodora
AU  - Smiljanić, Katarina
AU  - Vasović, Tamara
AU  - Aćimović, Jelena
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2024
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6437
AB  - Meat samples were subjected to thermal processing combined with simulated INFOGEST in vitro gastrointestinal (GI) digestion. Protein modifications (PMs) were screened with commercially available PM-specific antibodies. Specific proteins at 20, 37, 50, and 65 kDa react to more than 3 PM-specific antibodies among meat proteins. Lysine methylation and methionine oxidation were the most prominent PMs in WB. Mass spectrometry confirmed bands at ≈20 kDa as allergenic proteins: sarcoplasmic calcium-binding protein in oyster, 37 kDa as tropomyosin in shrimp, oyster, and abalone. MS-identified PMs of shellfish allergens were aligned to the IgE binding epitopes. GI digestion-resistant peptides of shellfish proteins were identified as paramyosins in oyster and abalone and SBP in shrimp. Our results point to the high susceptibility of immunodominant epitopes of major shellfish allergens to PMs. In TPM, saturation of oxidative modification increases with thermal processing resulting in higher susceptibility of TPM to gastric digestion.
PB  - Elsevier
T2  - Journal of Functional Foods
T1  - Protein modifications screening of raw and thermally treated meat gastrointestinal digesta
VL  - 113
SP  - 106052
DO  - 10.1016/j.jff.2024.106052
ER  - 

@article{
author = "Khulal, Urmila and Đukić, Teodora and Smiljanić, Katarina and Vasović, Tamara and Aćimović, Jelena and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2024",
abstract = "Meat samples were subjected to thermal processing combined with simulated INFOGEST in vitro gastrointestinal (GI) digestion. Protein modifications (PMs) were screened with commercially available PM-specific antibodies. Specific proteins at 20, 37, 50, and 65 kDa react to more than 3 PM-specific antibodies among meat proteins. Lysine methylation and methionine oxidation were the most prominent PMs in WB. Mass spectrometry confirmed bands at ≈20 kDa as allergenic proteins: sarcoplasmic calcium-binding protein in oyster, 37 kDa as tropomyosin in shrimp, oyster, and abalone. MS-identified PMs of shellfish allergens were aligned to the IgE binding epitopes. GI digestion-resistant peptides of shellfish proteins were identified as paramyosins in oyster and abalone and SBP in shrimp. Our results point to the high susceptibility of immunodominant epitopes of major shellfish allergens to PMs. In TPM, saturation of oxidative modification increases with thermal processing resulting in higher susceptibility of TPM to gastric digestion.",
publisher = "Elsevier",
journal = "Journal of Functional Foods",
title = "Protein modifications screening of raw and thermally treated meat gastrointestinal digesta",
volume = "113",
pages = "106052",
doi = "10.1016/j.jff.2024.106052"
}

Khulal, U., Đukić, T., Smiljanić, K., Vasović, T., Aćimović, J., Rajković, A.,& Ćirković-Veličković, T.. (2024). Protein modifications screening of raw and thermally treated meat gastrointestinal digesta. in Journal of Functional Foods
Elsevier., 113, 106052.
https://doi.org/10.1016/j.jff.2024.106052

Khulal U, Đukić T, Smiljanić K, Vasović T, Aćimović J, Rajković A, Ćirković-Veličković T. Protein modifications screening of raw and thermally treated meat gastrointestinal digesta. in Journal of Functional Foods. 2024;113:106052.
doi:10.1016/j.jff.2024.106052 .

Khulal, Urmila, Đukić, Teodora, Smiljanić, Katarina, Vasović, Tamara, Aćimović, Jelena, Rajković, Andreja, Ćirković-Veličković, Tanja, "Protein modifications screening of raw and thermally treated meat gastrointestinal digesta" in Journal of Functional Foods, 113 (2024):106052,
https://doi.org/10.1016/j.jff.2024.106052 . .

TY  - JOUR
AU  - Abdelhameed, Shorok A. M.
AU  - de Azambuja, Francisco
AU  - Vasović, Tamara
AU  - Savić, Nada D.
AU  - Ćirković-Veličković, Tanja
AU  - Parac-Vogt, Tatjana N.
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5816
AB  - Oxidative modifications of proteins are key to many applications in biotechnology. Metal-catalyzed oxidation reactions efficiently oxidize proteins but with low selectivity, and are highly dependent on the protein surface residues to direct the reaction. Herein, we demonstrate that discrete inorganic ligands such as polyoxometalates enable an efficient and selective protein oxidative cleavage. In the presence of ascorbate (1 mM), the Cu-substituted polyoxometalate K8[Cu2+(H2O)(α2-P2W17O61)], (CuIIWD, 0.05 mM) selectively cleave hen egg white lysozyme under physiological conditions (pH =7.5, 37 °C) producing only four bands in the gel electropherogram (12.7, 11, 10, and 5 kDa). Liquid chromatography/mass spectrometry analysis reveals a regioselective cleavage in the vicinity of crystallographic CuIIWD/lysozyme interaction sites. Mechanistically, polyoxometalate is critical to position the Cu at the protein surface and limit the generation of oxidative species to the proximity of binding sites. Ultimately, this study outlines the potential of discrete, designable metal oxo clusters as catalysts for the selective modification of proteins through radical mechanisms under non-denaturing conditions.
PB  - Springer Nature
T2  - Nature Communications
T1  - Regioselective protein oxidative cleavage enabled by enzyme-like recognition of an inorganic metal oxo cluster ligand
VL  - 14
IS  - 1
SP  - 486
DO  - 10.1038/s41467-023-36085-z
ER  - 

@article{
author = "Abdelhameed, Shorok A. M. and de Azambuja, Francisco and Vasović, Tamara and Savić, Nada D. and Ćirković-Veličković, Tanja and Parac-Vogt, Tatjana N.",
year = "2023",
abstract = "Oxidative modifications of proteins are key to many applications in biotechnology. Metal-catalyzed oxidation reactions efficiently oxidize proteins but with low selectivity, and are highly dependent on the protein surface residues to direct the reaction. Herein, we demonstrate that discrete inorganic ligands such as polyoxometalates enable an efficient and selective protein oxidative cleavage. In the presence of ascorbate (1 mM), the Cu-substituted polyoxometalate K8[Cu2+(H2O)(α2-P2W17O61)], (CuIIWD, 0.05 mM) selectively cleave hen egg white lysozyme under physiological conditions (pH =7.5, 37 °C) producing only four bands in the gel electropherogram (12.7, 11, 10, and 5 kDa). Liquid chromatography/mass spectrometry analysis reveals a regioselective cleavage in the vicinity of crystallographic CuIIWD/lysozyme interaction sites. Mechanistically, polyoxometalate is critical to position the Cu at the protein surface and limit the generation of oxidative species to the proximity of binding sites. Ultimately, this study outlines the potential of discrete, designable metal oxo clusters as catalysts for the selective modification of proteins through radical mechanisms under non-denaturing conditions.",
publisher = "Springer Nature",
journal = "Nature Communications",
title = "Regioselective protein oxidative cleavage enabled by enzyme-like recognition of an inorganic metal oxo cluster ligand",
volume = "14",
number = "1",
pages = "486",
doi = "10.1038/s41467-023-36085-z"
}

Abdelhameed, S. A. M., de Azambuja, F., Vasović, T., Savić, N. D., Ćirković-Veličković, T.,& Parac-Vogt, T. N.. (2023). Regioselective protein oxidative cleavage enabled by enzyme-like recognition of an inorganic metal oxo cluster ligand. in Nature Communications
Springer Nature., 14(1), 486.
https://doi.org/10.1038/s41467-023-36085-z

Abdelhameed SAM, de Azambuja F, Vasović T, Savić ND, Ćirković-Veličković T, Parac-Vogt TN. Regioselective protein oxidative cleavage enabled by enzyme-like recognition of an inorganic metal oxo cluster ligand. in Nature Communications. 2023;14(1):486.
doi:10.1038/s41467-023-36085-z .

Abdelhameed, Shorok A. M., de Azambuja, Francisco, Vasović, Tamara, Savić, Nada D., Ćirković-Veličković, Tanja, Parac-Vogt, Tatjana N., "Regioselective protein oxidative cleavage enabled by enzyme-like recognition of an inorganic metal oxo cluster ligand" in Nature Communications, 14, no. 1 (2023):486,
https://doi.org/10.1038/s41467-023-36085-z . .

TY  - DATA
AU  - Abdelhameed, Shorok A. M.
AU  - de Azambuja, Francisco
AU  - Vasović, Tamara
AU  - Savić, Nada D.
AU  - Ćirković-Veličković, Tanja
AU  - Parac-Vogt, Tatjana N.
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5816
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5840
AB  - Oxidative modifications of proteins are key to many applications in biotechnology. Metal-catalyzed oxidation reactions efficiently oxidize proteins but with low selectivity, and are highly dependent on the protein surface residues to direct the reaction. Herein, we demonstrate that discrete inorganic ligands such as polyoxometalates enable an efficient and selective protein oxidative cleavage. In the presence of ascorbate (1 mM), the Cu-substituted polyoxometalate K8[Cu2+(H2O)(α2-P2W17O61)], (CuIIWD, 0.05 mM) selectively cleave hen egg white lysozyme under physiological conditions (pH =7.5, 37 °C) producing only four bands in the gel electropherogram (12.7, 11, 10, and 5 kDa). Liquid chromatography/mass spectrometry analysis reveals a regioselective cleavage in the vicinity of crystallographic CuIIWD/lysozyme interaction sites. Mechanistically, polyoxometalate is critical to position the Cu at the protein surface and limit the generation of oxidative species to the proximity of binding sites. Ultimately, this study outlines the potential of discrete, designable metal oxo clusters as catalysts for the selective modification of proteins through radical mechanisms under non-denaturing conditions.
PB  - Springer Nature
T2  - Nature Communications
T1  - Supplementary material for: Abdelhameed, S. A. M., de Azambuja, F., Vasović, T., Savić, N. D., Ćirković-Veličković, T.,& Parac-Vogt, T. N.. (2023). Regioselective protein oxidative cleavage enabled by enzyme-like recognition of an inorganic metal oxo cluster ligand. in Nature Communications Springer Nature., 14(1), 486. https://doi.org/10.1038/s41467-023-36085-z
VL  - 14
IS  - 1
SP  - 486
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5840
ER  - 

