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  - 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  - 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  - 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  - 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  - 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  - 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  - 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 .

TY  - CONF
AU  - Khulal, Urmila
AU  - Radomirović, Mirjana Ž.
AU  - de Guzman, Maria Krishna
AU  - Mutić, Jelena
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6034
AB  - Tropomyosin (TM) is known to be a major shrimp allergen (e.g., Pen m 1) and considered a cross-reacting panallergen among shellfish/invertebrates. The clam TM is also considered its major allergen but has not been widely studied. The food processing techniques can alter the TM allergenicity. Hence, the objective of this research is to detect and quantify TM in fresh and differentially treated clams collected in Korea via in-house developed sandwich ELISA protocol to evaluate the effect of various real-life processing techniques on TM stability.
Freshly bought live clams (FC), 4 groups of randomly selected equal number of similarly sized clams were differentially treated. Fresh and packaged (FPC), fresh and frozen at -20◦C (FroC). The fresh clams boiled (BC) in boiling water and the marinated clams (MC) suspended in marinade solution for 5 days; soluble protein extracted overnight from 5 samples in PBS buffer with protease inhibitor; BCA assay determined the protein content; capture-detection-enzyme linked secondary antibody in-house ELISA. ELISA was validated with specific antibody based Western blot (WB).
The total soluble protein content of raw clams (FC, FPC, FroC) was between 2.8-4.9 mg/ml. The cooked clams (BC, MC) lost total protein during the cooking and was determined <1 mg/ml. The leaked protein in boiled water (BW) and marinade solution (MS) was confirmed with the protein assay as 0.48 mg/ml and 5.5 mg/ml, respectively. ELISA quantified TM (pg/ml) in FPC =BC (610) >FroC (290) >FC (75) >MC. It (and WB) showed that boiling has no effect on heat stable TM IgG binding, BW contained considerable amount of TM (with pronounced IgG binding). MC, however showed no TM epitope recognition in WB (no band in SDS PAGE) and was not quantified by ELISA nor in MS (<LLOQ). Marination might degrade the TM to significant extent possibly altering the allergenicity.
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  - Detection and quantification of tropomyosin in differentially treated clams from Korea
SP  - 25
EP  - 25
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6034
ER  - 

@conference{
author = "Khulal, Urmila and Radomirović, Mirjana Ž. and de Guzman, Maria Krishna and Mutić, Jelena and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Tropomyosin (TM) is known to be a major shrimp allergen (e.g., Pen m 1) and considered a cross-reacting panallergen among shellfish/invertebrates. The clam TM is also considered its major allergen but has not been widely studied. The food processing techniques can alter the TM allergenicity. Hence, the objective of this research is to detect and quantify TM in fresh and differentially treated clams collected in Korea via in-house developed sandwich ELISA protocol to evaluate the effect of various real-life processing techniques on TM stability.
Freshly bought live clams (FC), 4 groups of randomly selected equal number of similarly sized clams were differentially treated. Fresh and packaged (FPC), fresh and frozen at -20◦C (FroC). The fresh clams boiled (BC) in boiling water and the marinated clams (MC) suspended in marinade solution for 5 days; soluble protein extracted overnight from 5 samples in PBS buffer with protease inhibitor; BCA assay determined the protein content; capture-detection-enzyme linked secondary antibody in-house ELISA. ELISA was validated with specific antibody based Western blot (WB).
The total soluble protein content of raw clams (FC, FPC, FroC) was between 2.8-4.9 mg/ml. The cooked clams (BC, MC) lost total protein during the cooking and was determined <1 mg/ml. The leaked protein in boiled water (BW) and marinade solution (MS) was confirmed with the protein assay as 0.48 mg/ml and 5.5 mg/ml, respectively. ELISA quantified TM (pg/ml) in FPC =BC (610) >FroC (290) >FC (75) >MC. It (and WB) showed that boiling has no effect on heat stable TM IgG binding, BW contained considerable amount of TM (with pronounced IgG binding). MC, however showed no TM epitope recognition in WB (no band in SDS PAGE) and was not quantified by ELISA nor in MS (<LLOQ). Marination might degrade the TM to significant extent possibly altering the allergenicity.",
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 = "Detection and quantification of tropomyosin in differentially treated clams from Korea",
pages = "25-25",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6034"
}

Khulal, U., Radomirović, M. Ž., de Guzman, M. K., Mutić, J., Rajković, A.,& Ćirković-Veličković, T.. (2021). Detection and quantification of tropomyosin in differentially treated clams from Korea. 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., 25-25.
https://hdl.handle.net/21.15107/rcub_cherry_6034

Khulal U, Radomirović MŽ, de Guzman MK, Mutić J, Rajković A, Ćirković-Veličković T. Detection and quantification of tropomyosin in differentially treated clams from Korea. in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts. 2021;:25-25.
https://hdl.handle.net/21.15107/rcub_cherry_6034 .

Khulal, Urmila, Radomirović, Mirjana Ž., de Guzman, Maria Krishna, Mutić, Jelena, Rajković, Andreja, Ćirković-Veličković, Tanja, "Detection and quantification of tropomyosin in differentially treated clams from Korea" in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts (2021):25-25,
https://hdl.handle.net/21.15107/rcub_cherry_6034 .