@misc{
author = "Abdelhameed, Shorok A. M. and de Azambuja, Francisco and Vasović, Tamara and Savić, Nada D. and Ćirković-Veličković, Tanja and Parac-Vogt, Tatjana N.",
year = "2023",
abstract = "Oxidative modifications of proteins are key to many applications in biotechnology. Metal-catalyzed oxidation reactions efficiently oxidize proteins but with low selectivity, and are highly dependent on the protein surface residues to direct the reaction. Herein, we demonstrate that discrete inorganic ligands such as polyoxometalates enable an efficient and selective protein oxidative cleavage. In the presence of ascorbate (1 mM), the Cu-substituted polyoxometalate K8[Cu2+(H2O)(α2-P2W17O61)], (CuIIWD, 0.05 mM) selectively cleave hen egg white lysozyme under physiological conditions (pH =7.5, 37 °C) producing only four bands in the gel electropherogram (12.7, 11, 10, and 5 kDa). Liquid chromatography/mass spectrometry analysis reveals a regioselective cleavage in the vicinity of crystallographic CuIIWD/lysozyme interaction sites. Mechanistically, polyoxometalate is critical to position the Cu at the protein surface and limit the generation of oxidative species to the proximity of binding sites. Ultimately, this study outlines the potential of discrete, designable metal oxo clusters as catalysts for the selective modification of proteins through radical mechanisms under non-denaturing conditions.",
publisher = "Springer Nature",
journal = "Nature Communications",
title = "Supplementary material for: Abdelhameed, S. A. M., de Azambuja, F., Vasović, T., Savić, N. D., Ćirković-Veličković, T.,& Parac-Vogt, T. N.. (2023). Regioselective protein oxidative cleavage enabled by enzyme-like recognition of an inorganic metal oxo cluster ligand. in Nature Communications Springer Nature., 14(1), 486. https://doi.org/10.1038/s41467-023-36085-z",
volume = "14",
number = "1",
pages = "486",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5840"
}

Abdelhameed, S. A. M., de Azambuja, F., Vasović, T., Savić, N. D., Ćirković-Veličković, T.,& Parac-Vogt, T. N.. (2023). Supplementary material for: Abdelhameed, S. A. M., de Azambuja, F., Vasović, T., Savić, N. D., Ćirković-Veličković, T.,& Parac-Vogt, T. N.. (2023). Regioselective protein oxidative cleavage enabled by enzyme-like recognition of an inorganic metal oxo cluster ligand. in Nature Communications Springer Nature., 14(1), 486. https://doi.org/10.1038/s41467-023-36085-z. in Nature Communications
Springer Nature., 14(1), 486.
https://hdl.handle.net/21.15107/rcub_cherry_5840

Abdelhameed SAM, de Azambuja F, Vasović T, Savić ND, Ćirković-Veličković T, Parac-Vogt TN. Supplementary material for: Abdelhameed, S. A. M., de Azambuja, F., Vasović, T., Savić, N. D., Ćirković-Veličković, T.,& Parac-Vogt, T. N.. (2023). Regioselective protein oxidative cleavage enabled by enzyme-like recognition of an inorganic metal oxo cluster ligand. in Nature Communications Springer Nature., 14(1), 486. https://doi.org/10.1038/s41467-023-36085-z. in Nature Communications. 2023;14(1):486.
https://hdl.handle.net/21.15107/rcub_cherry_5840 .

Abdelhameed, Shorok A. M., de Azambuja, Francisco, Vasović, Tamara, Savić, Nada D., Ćirković-Veličković, Tanja, Parac-Vogt, Tatjana N., "Supplementary material for: Abdelhameed, S. A. M., de Azambuja, F., Vasović, T., Savić, N. D., Ćirković-Veličković, T.,& Parac-Vogt, T. N.. (2023). Regioselective protein oxidative cleavage enabled by enzyme-like recognition of an inorganic metal oxo cluster ligand. in Nature Communications Springer Nature., 14(1), 486. https://doi.org/10.1038/s41467-023-36085-z" in Nature Communications, 14, no. 1 (2023):486,
https://hdl.handle.net/21.15107/rcub_cherry_5840 .

TY  - JOUR
AU  - Khulal, Urmila
AU  - Stojadinović, Marija M.
AU  - Prodić, Ivana
AU  - Rajković, Andrea
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5765
AB  - The digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.
PB  - Elsevier
T2  - Food Chemistry
T1  - Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix
VL  - 405
SP  - 134981
DO  - 10.1016/j.foodchem.2022.134981
ER  - 

@article{
author = "Khulal, Urmila and Stojadinović, Marija M. and Prodić, Ivana and Rajković, Andrea and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "The digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix",
volume = "405",
pages = "134981",
doi = "10.1016/j.foodchem.2022.134981"
}

Khulal, U., Stojadinović, M. M., Prodić, I., Rajković, A.,& Ćirković-Veličković, T.. (2023). Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry
Elsevier., 405, 134981.
https://doi.org/10.1016/j.foodchem.2022.134981

Khulal U, Stojadinović MM, Prodić I, Rajković A, Ćirković-Veličković T. Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry. 2023;405:134981.
doi:10.1016/j.foodchem.2022.134981 .

Khulal, Urmila, Stojadinović, Marija M., Prodić, Ivana, Rajković, Andrea, Ćirković-Veličković, Tanja, "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix" in Food Chemistry, 405 (2023):134981,
https://doi.org/10.1016/j.foodchem.2022.134981 . .

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Radomirović, Mirjana Ž.
AU  - Simović, Ana
AU  - Radibratović, Milica
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4884
AB  - Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.
PB  - Bentham Science
T2  - Current Analytical Chemistry
T1  - Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk
VL  - 18
IS  - 3
SP  - 341
EP  - 359
DO  - 10.2174/1573411017666210108092338
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4884
ER  - 

@article{
author = "Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Radomirović, Mirjana Ž. and Simović, Ana and Radibratović, Milica and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.",
publisher = "Bentham Science",
journal = "Current Analytical Chemistry",
title = "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk",
volume = "18",
number = "3",
pages = "341-359",
doi = "10.2174/1573411017666210108092338",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4884"
}

Stanić-Vučinić, D., Stojadinović, M. M., Radomirović, M. Ž., Simović, A., Radibratović, M.,& Ćirković-Veličković, T.. (2022). Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry
Bentham Science., 18(3), 341-359.
https://doi.org/10.2174/1573411017666210108092338
https://hdl.handle.net/21.15107/rcub_cherry_4884

Stanić-Vučinić D, Stojadinović MM, Radomirović MŽ, Simović A, Radibratović M, Ćirković-Veličković T. Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry. 2022;18(3):341-359.
doi:10.2174/1573411017666210108092338
https://hdl.handle.net/21.15107/rcub_cherry_4884 .

Stanić-Vučinić, Dragana, Stojadinović, Marija M., Radomirović, Mirjana Ž., Simović, Ana, Radibratović, Milica, Ćirković-Veličković, Tanja, "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk" in Current Analytical Chemistry, 18, no. 3 (2022):341-359,
https://doi.org/10.2174/1573411017666210108092338 .,
https://hdl.handle.net/21.15107/rcub_cherry_4884 .

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Radomirović, Mirjana Ž.
AU  - Simović, Ana
AU  - Radibratović, Milica
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4883
AB  - Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.
PB  - Bentham Science
T2  - Current Analytical Chemistry
T1  - Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk
VL  - 18
IS  - 3
SP  - 341
EP  - 359
DO  - 10.2174/1573411017666210108092338
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4883
ER  - 

@article{
author = "Radosavljević, Jelena and Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Radomirović, Mirjana Ž. and Simović, Ana and Radibratović, Milica and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.",
publisher = "Bentham Science",
journal = "Current Analytical Chemistry",
title = "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk",
volume = "18",
number = "3",
pages = "341-359",
doi = "10.2174/1573411017666210108092338",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4883"
}

Radosavljević, J., Stanić-Vučinić, D., Stojadinović, M. M., Radomirović, M. Ž., Simović, A., Radibratović, M.,& Ćirković-Veličković, T.. (2022). Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry
Bentham Science., 18(3), 341-359.
https://doi.org/10.2174/1573411017666210108092338
https://hdl.handle.net/21.15107/rcub_cherry_4883

Radosavljević J, Stanić-Vučinić D, Stojadinović MM, Radomirović MŽ, Simović A, Radibratović M, Ćirković-Veličković T. Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry. 2022;18(3):341-359.
doi:10.2174/1573411017666210108092338
https://hdl.handle.net/21.15107/rcub_cherry_4883 .

Radosavljević, Jelena, Stanić-Vučinić, Dragana, Stojadinović, Marija M., Radomirović, Mirjana Ž., Simović, Ana, Radibratović, Milica, Ćirković-Veličković, Tanja, "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk" in Current Analytical Chemistry, 18, no. 3 (2022):341-359,
https://doi.org/10.2174/1573411017666210108092338 .,
https://hdl.handle.net/21.15107/rcub_cherry_4883 .

TY  - JOUR
AU  - Radomirović, Mirjana Ž.
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Van Haute, Sam
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4863
AB  - β-lactoglobulin (BLG) is a major whey protein with numerous techno-functional properties desirable for the food industry. Phycocyanobilin (PCB), a bioactive pigment of Arthrospira platensis with health-promoting effects, covalently binds to BLG at physiological pH. This study investigated the effects of this covalent modification on BLG functional properties. The BLG–PCB adduct possesses enhanced antioxidant properties, and bound PCB protects BLG against free radical-induced oxidation. Despite the similar thermal stabilities of BLG and BLG–PCB, BLG–PCB is less susceptible to covalent and noncovalent aggregation under moderate heat treatment (63 °C, 30 min). Blocked thiol group and reduced hydrophobicity due to hindering of hydrophobic residues by bound PCB, as well as the heat-induced transition of β-sheet to α-helix, contributed to the low susceptibility of BLG–PCB to aggregation. BLG–PCB has a higher resistance to pepsin and pancreatin digestion than BLG and unaltered IgE-binding properties. The improved functional properties of BLG–PCB make it a useful ingredient in the food industry.
PB  - Elsevier
T2  - Food Hydrocolloids
T1  - Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating
VL  - 123
SP  - 107169
DO  - 10.1016/j.foodhyd.2021.107169
ER  - 

@article{
author = "Radomirović, Mirjana Ž. and Minić, Simeon L. and Stanić-Vučinić, Dragana and Nikolić, Milan and Van Haute, Sam and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "β-lactoglobulin (BLG) is a major whey protein with numerous techno-functional properties desirable for the food industry. Phycocyanobilin (PCB), a bioactive pigment of Arthrospira platensis with health-promoting effects, covalently binds to BLG at physiological pH. This study investigated the effects of this covalent modification on BLG functional properties. The BLG–PCB adduct possesses enhanced antioxidant properties, and bound PCB protects BLG against free radical-induced oxidation. Despite the similar thermal stabilities of BLG and BLG–PCB, BLG–PCB is less susceptible to covalent and noncovalent aggregation under moderate heat treatment (63 °C, 30 min). Blocked thiol group and reduced hydrophobicity due to hindering of hydrophobic residues by bound PCB, as well as the heat-induced transition of β-sheet to α-helix, contributed to the low susceptibility of BLG–PCB to aggregation. BLG–PCB has a higher resistance to pepsin and pancreatin digestion than BLG and unaltered IgE-binding properties. The improved functional properties of BLG–PCB make it a useful ingredient in the food industry.",
publisher = "Elsevier",
journal = "Food Hydrocolloids",
title = "Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating",
volume = "123",
pages = "107169",
doi = "10.1016/j.foodhyd.2021.107169"
}

Radomirović, M. Ž., Minić, S. L., Stanić-Vučinić, D., Nikolić, M., Van Haute, S., Rajković, A.,& Ćirković-Veličković, T.. (2022). Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating. in Food Hydrocolloids
Elsevier., 123, 107169.
https://doi.org/10.1016/j.foodhyd.2021.107169

Radomirović MŽ, Minić SL, Stanić-Vučinić D, Nikolić M, Van Haute S, Rajković A, Ćirković-Veličković T. Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating. in Food Hydrocolloids. 2022;123:107169.
doi:10.1016/j.foodhyd.2021.107169 .

Radomirović, Mirjana Ž., Minić, Simeon L., Stanić-Vučinić, Dragana, Nikolić, Milan, Van Haute, Sam, Rajković, Andreja, Ćirković-Veličković, Tanja, "Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating" in Food Hydrocolloids, 123 (2022):107169,
https://doi.org/10.1016/j.foodhyd.2021.107169 . .

TY  - JOUR
AU  - Benedé, Sara
AU  - Lozano-Ojalvo, Daniel
AU  - Cristobal, Susana
AU  - Costa, Joana
AU  - D’Auria, Enza
AU  - Ćirković-Veličković, Tanja
AU  - Garrido-Arandia, María
AU  - Karakaya, Sibel
AU  - Mafra, Isabel
AU  - Mazzucchelli, Gabriel
AU  - Picariello, Gianluca
AU  - Romero-Sahagun, Alejandro
AU  - Villa, Caterina
AU  - Roncada, Paola
AU  - Molina, Elena
PY  - 2022
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4548
AB  - Current approaches based on electrophoretic, chromatographic or immunochemical principles have allowed characterizing multiple allergens, mapping their epitopes, studying their mechanisms of action, developing detection and diagnostic methods and therapeutic strategies for the food and pharmaceutical industry. However, some of the common structural features related to the allergenic potential of food proteins remain unknown, or the pathological mechanism of food allergy is not yet fully understood. In addition, it is also necessary to evaluate new allergens from novel protein sources that may pose a new risk for consumers. Technological development has allowed the expansion of advanced technologies for which their whole potential has not been entirely exploited and could provide novel contributions to still unexplored molecular traits underlying both the structure of food allergens and the mechanisms through which they sensitize or elicit adverse responses in human subjects, as well as improving analytical techniques for their detection. This review presents cutting-edge instrumental techniques recently applied when studying structural and functional aspects of proteins, mechanism of action and interaction between biomolecules. We also exemplify their role in the food allergy research and discuss their new possible applications in several areas of the food allergy field.
PB  - Taylor & Francis Group
T2  - Critical Reviews in Food Science and Nutrition
T1  - New applications of advanced instrumental techniques for the characterization of food allergenic proteins
VL  - 62
IS  - 31
DO  - 10.1080/10408398.2021.1931806
ER  - 

@article{
author = "Benedé, Sara and Lozano-Ojalvo, Daniel and Cristobal, Susana and Costa, Joana and D’Auria, Enza and Ćirković-Veličković, Tanja and Garrido-Arandia, María and Karakaya, Sibel and Mafra, Isabel and Mazzucchelli, Gabriel and Picariello, Gianluca and Romero-Sahagun, Alejandro and Villa, Caterina and Roncada, Paola and Molina, Elena",
year = "2022",
abstract = "Current approaches based on electrophoretic, chromatographic or immunochemical principles have allowed characterizing multiple allergens, mapping their epitopes, studying their mechanisms of action, developing detection and diagnostic methods and therapeutic strategies for the food and pharmaceutical industry. However, some of the common structural features related to the allergenic potential of food proteins remain unknown, or the pathological mechanism of food allergy is not yet fully understood. In addition, it is also necessary to evaluate new allergens from novel protein sources that may pose a new risk for consumers. Technological development has allowed the expansion of advanced technologies for which their whole potential has not been entirely exploited and could provide novel contributions to still unexplored molecular traits underlying both the structure of food allergens and the mechanisms through which they sensitize or elicit adverse responses in human subjects, as well as improving analytical techniques for their detection. This review presents cutting-edge instrumental techniques recently applied when studying structural and functional aspects of proteins, mechanism of action and interaction between biomolecules. We also exemplify their role in the food allergy research and discuss their new possible applications in several areas of the food allergy field.",
publisher = "Taylor & Francis Group",
journal = "Critical Reviews in Food Science and Nutrition",
title = "New applications of advanced instrumental techniques for the characterization of food allergenic proteins",
volume = "62",
number = "31",
doi = "10.1080/10408398.2021.1931806"
}

Benedé, S., Lozano-Ojalvo, D., Cristobal, S., Costa, J., D’Auria, E., Ćirković-Veličković, T., Garrido-Arandia, M., Karakaya, S., Mafra, I., Mazzucchelli, G., Picariello, G., Romero-Sahagun, A., Villa, C., Roncada, P.,& Molina, E.. (2022). New applications of advanced instrumental techniques for the characterization of food allergenic proteins. in Critical Reviews in Food Science and Nutrition
Taylor & Francis Group., 62(31).
https://doi.org/10.1080/10408398.2021.1931806

Benedé S, Lozano-Ojalvo D, Cristobal S, Costa J, D’Auria E, Ćirković-Veličković T, Garrido-Arandia M, Karakaya S, Mafra I, Mazzucchelli G, Picariello G, Romero-Sahagun A, Villa C, Roncada P, Molina E. New applications of advanced instrumental techniques for the characterization of food allergenic proteins. in Critical Reviews in Food Science and Nutrition. 2022;62(31).
doi:10.1080/10408398.2021.1931806 .

Benedé, Sara, Lozano-Ojalvo, Daniel, Cristobal, Susana, Costa, Joana, D’Auria, Enza, Ćirković-Veličković, Tanja, Garrido-Arandia, María, Karakaya, Sibel, Mafra, Isabel, Mazzucchelli, Gabriel, Picariello, Gianluca, Romero-Sahagun, Alejandro, Villa, Caterina, Roncada, Paola, Molina, Elena, "New applications of advanced instrumental techniques for the characterization of food allergenic proteins" in Critical Reviews in Food Science and Nutrition, 62, no. 31 (2022),
https://doi.org/10.1080/10408398.2021.1931806 . .

TY  - CONF
AU  - Simović, Ana
AU  - Radomirović, Mirjana Ž.
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Minić, Simeon L.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5520
AB  - The emergence of the coronavirus SARS-CoV-2 has attracted attention of the whole scientific community. The SARS-CoV-2 spike (S) protein plays the most important role in viral attachment to host receptor angiotensin-converting enzyme 2 (ACE2), via the receptor-binding domain (RBD), fusion and entry into the host, and it serves as a target for the development of antibodies, entry inhibitors and vaccines. It has been demonstrated that phycocyanobilin (PCB), a bioactive open-chain tetrapyrrole chromophore of phycocyanin (PC), chromoprotein derived from the cyanobacterium Arthrospira platensis, can bind a plethora of different proteins, both in a noncovalent and covalent manner. This study aimed to investigate interactions of PCB with S protein and RBD respectively. Electrophoretic techniques, fluorescence spectroscopy, and inhibition of S–PCB and RBD–PCB covalent adduct formation using iodoacetamide and N-ethylmaleimide, were employed to examine interactions of PCB with S protein and RBD, while the effects of PCB binding on RBD structure were studied by CD spectroscopy. SDS-PAGE with Zn2+ staining has revealed that PCB covalently binds to both S protein and RBD, via free cysteine residues. Binding constants determined by the fluorescence quenching method were: 2.1×107 M–1 for PCB and S protein and 8.4×104 M–1 for PCB and RBD. Far-UV circular dichroism spectra showed that the binding of PCB influences RBD structure by decreasing the disordered structure content. Due to moderately strong noncovalent interactions of PCB with S protein and RBD, as well as covalent adducts formation, it may exert one of its many bioactive effects via impact on S protein binding to ACE2 receptor.
PB  - Faculty of Chemistry, Serbian Biochemical Society
C3  - Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia
T1  - Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain
SP  - 130
EP  - 131
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5520
ER  - 

@conference{
author = "Simović, Ana and Radomirović, Mirjana Ž. and Gligorijević, Nikola and Stanić-Vučinić, Dragana and Minić, Simeon L. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "The emergence of the coronavirus SARS-CoV-2 has attracted attention of the whole scientific community. The SARS-CoV-2 spike (S) protein plays the most important role in viral attachment to host receptor angiotensin-converting enzyme 2 (ACE2), via the receptor-binding domain (RBD), fusion and entry into the host, and it serves as a target for the development of antibodies, entry inhibitors and vaccines. It has been demonstrated that phycocyanobilin (PCB), a bioactive open-chain tetrapyrrole chromophore of phycocyanin (PC), chromoprotein derived from the cyanobacterium Arthrospira platensis, can bind a plethora of different proteins, both in a noncovalent and covalent manner. This study aimed to investigate interactions of PCB with S protein and RBD respectively. Electrophoretic techniques, fluorescence spectroscopy, and inhibition of S–PCB and RBD–PCB covalent adduct formation using iodoacetamide and N-ethylmaleimide, were employed to examine interactions of PCB with S protein and RBD, while the effects of PCB binding on RBD structure were studied by CD spectroscopy. SDS-PAGE with Zn2+ staining has revealed that PCB covalently binds to both S protein and RBD, via free cysteine residues. Binding constants determined by the fluorescence quenching method were: 2.1×107 M–1 for PCB and S protein and 8.4×104 M–1 for PCB and RBD. Far-UV circular dichroism spectra showed that the binding of PCB influences RBD structure by decreasing the disordered structure content. Due to moderately strong noncovalent interactions of PCB with S protein and RBD, as well as covalent adducts formation, it may exert one of its many bioactive effects via impact on S protein binding to ACE2 receptor.",
publisher = "Faculty of Chemistry, Serbian Biochemical Society",
journal = "Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia",
title = "Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain",
pages = "130-131",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5520"
}

Simović, A., Radomirović, M. Ž., Gligorijević, N., Stanić-Vučinić, D., Minić, S. L., Nikolić, M.,& Ćirković-Veličković, T.. (2022). Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain. in Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia
Faculty of Chemistry, Serbian Biochemical Society., 130-131.
https://hdl.handle.net/21.15107/rcub_cherry_5520

Simović A, Radomirović MŽ, Gligorijević N, Stanić-Vučinić D, Minić SL, Nikolić M, Ćirković-Veličković T. Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain. in Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia. 2022;:130-131.
https://hdl.handle.net/21.15107/rcub_cherry_5520 .

Simović, Ana, Radomirović, Mirjana Ž., Gligorijević, Nikola, Stanić-Vučinić, Dragana, Minić, Simeon L., Nikolić, Milan, Ćirković-Veličković, Tanja, "Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain" in Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia (2022):130-131,
https://hdl.handle.net/21.15107/rcub_cherry_5520 .

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  - CONF
AU  - Simović, Ana
AU  - Combet, Sophie
AU  - Ćirković-Veličković, Tanja
AU  - Nikolic, Milan
AU  - Minic, Simeon
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5133
AB  - The high content of vitamins, minerals, antioxidants, and proteins makes red algae Porphyra sp. (Nori) superfood with exceptional health-promoting benefits. Its intense colour originates from R-phycoerythrin (R-PE), phycobiliprotein containing covalently attached tetrapyrrole chromophores: red phycoerythrobilin and orange phycourobilin. The present study aims to characterize the stability of R-PE, a natural colourant with a high potential for application in the food, cosmetic, and pharmaceutical industries. We purified R-PE from dried Nori flakes with a high purity ratio (A560 /A280 ≥5). Far-UV CD spectroscopic showed that α-helix is the dominant secondary structure (75%). The thermal unfolding of α-helix revealed two transitions (Tm1 and Tm2 at 56 and 72°C, respectively), ascribed to the different subunits of R-PE. Absorption measurements showed that high pressure (HP) induces dissociation of R-PE into subunits followed by subunit unfolding. Contrary to temperature, HP treatment showed a significant advantage under applied conditions: the protein unfolding is partly reversible, and the R-PE colour bleaching is minimized. Based on the fluorescence quenching approach, R-PE's binding affinities for Cu2+ and Zn2+ ions were 6.27x105 and 1.71x103 M-1, respectively. Absorption and near-UV/VIS CD spectroscopy suggested conformational changes in protein chromophores upon metal ions binding. Far-UV CD spectroscopy did not reveal that metal binding affects R-PE structure. The obtained results give new insights into the stability of R-PE with a good use-value in replacement of toxic synthetic dyes, preservation of R-PE red colour in fortified food and beverages by HP processing, and as a biosensor for Cu2+ in aquatic life systems.
Acknowledgments: This study was financially supported by the Ministry of Education, Science and Technological Development of the Republic of Serbia, Contract number: 451-03-9/2021-14/200168 and the European Commission, under the Horizon2020, FoodEnTwin Project, GA No. 810752.
PB  - Sociedade Portuguesa de Química
C3  - Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference
T1  - Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes
SP  - 138
EP  - 138
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5133
ER  - 

@conference{
author = "Simović, Ana and Combet, Sophie and Ćirković-Veličković, Tanja and Nikolic, Milan and Minic, Simeon",
year = "2022",
abstract = "The high content of vitamins, minerals, antioxidants, and proteins makes red algae Porphyra sp. (Nori) superfood with exceptional health-promoting benefits. Its intense colour originates from R-phycoerythrin (R-PE), phycobiliprotein containing covalently attached tetrapyrrole chromophores: red phycoerythrobilin and orange phycourobilin. The present study aims to characterize the stability of R-PE, a natural colourant with a high potential for application in the food, cosmetic, and pharmaceutical industries. We purified R-PE from dried Nori flakes with a high purity ratio (A560 /A280 ≥5). Far-UV CD spectroscopic showed that α-helix is the dominant secondary structure (75%). The thermal unfolding of α-helix revealed two transitions (Tm1 and Tm2 at 56 and 72°C, respectively), ascribed to the different subunits of R-PE. Absorption measurements showed that high pressure (HP) induces dissociation of R-PE into subunits followed by subunit unfolding. Contrary to temperature, HP treatment showed a significant advantage under applied conditions: the protein unfolding is partly reversible, and the R-PE colour bleaching is minimized. Based on the fluorescence quenching approach, R-PE's binding affinities for Cu2+ and Zn2+ ions were 6.27x105 and 1.71x103 M-1, respectively. Absorption and near-UV/VIS CD spectroscopy suggested conformational changes in protein chromophores upon metal ions binding. Far-UV CD spectroscopy did not reveal that metal binding affects R-PE structure. The obtained results give new insights into the stability of R-PE with a good use-value in replacement of toxic synthetic dyes, preservation of R-PE red colour in fortified food and beverages by HP processing, and as a biosensor for Cu2+ in aquatic life systems.
Acknowledgments: This study was financially supported by the Ministry of Education, Science and Technological Development of the Republic of Serbia, Contract number: 451-03-9/2021-14/200168 and the European Commission, under the Horizon2020, FoodEnTwin Project, GA No. 810752.",
publisher = "Sociedade Portuguesa de Química",
journal = "Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference",
title = "Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes",
pages = "138-138",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5133"
}

Simović, A., Combet, S., Ćirković-Veličković, T., Nikolic, M.,& Minic, S.. (2022). Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes. in Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference
Sociedade Portuguesa de Química., 138-138.
https://hdl.handle.net/21.15107/rcub_cherry_5133

Simović A, Combet S, Ćirković-Veličković T, Nikolic M, Minic S. Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes. in Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference. 2022;:138-138.
https://hdl.handle.net/21.15107/rcub_cherry_5133 .

Simović, Ana, Combet, Sophie, Ćirković-Veličković, Tanja, Nikolic, Milan, Minic, Simeon, "Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes" in Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference (2022):138-138,
https://hdl.handle.net/21.15107/rcub_cherry_5133 .

TY  - JOUR
AU  - Trifunović, Sara
AU  - Smiljanić, Katarina
AU  - Sickmann, Albert
AU  - Solari, Fiorella Andrea
AU  - Kolarević, Stoimir
AU  - Divac Rankov, Aleksandra
AU  - Ljujic, Mila
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5458
AB  - Abstract
Background: Although still considered a safer alternative to classical cigarettes, growing body of work points to
harmful effects of electronic cigarettes (e-cigarettes) affecting a range of cellular processes. The biological effect of
e-cigarettes needs to be investigated in more detail considering their widespread use.
Methods: In this study, we treated V79 lung fibroblasts with sub-cytotoxic concentration of e-cigarette liquids, with
and without nicotine. Mutagenicity was evaluated by HPRT assay, genotoxicity by comet assay and the effect on cel-
lular communication by metabolic cooperation assay. Additionally, comprehensive proteome analysis was performed
via high resolution, parallel accumulation serial fragmentation-PASEF mass spectrometry.
Results: E-cigarette liquid concentration used in this study showed no mutagenic or genotoxic effect, however it
negatively impacted metabolic cooperation between V79 cells. Both e-cigarette liquids induced significant depletion
in total number of proteins and impairment of mitochondrial function in treated cells. The focal adhesion proteins
were upregulated, which is in accordance with the results of metabolic cooperation assay. Increased presence of post-
translational modifications (PTMs), including carbonylation and direct oxidative modifications, was observed. Data are
available via ProteomeXchange with identifier PXD032071.
Conclusions: Our study revealed impairment of metabolic cooperation as well as significant proteome and PTMs
alterations in V79 cells treated with e-cigarette liquid warranting future studies on e-cigarettes health impact.
PB  - BMC Springer Nature
T2  - Respiratory Research
T1  - Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells
VL  - 23
IS  - 191
DO  - 10.1186/s12931-022-02102-w
ER  - 

@article{
author = "Trifunović, Sara and Smiljanić, Katarina and Sickmann, Albert and Solari, Fiorella Andrea and Kolarević, Stoimir and Divac Rankov, Aleksandra and Ljujic, Mila",
year = "2022",
abstract = "Abstract
Background: Although still considered a safer alternative to classical cigarettes, growing body of work points to
harmful effects of electronic cigarettes (e-cigarettes) affecting a range of cellular processes. The biological effect of
e-cigarettes needs to be investigated in more detail considering their widespread use.
Methods: In this study, we treated V79 lung fibroblasts with sub-cytotoxic concentration of e-cigarette liquids, with
and without nicotine. Mutagenicity was evaluated by HPRT assay, genotoxicity by comet assay and the effect on cel-
lular communication by metabolic cooperation assay. Additionally, comprehensive proteome analysis was performed
via high resolution, parallel accumulation serial fragmentation-PASEF mass spectrometry.
Results: E-cigarette liquid concentration used in this study showed no mutagenic or genotoxic effect, however it
negatively impacted metabolic cooperation between V79 cells. Both e-cigarette liquids induced significant depletion
in total number of proteins and impairment of mitochondrial function in treated cells. The focal adhesion proteins
were upregulated, which is in accordance with the results of metabolic cooperation assay. Increased presence of post-
translational modifications (PTMs), including carbonylation and direct oxidative modifications, was observed. Data are
available via ProteomeXchange with identifier PXD032071.
Conclusions: Our study revealed impairment of metabolic cooperation as well as significant proteome and PTMs
alterations in V79 cells treated with e-cigarette liquid warranting future studies on e-cigarettes health impact.",
publisher = "BMC Springer Nature",
journal = "Respiratory Research",
title = "Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells",
volume = "23",
number = "191",
doi = "10.1186/s12931-022-02102-w"
}

Trifunović, S., Smiljanić, K., Sickmann, A., Solari, F. A., Kolarević, S., Divac Rankov, A.,& Ljujic, M.. (2022). Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells. in Respiratory Research
BMC Springer Nature., 23(191).
https://doi.org/10.1186/s12931-022-02102-w

Trifunović S, Smiljanić K, Sickmann A, Solari FA, Kolarević S, Divac Rankov A, Ljujic M. Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells. in Respiratory Research. 2022;23(191).
doi:10.1186/s12931-022-02102-w .

Trifunović, Sara, Smiljanić, Katarina, Sickmann, Albert, Solari, Fiorella Andrea, Kolarević, Stoimir, Divac Rankov, Aleksandra, Ljujic, Mila, "Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells" in Respiratory Research, 23, no. 191 (2022),
https://doi.org/10.1186/s12931-022-02102-w . .

TY  - CONF
AU  - Ljujic, Mila
AU  - Trifunović, Sara
AU  - Smiljanić, Katarina
AU  - Solari, Fiorella Andrea
AU  - Sickmann, Albert
AU  - Divac Rankov, Aleksandra
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5731
AB  - The COVID-19 pandemic caused by the SARS-CoV2 virus poses a global health threat with over 5 million deaths recorded. There is little understanding regarding SARS-CoV2 pathogenesis in the human airways and disease severity increases with age. Neutrophils are white blood cells found in large numbers in the airways of the lungs in severe COVID-19 patients. It is not known whether this influx of neutrophils into the airway has a protective or detrimental effect. We aim to understand the role of neutrophils during COVID-19 pathology, using an experimental infection model of the airway epithelium from the eldelry and children. To do this, we collect nasal airway cells from healthy elderly and children and grow them at air-liquid interface. Once differentiation and ciliation of these cells is reached, we infect the cells with SARS-CoV2 virus and allow neutrophils to migrate from the basolateral (blood) to the apical (air) side of the epithelium, similar to a physiological airway. Using flow cytometric analyses, we measure the expression of activation markers and the number of neutrophils that migrate across the epithelium of different ages in response to SARS-CoV2 infection. Preliminary work shows less viable neutrophils recovered from the elderly epithelium, more activated neutrophils when migrating through the elderly epithelium, as well as increased numbers of neutrophils remaining on the basolateral (blood) side of the elderly epithelium. These findings point to an inflammatory neutrophil phenotype influenced by the damaged elderly epithelium and supports the hypothesis that neutrophils are responsible for the severity of disease.
PB  - European Respiraotory Society (ERS)
C3  - European Respiratory Journal
T1  - Electronic cigarette liquids impair protein synthesis and alter proteomic profiles in V79 cells
VL  - 60
IS  - 66
SP  - 506
DO  - 10.1183/13993003.congress-2022.506
ER  - 

@conference{
author = "Ljujic, Mila and Trifunović, Sara and Smiljanić, Katarina and Solari, Fiorella Andrea and Sickmann, Albert and Divac Rankov, Aleksandra",
year = "2022",
abstract = "The COVID-19 pandemic caused by the SARS-CoV2 virus poses a global health threat with over 5 million deaths recorded. There is little understanding regarding SARS-CoV2 pathogenesis in the human airways and disease severity increases with age. Neutrophils are white blood cells found in large numbers in the airways of the lungs in severe COVID-19 patients. It is not known whether this influx of neutrophils into the airway has a protective or detrimental effect. We aim to understand the role of neutrophils during COVID-19 pathology, using an experimental infection model of the airway epithelium from the eldelry and children. To do this, we collect nasal airway cells from healthy elderly and children and grow them at air-liquid interface. Once differentiation and ciliation of these cells is reached, we infect the cells with SARS-CoV2 virus and allow neutrophils to migrate from the basolateral (blood) to the apical (air) side of the epithelium, similar to a physiological airway. Using flow cytometric analyses, we measure the expression of activation markers and the number of neutrophils that migrate across the epithelium of different ages in response to SARS-CoV2 infection. Preliminary work shows less viable neutrophils recovered from the elderly epithelium, more activated neutrophils when migrating through the elderly epithelium, as well as increased numbers of neutrophils remaining on the basolateral (blood) side of the elderly epithelium. These findings point to an inflammatory neutrophil phenotype influenced by the damaged elderly epithelium and supports the hypothesis that neutrophils are responsible for the severity of disease.",
publisher = "European Respiraotory Society (ERS)",
journal = "European Respiratory Journal",
title = "Electronic cigarette liquids impair protein synthesis and alter proteomic profiles in V79 cells",
volume = "60",
number = "66",
pages = "506",
doi = "10.1183/13993003.congress-2022.506"
}

Ljujic, M., Trifunović, S., Smiljanić, K., Solari, F. A., Sickmann, A.,& Divac Rankov, A.. (2022). Electronic cigarette liquids impair protein synthesis and alter proteomic profiles in V79 cells. in European Respiratory Journal
European Respiraotory Society (ERS)., 60(66), 506.
https://doi.org/10.1183/13993003.congress-2022.506

Ljujic M, Trifunović S, Smiljanić K, Solari FA, Sickmann A, Divac Rankov A. Electronic cigarette liquids impair protein synthesis and alter proteomic profiles in V79 cells. in European Respiratory Journal. 2022;60(66):506.
doi:10.1183/13993003.congress-2022.506 .

Ljujic, Mila, Trifunović, Sara, Smiljanić, Katarina, Solari, Fiorella Andrea, Sickmann, Albert, Divac Rankov, Aleksandra, "Electronic cigarette liquids impair protein synthesis and alter proteomic profiles in V79 cells" in European Respiratory Journal, 60, no. 66 (2022):506,
https://doi.org/10.1183/13993003.congress-2022.506 . .

TY  - THES
AU  - Bajkanović, Dragana
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5469
AB  - Cilj ovog rada je bio ispitati regioselektivnost Zr-Wells-Dawson 1:2 polioksometalata (Zr-WD 1:2) na β-laktoglobulinu (BLG) kao model proteinu. Literaturni podaci ukazuju na selektivnost ka kiselim aminokiselinama, kao što su aspartat i glutamat. Kako bismo dobili što pouzdanije rezultate u radu su korišteni nativni BLG (smjesa A i B izoforme), redukovan i alkilovan BLG i pojedinačne izoforme A i B. Rezultati dobijeni reakcijom sa Zr-WD 1:2 ukazuju da dolazi do hidrolize i da je elektroforetski profil različit za sve ispitivane tipove BLG. Zbog uslova reakcije (7 dana na 60 °C) dolazi i do autolize tako da krajnji efekat jeste kombinovani efekat autolize i dejstva Zr-WD 1:2. Bitno za naglasiti jeste to da nakon 24 časa na elektroforetskim profilma se javljaju proizvodi hidrolize, dok autoliza izostaje. Takođe, rezultati su pokazali da Zr-WD 1:2 ne ispoljava isključivu selektivnost ka kiselim aminokiselinama (aspartatu i glutamatu) već dolazi do hidrolize i na drugim aminokiselinama što nije u skladu sa literaturnim podacima u uzorku redukovanog i alkilovanog BLG.
T1  - Ispitivanje regioselektivnosti Zr-Wells-Dawson 1:2 polioksometalata na β-laktoglobulinu kao model proteinu
SP  - 1
EP  - 67
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5469
ER  - 

@mastersthesis{
author = "Bajkanović, Dragana",
year = "2022",
abstract = "Cilj ovog rada je bio ispitati regioselektivnost Zr-Wells-Dawson 1:2 polioksometalata (Zr-WD 1:2) na β-laktoglobulinu (BLG) kao model proteinu. Literaturni podaci ukazuju na selektivnost ka kiselim aminokiselinama, kao što su aspartat i glutamat. Kako bismo dobili što pouzdanije rezultate u radu su korišteni nativni BLG (smjesa A i B izoforme), redukovan i alkilovan BLG i pojedinačne izoforme A i B. Rezultati dobijeni reakcijom sa Zr-WD 1:2 ukazuju da dolazi do hidrolize i da je elektroforetski profil različit za sve ispitivane tipove BLG. Zbog uslova reakcije (7 dana na 60 °C) dolazi i do autolize tako da krajnji efekat jeste kombinovani efekat autolize i dejstva Zr-WD 1:2. Bitno za naglasiti jeste to da nakon 24 časa na elektroforetskim profilma se javljaju proizvodi hidrolize, dok autoliza izostaje. Takođe, rezultati su pokazali da Zr-WD 1:2 ne ispoljava isključivu selektivnost ka kiselim aminokiselinama (aspartatu i glutamatu) već dolazi do hidrolize i na drugim aminokiselinama što nije u skladu sa literaturnim podacima u uzorku redukovanog i alkilovanog BLG.",
title = "Ispitivanje regioselektivnosti Zr-Wells-Dawson 1:2 polioksometalata na β-laktoglobulinu kao model proteinu",
pages = "1-67",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5469"
}

Bajkanović, D.. (2022). Ispitivanje regioselektivnosti Zr-Wells-Dawson 1:2 polioksometalata na β-laktoglobulinu kao model proteinu. , 1-67.
https://hdl.handle.net/21.15107/rcub_cherry_5469

Bajkanović D. Ispitivanje regioselektivnosti Zr-Wells-Dawson 1:2 polioksometalata na β-laktoglobulinu kao model proteinu. 2022;:1-67.
https://hdl.handle.net/21.15107/rcub_cherry_5469 .

Bajkanović, Dragana, "Ispitivanje regioselektivnosti Zr-Wells-Dawson 1:2 polioksometalata na β-laktoglobulinu kao model proteinu" (2022):1-67,
https://hdl.handle.net/21.15107/rcub_cherry_5469 .

TY  - JOUR
AU  - Ristivojević, Petar
AU  - Jovanović, Vesna B.
AU  - Milojković-Opsenica, Dušanka
AU  - Park, Jihae
AU  - Rollinger, Judith M.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4844
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4864
AB  - Brown seaweeds are traditionally used as food in Asian countries, and they are a valuable source of bioactive compounds. Herein, a novel high-throughput methodological approach was developed for the tracing of compounds with radical scavenging and antimicrobial activities in Saccharina japonica and Undaria pinnatifida methanol extracts. The seaweed metabolites were separated by a novel high-performance thin-layer chromatography method, the bioactive bands were identified by bioautography assays. The bioactive compounds were characterized with ultra-high-performance liquid chromatography coupled with linear trap quadrupole tandem mass spectrometry. Stearidonic, eicosapentaenoic, and arachidonic acids were identified as major components having radical scavenging and antimicrobial activities. The suggested method provides a fast identification and quantification of bioactive compounds in multicomponent biological samples.
PB  - Elsevier
T2  - Food Chemistry
T1  - Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds
VL  - 334
SP  - 127562
DO  - 10.1016/j.foodchem.2020.127562
ER  - 

@article{
author = "Ristivojević, Petar and Jovanović, Vesna B. and Milojković-Opsenica, Dušanka and Park, Jihae and Rollinger, Judith M. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Brown seaweeds are traditionally used as food in Asian countries, and they are a valuable source of bioactive compounds. Herein, a novel high-throughput methodological approach was developed for the tracing of compounds with radical scavenging and antimicrobial activities in Saccharina japonica and Undaria pinnatifida methanol extracts. The seaweed metabolites were separated by a novel high-performance thin-layer chromatography method, the bioactive bands were identified by bioautography assays. The bioactive compounds were characterized with ultra-high-performance liquid chromatography coupled with linear trap quadrupole tandem mass spectrometry. Stearidonic, eicosapentaenoic, and arachidonic acids were identified as major components having radical scavenging and antimicrobial activities. The suggested method provides a fast identification and quantification of bioactive compounds in multicomponent biological samples.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds",
volume = "334",
pages = "127562",
doi = "10.1016/j.foodchem.2020.127562"
}

Ristivojević, P., Jovanović, V. B., Milojković-Opsenica, D., Park, J., Rollinger, J. M.,& Ćirković-Veličković, T.. (2021). Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds. in Food Chemistry
Elsevier., 334, 127562.
https://doi.org/10.1016/j.foodchem.2020.127562

Ristivojević P, Jovanović VB, Milojković-Opsenica D, Park J, Rollinger JM, Ćirković-Veličković T. Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds. in Food Chemistry. 2021;334:127562.
doi:10.1016/j.foodchem.2020.127562 .

Ristivojević, Petar, Jovanović, Vesna B., Milojković-Opsenica, Dušanka, Park, Jihae, Rollinger, Judith M., Ćirković-Veličković, Tanja, "Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds" in Food Chemistry, 334 (2021):127562,
https://doi.org/10.1016/j.foodchem.2020.127562 . .

TY  - JOUR
AU  - Ristivojević, Petar
AU  - Jovanović, Vesna B.
AU  - Milojković-Opsenica, Dušanka
AU  - Park, Jihae
AU  - Rollinger, Judith M.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4844
AB  - Brown seaweeds are traditionally used as food in Asian countries, and they are a valuable source of bioactive compounds. Herein, a novel high-throughput methodological approach was developed for the tracing of compounds with radical scavenging and antimicrobial activities in Saccharina japonica and Undaria pinnatifida methanol extracts. The seaweed metabolites were separated by a novel high-performance thin-layer chromatography method, the bioactive bands were identified by bioautography assays. The bioactive compounds were characterized with ultra-high-performance liquid chromatography coupled with linear trap quadrupole tandem mass spectrometry. Stearidonic, eicosapentaenoic, and arachidonic acids were identified as major components having radical scavenging and antimicrobial activities. The suggested method provides a fast identification and quantification of bioactive compounds in multicomponent biological samples.
PB  - Elsevier
T2  - Food Chemistry
T1  - Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds
VL  - 334
SP  - 127562
DO  - 10.1016/j.foodchem.2020.127562
ER  - 

@article{
author = "Ristivojević, Petar and Jovanović, Vesna B. and Milojković-Opsenica, Dušanka and Park, Jihae and Rollinger, Judith M. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Brown seaweeds are traditionally used as food in Asian countries, and they are a valuable source of bioactive compounds. Herein, a novel high-throughput methodological approach was developed for the tracing of compounds with radical scavenging and antimicrobial activities in Saccharina japonica and Undaria pinnatifida methanol extracts. The seaweed metabolites were separated by a novel high-performance thin-layer chromatography method, the bioactive bands were identified by bioautography assays. The bioactive compounds were characterized with ultra-high-performance liquid chromatography coupled with linear trap quadrupole tandem mass spectrometry. Stearidonic, eicosapentaenoic, and arachidonic acids were identified as major components having radical scavenging and antimicrobial activities. The suggested method provides a fast identification and quantification of bioactive compounds in multicomponent biological samples.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds",
volume = "334",
pages = "127562",
doi = "10.1016/j.foodchem.2020.127562"
}

Ristivojević, P., Jovanović, V. B., Milojković-Opsenica, D., Park, J., Rollinger, J. M.,& Ćirković-Veličković, T.. (2021). Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds. in Food Chemistry
Elsevier., 334, 127562.
https://doi.org/10.1016/j.foodchem.2020.127562

Ristivojević P, Jovanović VB, Milojković-Opsenica D, Park J, Rollinger JM, Ćirković-Veličković T. Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds. in Food Chemistry. 2021;334:127562.
doi:10.1016/j.foodchem.2020.127562 .

Ristivojević, Petar, Jovanović, Vesna B., Milojković-Opsenica, Dušanka, Park, Jihae, Rollinger, Judith M., Ćirković-Veličković, Tanja, "Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds" in Food Chemistry, 334 (2021):127562,
https://doi.org/10.1016/j.foodchem.2020.127562 . .

TY  - JOUR
AU  - Krstić-Ristivojević, Maja
AU  - Apostolović, Danijela
AU  - Smiljanić, Katarina
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4809
AB  - Food hypersensitivity reactions are adverse reactions to harmless dietary substances, whose causes are hidden within derangements of the complex immune machinery of humans and mammals. Until recently, enterocytes were considered as solely absorptive cells providing a physical barrier for unwanted lumen constituents. This review focuses on the enterocytes, which are the hub for innate and adaptive immune reactions. Furthermore, the ambiguous nature of enterocytes is also reflected in the fact that enterocytes can be considered as antigen-presenting cells since they constitutively express major histocompatibility complex (MHC) class II molecules. Taken together, it becomes clear that enterocytes have an immense role in maintaining oral tolerance to foreign antigens. In general, the immune system and its mechanisms underlying food hypersensitivity are still unknown and the involvement of components belonging to other anatomical systems, such as enterocytes, in these mechanisms make their elucidation even more difficult. The findings from studies with animal models provide us with valuable information about allergic mechanisms in the animal world, while on the other hand, these models are used to extrapolate results to the pathological conditions occurring in humans. There is a constant need for studies that deal with this topic and can overcome the glitches related to ethics in working with animals.
PB  - MDPI
T2  - Animals
T1  - Enterocytes in Food Hypersensitivity Reactions
VL  - 11
IS  - 9
SP  - 2713
DO  - 10.3390/ani11092713
ER  - 

@article{
author = "Krstić-Ristivojević, Maja and Apostolović, Danijela and Smiljanić, Katarina",
year = "2021",
abstract = "Food hypersensitivity reactions are adverse reactions to harmless dietary substances, whose causes are hidden within derangements of the complex immune machinery of humans and mammals. Until recently, enterocytes were considered as solely absorptive cells providing a physical barrier for unwanted lumen constituents. This review focuses on the enterocytes, which are the hub for innate and adaptive immune reactions. Furthermore, the ambiguous nature of enterocytes is also reflected in the fact that enterocytes can be considered as antigen-presenting cells since they constitutively express major histocompatibility complex (MHC) class II molecules. Taken together, it becomes clear that enterocytes have an immense role in maintaining oral tolerance to foreign antigens. In general, the immune system and its mechanisms underlying food hypersensitivity are still unknown and the involvement of components belonging to other anatomical systems, such as enterocytes, in these mechanisms make their elucidation even more difficult. The findings from studies with animal models provide us with valuable information about allergic mechanisms in the animal world, while on the other hand, these models are used to extrapolate results to the pathological conditions occurring in humans. There is a constant need for studies that deal with this topic and can overcome the glitches related to ethics in working with animals.",
publisher = "MDPI",
journal = "Animals",
title = "Enterocytes in Food Hypersensitivity Reactions",
volume = "11",
number = "9",
pages = "2713",
doi = "10.3390/ani11092713"
}

Krstić-Ristivojević, M., Apostolović, D.,& Smiljanić, K.. (2021). Enterocytes in Food Hypersensitivity Reactions. in Animals
MDPI., 11(9), 2713.
https://doi.org/10.3390/ani11092713

Krstić-Ristivojević M, Apostolović D, Smiljanić K. Enterocytes in Food Hypersensitivity Reactions. in Animals. 2021;11(9):2713.
doi:10.3390/ani11092713 .

Krstić-Ristivojević, Maja, Apostolović, Danijela, Smiljanić, Katarina, "Enterocytes in Food Hypersensitivity Reactions" in Animals, 11, no. 9 (2021):2713,
https://doi.org/10.3390/ani11092713 . .

TY  - JOUR
AU  - Peruško, Marija
AU  - Apostolović, Danijela
AU  - Kiewiet, Mensiena Berentje Geertje
AU  - Grundström, Jeanette
AU  - Hamsten, Carl
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - Hage, Marianne van
PY  - 2021
UR  - https://onlinelibrary.wiley.com/doi/abs/10.1111/all.14889
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4446
AB  - Background Mammalian meat is the most common trigger of the allergic reactions in patients with α-Gal syndrome (AGS). Milk and dairy, although less often, also cause a significant number of allergic manifestations. The aim of this study was to identify α-Gal-containing bovine milk proteins with allergenic properties among AGS patients. Methods Thirty-eight AGS patients with IgE to milk were included in the study. Milk proteins were analyzed for the presence of α-Gal and for binding by patients’ IgE using immunoblot, ImmunoCAP, and inhibition ELISA. Allergenicity of milk and milk proteins was assessed by basophil activation test. Results More than half of the AGS patients reported allergic reactions to milk or dairy products. Bovine γ-globulin (BGG), lactoferrin (LF), and lactoperoxidase (LPO) were identified as α-Gal carrying proteins which were recognized by AGS patients’ IgE. Whey mirrored the anti-α-Gal and IgE reactivity of BGG, LF, and LPO. Eighty-nine percent of the patients displayed IgE to BGG, 91% to LF, and 57% to LPO. Inhibition of α-Gal-specific IgE binding was achieved by BGG, LF, LPO, and whey. These proteins also activated AGS patients’ basophils. Interestingly, at lower concentrations, LF was the most potent inhibitor of IgE binding, and the most potent activator of basophils. Conclusion BGG, LF, and LPO were all found to be relevant milk α-Gal-containing glycoproteins that bound AGS patients’ IgE antibodies and activated their basophils. These proteins are probably involved in the allergic reactions to milk in AGS patients. LPO was for the first time shown to be an allergen.
PB  - Wiley
T2  - Allergy
T2  - Allergy
T1  - Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome
VL  - 76
IS  - 12
SP  - 3766
EP  - 3775
DO  - 10.1111/all.14889
ER  - 

@article{
author = "Peruško, Marija and Apostolović, Danijela and Kiewiet, Mensiena Berentje Geertje and Grundström, Jeanette and Hamsten, Carl and Starkhammar, Maria and Ćirković-Veličković, Tanja and Hage, Marianne van",
year = "2021",
abstract = "Background Mammalian meat is the most common trigger of the allergic reactions in patients with α-Gal syndrome (AGS). Milk and dairy, although less often, also cause a significant number of allergic manifestations. The aim of this study was to identify α-Gal-containing bovine milk proteins with allergenic properties among AGS patients. Methods Thirty-eight AGS patients with IgE to milk were included in the study. Milk proteins were analyzed for the presence of α-Gal and for binding by patients’ IgE using immunoblot, ImmunoCAP, and inhibition ELISA. Allergenicity of milk and milk proteins was assessed by basophil activation test. Results More than half of the AGS patients reported allergic reactions to milk or dairy products. Bovine γ-globulin (BGG), lactoferrin (LF), and lactoperoxidase (LPO) were identified as α-Gal carrying proteins which were recognized by AGS patients’ IgE. Whey mirrored the anti-α-Gal and IgE reactivity of BGG, LF, and LPO. Eighty-nine percent of the patients displayed IgE to BGG, 91% to LF, and 57% to LPO. Inhibition of α-Gal-specific IgE binding was achieved by BGG, LF, LPO, and whey. These proteins also activated AGS patients’ basophils. Interestingly, at lower concentrations, LF was the most potent inhibitor of IgE binding, and the most potent activator of basophils. Conclusion BGG, LF, and LPO were all found to be relevant milk α-Gal-containing glycoproteins that bound AGS patients’ IgE antibodies and activated their basophils. These proteins are probably involved in the allergic reactions to milk in AGS patients. LPO was for the first time shown to be an allergen.",
publisher = "Wiley",
journal = "Allergy, Allergy",
title = "Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome",
volume = "76",
number = "12",
pages = "3766-3775",
doi = "10.1111/all.14889"
}

Peruško, M., Apostolović, D., Kiewiet, M. B. G., Grundström, J., Hamsten, C., Starkhammar, M., Ćirković-Veličković, T.,& Hage, M. v.. (2021). Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome. in Allergy
Wiley., 76(12), 3766-3775.
https://doi.org/10.1111/all.14889

Peruško M, Apostolović D, Kiewiet MBG, Grundström J, Hamsten C, Starkhammar M, Ćirković-Veličković T, Hage MV. Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome. in Allergy. 2021;76(12):3766-3775.
doi:10.1111/all.14889 .

Peruško, Marija, Apostolović, Danijela, Kiewiet, Mensiena Berentje Geertje, Grundström, Jeanette, Hamsten, Carl, Starkhammar, Maria, Ćirković-Veličković, Tanja, Hage, Marianne van, "Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome" in Allergy, 76, no. 12 (2021):3766-3775,
https://doi.org/10.1111/all.14889 . .

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Grundström, Jeanette
AU  - Peruško, Marija
AU  - Kiewiet, M. B. Gea
AU  - Hamsten, Carl
AU  - Starkhammar, Maria
AU  - van Hage, Marianne
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4839
PB  - Wiley
T2  - Clinical and Translational Allergy
T2  - Clinical and Translational AllergyClin Transl Allergy
T1  - Course of IgE to α-Gal in a Swedish population of α-Gal syndrome patients
VL  - 11
IS  - 10
SP  - e12087
DO  - 10.1002/clt2.12087
ER  - 

@article{
author = "Apostolović, Danijela and Grundström, Jeanette and Peruško, Marija and Kiewiet, M. B. Gea and Hamsten, Carl and Starkhammar, Maria and van Hage, Marianne",
year = "2021",
publisher = "Wiley",
journal = "Clinical and Translational Allergy, Clinical and Translational AllergyClin Transl Allergy",
title = "Course of IgE to α-Gal in a Swedish population of α-Gal syndrome patients",
volume = "11",
number = "10",
pages = "e12087",
doi = "10.1002/clt2.12087"
}

Apostolović, D., Grundström, J., Peruško, M., Kiewiet, M. B. G., Hamsten, C., Starkhammar, M.,& van Hage, M.. (2021). Course of IgE to α-Gal in a Swedish population of α-Gal syndrome patients. in Clinical and Translational Allergy
Wiley., 11(10), e12087.
https://doi.org/10.1002/clt2.12087

Apostolović D, Grundström J, Peruško M, Kiewiet MBG, Hamsten C, Starkhammar M, van Hage M. Course of IgE to α-Gal in a Swedish population of α-Gal syndrome patients. in Clinical and Translational Allergy. 2021;11(10):e12087.
doi:10.1002/clt2.12087 .

Apostolović, Danijela, Grundström, Jeanette, Peruško, Marija, Kiewiet, M. B. Gea, Hamsten, Carl, Starkhammar, Maria, van Hage, Marianne, "Course of IgE to α-Gal in a Swedish population of α-Gal syndrome patients" in Clinical and Translational Allergy, 11, no. 10 (2021):e12087,
https://doi.org/10.1002/clt2.12087 . .

TY  - JOUR
AU  - Nikkhah, Amin
AU  - Van Haute, Sam
AU  - Jovanović, Vesna B.
AU  - Jung, Heejung
AU  - Dewulf, Jo
AU  - Ćirković-Veličković, Tanja
AU  - Ghnimi, Sami
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4586
AB  - In the original version of this Article, Sam Van Haute and Sami Ghnimi were omitted as corresponding authors.
Correspondence and requests for materials should also be addressed to sam.vanhaute@ghent.ac.kr and sghnimi@
isara.fr.
The original Article has been corrected.
PB  - Springer Nature
T2  - Scientific Reports
T1  - Correction to:  Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source (Sci Rep 2021, 11 (1), 14030. DOI: https://doi.org/10.1038/s41598-021-93284-8)
VL  - 11
IS  - 1
SP  - 14030
DO  - 10.1038/s41598-021-97513-y
ER  - 

@article{
author = "Nikkhah, Amin and Van Haute, Sam and Jovanović, Vesna B. and Jung, Heejung and Dewulf, Jo and Ćirković-Veličković, Tanja and Ghnimi, Sami",
year = "2021",
abstract = "In the original version of this Article, Sam Van Haute and Sami Ghnimi were omitted as corresponding authors.
Correspondence and requests for materials should also be addressed to sam.vanhaute@ghent.ac.kr and sghnimi@
isara.fr.
The original Article has been corrected.",
publisher = "Springer Nature",
journal = "Scientific Reports",
title = "Correction to:  Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source (Sci Rep 2021, 11 (1), 14030. DOI: https://doi.org/10.1038/s41598-021-93284-8)",
volume = "11",
number = "1",
pages = "14030",
doi = "10.1038/s41598-021-97513-y"
}

Nikkhah, A., Van Haute, S., Jovanović, V. B., Jung, H., Dewulf, J., Ćirković-Veličković, T.,& Ghnimi, S.. (2021). Correction to:  Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source (Sci Rep 2021, 11 (1), 14030. DOI: https://doi.org/10.1038/s41598-021-93284-8). in Scientific Reports
Springer Nature., 11(1), 14030.
https://doi.org/10.1038/s41598-021-97513-y

Nikkhah A, Van Haute S, Jovanović VB, Jung H, Dewulf J, Ćirković-Veličković T, Ghnimi S. Correction to:  Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source (Sci Rep 2021, 11 (1), 14030. DOI: https://doi.org/10.1038/s41598-021-93284-8). in Scientific Reports. 2021;11(1):14030.
doi:10.1038/s41598-021-97513-y .

Nikkhah, Amin, Van Haute, Sam, Jovanović, Vesna B., Jung, Heejung, Dewulf, Jo, Ćirković-Veličković, Tanja, Ghnimi, Sami, "Correction to:  Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source (Sci Rep 2021, 11 (1), 14030. DOI: https://doi.org/10.1038/s41598-021-93284-8)" in Scientific Reports, 11, no. 1 (2021):14030,
https://doi.org/10.1038/s41598-021-97513-y . .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6025
AB  - Food allergies affect up to 10% of the general population and represent an important health problem in the field of food safety in industrialized countries. Hence, developing reliable, specific, and sensitive methods for detecting and quantifying allergens in food products is of high importance. Shellfish have been recognized as one of the eight most common sources of allergens, with tropomyosin (TPM) being considered a major heat-stable allergen, having a highly conserved amino acid sequence among different shellfish species. Allergenicity of TPM may change during food processing, such as cooking. The objective of this study was to develop an enzyme-linked immunosorbent assay (ELISA) for the detection and quantification of shellfish tropomyosin in food samples. 
Two different extraction buffers - phosphate-buffered saline (PBS) and PBS containing 1 M sodium-chloride (PBSN), were compared for their ability to recover proteins from pre-cooked frozen Mediterranean mussel (Mytilus galloprovincialis) and fresh frozen razor mud shrimp (Solenocera melantho). The samples were additionally cooked according to the manufacturer's instruction and analyzed as such. The protein content was quantified using Bradford protein assay, and the protein components of soluble extracts were profiled using SDS-PAGE. TPM presence was confirmed using Western blot. Sandwich ELISA was developed using a monoclonal anti-TPM antibody as a capture antibody, while polyclonal anti-TPM antibody served as a detection antibody and was coupled to the biotinylated secondary antibody and streptavidin-alkaline phosphatase conjugate. Tropomyosin was quantified using highly purified natural shrimp tropomyosin as standard. 
The profile of extracted proteins was changed when using PBSN instead of PBS. A higher concentration of proteins was recovered from raw shrimp using PBSN instead of PBS. At the same time, the type of extraction buffer did not affect protein recovery either from heated shrimp or pre-cooked/heated mussels. Significantly fewer proteins were extracted from cooked shrimp sample compared to the raw shrimp, while cooking showed no effect on the extraction of proteins from mussels. Cooking did not affect TPM recognition in Western blot. TPM was quantified in shrimp samples in sandwich ELISA. However, developed ELISA could not quantify mussel's TPM, indicating that this approach may distinguish mussels and shrimp TPM.
PB  - Sociedade Portuguesa de Química, Av. Da República, 45 – 3º Esq, 1050-187 Lisboa – Portugal
C3  - XXI EuroFoodChem conference, Virtual Congress, 22nd-24th November, 2021. In: Book of Abstracts
T1  - Extraction and quantification of tropomyosin in selected samples of shellfish
SP  - 118
EP  - 118
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6025
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Gligorijević, Nikola and Stanić-Vučinić, Dragana and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Food allergies affect up to 10% of the general population and represent an important health problem in the field of food safety in industrialized countries. Hence, developing reliable, specific, and sensitive methods for detecting and quantifying allergens in food products is of high importance. Shellfish have been recognized as one of the eight most common sources of allergens, with tropomyosin (TPM) being considered a major heat-stable allergen, having a highly conserved amino acid sequence among different shellfish species. Allergenicity of TPM may change during food processing, such as cooking. The objective of this study was to develop an enzyme-linked immunosorbent assay (ELISA) for the detection and quantification of shellfish tropomyosin in food samples. 
Two different extraction buffers - phosphate-buffered saline (PBS) and PBS containing 1 M sodium-chloride (PBSN), were compared for their ability to recover proteins from pre-cooked frozen Mediterranean mussel (Mytilus galloprovincialis) and fresh frozen razor mud shrimp (Solenocera melantho). The samples were additionally cooked according to the manufacturer's instruction and analyzed as such. The protein content was quantified using Bradford protein assay, and the protein components of soluble extracts were profiled using SDS-PAGE. TPM presence was confirmed using Western blot. Sandwich ELISA was developed using a monoclonal anti-TPM antibody as a capture antibody, while polyclonal anti-TPM antibody served as a detection antibody and was coupled to the biotinylated secondary antibody and streptavidin-alkaline phosphatase conjugate. Tropomyosin was quantified using highly purified natural shrimp tropomyosin as standard. 
The profile of extracted proteins was changed when using PBSN instead of PBS. A higher concentration of proteins was recovered from raw shrimp using PBSN instead of PBS. At the same time, the type of extraction buffer did not affect protein recovery either from heated shrimp or pre-cooked/heated mussels. Significantly fewer proteins were extracted from cooked shrimp sample compared to the raw shrimp, while cooking showed no effect on the extraction of proteins from mussels. Cooking did not affect TPM recognition in Western blot. TPM was quantified in shrimp samples in sandwich ELISA. However, developed ELISA could not quantify mussel's TPM, indicating that this approach may distinguish mussels and shrimp TPM.",
publisher = "Sociedade Portuguesa de Química, Av. Da República, 45 – 3º Esq, 1050-187 Lisboa – Portugal",
journal = "XXI EuroFoodChem conference, Virtual Congress, 22nd-24th November, 2021. In: Book of Abstracts",
title = "Extraction and quantification of tropomyosin in selected samples of shellfish",
pages = "118-118",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6025"
}

Radomirović, M. Ž., Gligorijević, N., Stanić-Vučinić, D., Rajković, A.,& Ćirković-Veličković, T.. (2021). Extraction and quantification of tropomyosin in selected samples of shellfish. in XXI EuroFoodChem conference, Virtual Congress, 22nd-24th November, 2021. In: Book of Abstracts
Sociedade Portuguesa de Química, Av. Da República, 45 – 3º Esq, 1050-187 Lisboa – Portugal., 118-118.
https://hdl.handle.net/21.15107/rcub_cherry_6025

Radomirović MŽ, Gligorijević N, Stanić-Vučinić D, Rajković A, Ćirković-Veličković T. Extraction and quantification of tropomyosin in selected samples of shellfish. in XXI EuroFoodChem conference, Virtual Congress, 22nd-24th November, 2021. In: Book of Abstracts. 2021;:118-118.
https://hdl.handle.net/21.15107/rcub_cherry_6025 .

Radomirović, Mirjana Ž., Gligorijević, Nikola, Stanić-Vučinić, Dragana, Rajković, Andreja, Ćirković-Veličković, Tanja, "Extraction and quantification of tropomyosin in selected samples of shellfish" in XXI EuroFoodChem conference, Virtual Congress, 22nd-24th November, 2021. In: Book of Abstracts (2021):118-118,
https://hdl.handle.net/21.15107/rcub_cherry_6025 .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Nikolić, Milan
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6032
AB  - Phycobiliproteins (PBP) have been employed in numerous fluorescence-based techniques owing to highly fluorescent, covalently bound tetrapyrrole chromophores. So far, only entire PBPs have been utilized as fluorescent probes. A new method for covalent attachment of phycocyanin’s chromophore, phycocyanobilin (PCB), to potentially any protein, is proposed, relying on the ability of PCB to be attached to sulfhydryl groups of proteins. Traut’s reagent (TR, 2-iminothiolane) was exploited for introduction of sulfhydryl groups in the model protein, bovine serum albumin (BSA), by modifying its primary amines. Introduced sulfhydryl groups were then targeted for modification by PCB. All tested molar ratios of TR per mole of protein were successful in modification of BSA. Near-UV and far-UV circular dichroism spectroscopy revealed that a higher degree of modification by TR induces more profound alterations of BSA structure, leading at the same time to minor changes in BSA oligomerization and aggregation profile. PCB was covalently attached to introduced sulfhydryl groups at pH 9 at 20–fold ratio of TR. An increase in the molar ratio of TR per mole of BSA leads to amplification of fluorescent signal of PCB-modified BSA, most significantly observed starting from 50-fold and higher TR ratios. Using BSA as a model protein, a 50-fold molar excess of TR seems to be the optimal ratio for balancing between the effect on protein structure and the degree of labeling and thus fluorescent signal obtained. The proposed method could be used for labeling of virtually any protein, as means of either obtaining fluorescent probes for application in fluorescent techniques or functionalization of, for example, food proteins through covalent attachment of bioactive PCB.
PB  - Belgrade : Faculty of Chemistry
C3  - FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts
T1  - Traut’s reagent application in fluorescent labeling of bovine serum albumin with phycocyanobilin
SP  - 37
EP  - 37
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6032
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Gligorijević, Nikola and Minić, Simeon and Nikolić, Milan and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Phycobiliproteins (PBP) have been employed in numerous fluorescence-based techniques owing to highly fluorescent, covalently bound tetrapyrrole chromophores. So far, only entire PBPs have been utilized as fluorescent probes. A new method for covalent attachment of phycocyanin’s chromophore, phycocyanobilin (PCB), to potentially any protein, is proposed, relying on the ability of PCB to be attached to sulfhydryl groups of proteins. Traut’s reagent (TR, 2-iminothiolane) was exploited for introduction of sulfhydryl groups in the model protein, bovine serum albumin (BSA), by modifying its primary amines. Introduced sulfhydryl groups were then targeted for modification by PCB. All tested molar ratios of TR per mole of protein were successful in modification of BSA. Near-UV and far-UV circular dichroism spectroscopy revealed that a higher degree of modification by TR induces more profound alterations of BSA structure, leading at the same time to minor changes in BSA oligomerization and aggregation profile. PCB was covalently attached to introduced sulfhydryl groups at pH 9 at 20–fold ratio of TR. An increase in the molar ratio of TR per mole of BSA leads to amplification of fluorescent signal of PCB-modified BSA, most significantly observed starting from 50-fold and higher TR ratios. Using BSA as a model protein, a 50-fold molar excess of TR seems to be the optimal ratio for balancing between the effect on protein structure and the degree of labeling and thus fluorescent signal obtained. The proposed method could be used for labeling of virtually any protein, as means of either obtaining fluorescent probes for application in fluorescent techniques or functionalization of, for example, food proteins through covalent attachment of bioactive PCB.",
publisher = "Belgrade : Faculty of Chemistry",
journal = "FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts",
title = "Traut’s reagent application in fluorescent labeling of bovine serum albumin with phycocyanobilin",
pages = "37-37",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6032"
}

Radomirović, M. Ž., Gligorijević, N., Minić, S., Nikolić, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Traut’s reagent application in fluorescent labeling of bovine serum albumin with phycocyanobilin. in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts
Belgrade : Faculty of Chemistry., 37-37.
https://hdl.handle.net/21.15107/rcub_cherry_6032

Radomirović MŽ, Gligorijević N, Minić S, Nikolić M, Stanić-Vučinić D, Ćirković-Veličković T. Traut’s reagent application in fluorescent labeling of bovine serum albumin with phycocyanobilin. in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts. 2021;:37-37.
https://hdl.handle.net/21.15107/rcub_cherry_6032 .

Radomirović, Mirjana Ž., Gligorijević, Nikola, Minić, Simeon, Nikolić, Milan, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Traut’s reagent application in fluorescent labeling of bovine serum albumin with phycocyanobilin" in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts (2021):37-37,
https://hdl.handle.net/21.15107/rcub_cherry_6032 .

TY  - CONF
AU  - Gligorijević, Nikola
AU  - Radomirović, Mirjana Ž.
AU  - Rajković, Andreja
AU  - Nedić, Olgica
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6033
AB  - The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, only to be later discovered that the presence of several antioxidants, including resveratrol, are responsible for it. We investigated if resveratrol has a more direct role in protection from harmful oxidation and development of thrombosis, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetric analysis demonstrated binding of resveratrol to fibrinogen, the main protein in the coagulation process, which also has an important application as a food additive in making of fibrin gels. Various spectroscopic methods have demonstrated that binding of resveratrol does not unfold or destabilize fibrinogen since both near and far-UV CD spectra as well as its melting temperature remained unchanged. A mutually protective effect against the free radical-induced oxidation of resveratrol and fibrinogen was found. The presence of fibrinogen caused a very small masking effect of the antioxidative potential of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing potential bioavailability and activity of resveratrol in circulation. By direct interaction and protection of fibrinogen, resveratrol may serve as an important antioxidant for prevention of thrombosis. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.
C3  - FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021
T1  - Resveratrol and fibrinogen interactions
SP  - 15
EP  - 15
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6033
ER  - 

@conference{
author = "Gligorijević, Nikola and Radomirović, Mirjana Ž. and Rajković, Andreja and Nedić, Olgica and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, only to be later discovered that the presence of several antioxidants, including resveratrol, are responsible for it. We investigated if resveratrol has a more direct role in protection from harmful oxidation and development of thrombosis, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetric analysis demonstrated binding of resveratrol to fibrinogen, the main protein in the coagulation process, which also has an important application as a food additive in making of fibrin gels. Various spectroscopic methods have demonstrated that binding of resveratrol does not unfold or destabilize fibrinogen since both near and far-UV CD spectra as well as its melting temperature remained unchanged. A mutually protective effect against the free radical-induced oxidation of resveratrol and fibrinogen was found. The presence of fibrinogen caused a very small masking effect of the antioxidative potential of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing potential bioavailability and activity of resveratrol in circulation. By direct interaction and protection of fibrinogen, resveratrol may serve as an important antioxidant for prevention of thrombosis. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.",
journal = "FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021",
title = "Resveratrol and fibrinogen interactions",
pages = "15-15",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6033"
}

Gligorijević, N., Radomirović, M. Ž., Rajković, A., Nedić, O.,& Ćirković-Veličković, T.. (2021). Resveratrol and fibrinogen interactions. in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021, 15-15.
https://hdl.handle.net/21.15107/rcub_cherry_6033

Gligorijević N, Radomirović MŽ, Rajković A, Nedić O, Ćirković-Veličković T. Resveratrol and fibrinogen interactions. in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021. 2021;:15-15.
https://hdl.handle.net/21.15107/rcub_cherry_6033 .

Gligorijević, Nikola, Radomirović, Mirjana Ž., Rajković, Andreja, Nedić, Olgica, Ćirković-Veličković, Tanja, "Resveratrol and fibrinogen interactions" in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021 (2021):15-15,
https://hdl.handle.net/21.15107/rcub_cherry_6033 .