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/123456789/6039
AB  - Phycobiliproteins (PBP) are extensively used as fluorescent probes due to highly fluorescent, covalently bound, tetrapyrrole chromophores. A new method for covalent attachment of phycocyanin’s chromophore, phycocyanobilin (PCB), is proposed. We exploited Traut’s reagent (TR) to introduce sulfhydryl groups in the bovine serum albumin (BSA), by modifying its lysine residues. TR successfully modified BSA under all tested molar ratios of reagent per mole of BSA. The higher degree of modification by TR induces more profound alterations of BSA structure. PCB was covalently attached to introduced sulfhydryl groups at pH 9 at 20–fold ratio. An increase in the molar ratio of TR per mole of BSA leads to amplification of fluorescent signal of PCB-modified BSA. Using BSA as a model protein, a 50-fold molar excess of TR seems to be the optimal choice for balancing between a satisfactory level of signal amplification and the adverse effect on protein structure. The method could be used for labeling virtually any protein.
PB  - Beograd : Srpsko hemijsko društvo
C3  - 57th Meeting of the Serbian Chemical Society, Kragujevac, Serbia, 18th-19th June, 2021. In: Book of Abstracts and Proceedings
T1  - Fluorescent labeling of bovine serum albumin with phycocyanobilin using Traut’s reagent
SP  - 71
EP  - 71
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6039
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) are extensively used as fluorescent probes due to highly fluorescent, covalently bound, tetrapyrrole chromophores. A new method for covalent attachment of phycocyanin’s chromophore, phycocyanobilin (PCB), is proposed. We exploited Traut’s reagent (TR) to introduce sulfhydryl groups in the bovine serum albumin (BSA), by modifying its lysine residues. TR successfully modified BSA under all tested molar ratios of reagent per mole of BSA. The higher degree of modification by TR induces more profound alterations of BSA structure. PCB was covalently attached to introduced sulfhydryl groups at pH 9 at 20–fold ratio. An increase in the molar ratio of TR per mole of BSA leads to amplification of fluorescent signal of PCB-modified BSA. Using BSA as a model protein, a 50-fold molar excess of TR seems to be the optimal choice for balancing between a satisfactory level of signal amplification and the adverse effect on protein structure. The method could be used for labeling virtually any protein.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "57th Meeting of the Serbian Chemical Society, Kragujevac, Serbia, 18th-19th June, 2021. In: Book of Abstracts and Proceedings",
title = "Fluorescent labeling of bovine serum albumin with phycocyanobilin using Traut’s reagent",
pages = "71-71",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6039"
}

Radomirović, M. Ž., Gligorijević, N., Minić, S., Nikolić, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Fluorescent labeling of bovine serum albumin with phycocyanobilin using Traut’s reagent. in 57th Meeting of the Serbian Chemical Society, Kragujevac, Serbia, 18th-19th June, 2021. In: Book of Abstracts and Proceedings
Beograd : Srpsko hemijsko društvo., 71-71.
https://hdl.handle.net/21.15107/rcub_cherry_6039

Radomirović MŽ, Gligorijević N, Minić S, Nikolić M, Stanić-Vučinić D, Ćirković-Veličković T. Fluorescent labeling of bovine serum albumin with phycocyanobilin using Traut’s reagent. in 57th Meeting of the Serbian Chemical Society, Kragujevac, Serbia, 18th-19th June, 2021. In: Book of Abstracts and Proceedings. 2021;:71-71.
https://hdl.handle.net/21.15107/rcub_cherry_6039 .

Radomirović, Mirjana Ž., Gligorijević, Nikola, Minić, Simeon, Nikolić, Milan, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Fluorescent labeling of bovine serum albumin with phycocyanobilin using Traut’s reagent" in 57th Meeting of the Serbian Chemical Society, Kragujevac, Serbia, 18th-19th June, 2021. In: Book of Abstracts and Proceedings (2021):71-71,
https://hdl.handle.net/21.15107/rcub_cherry_6039 .

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Jovanović, Vesna B.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5716
C3  - Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021
T1  - Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting
SP  - 71
EP  - 71
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5716
ER  - 

@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Đukić, Teodora and Vasović, Tamara and Jovanović, Vesna B. and Ćirković-Veličković, Tanja",
year = "2021",
journal = "Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021",
title = "Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting",
pages = "71-71",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5716"
}

Smiljanić, K., Prodić, I., Đukić, T., Vasović, T., Jovanović, V. B.,& Ćirković-Veličković, T.. (2021). Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021, 71-71.
https://hdl.handle.net/21.15107/rcub_cherry_5716

Smiljanić K, Prodić I, Đukić T, Vasović T, Jovanović VB, Ćirković-Veličković T. Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021. 2021;:71-71.
https://hdl.handle.net/21.15107/rcub_cherry_5716 .

Smiljanić, Katarina, Prodić, Ivana, Đukić, Teodora, Vasović, Tamara, Jovanović, Vesna B., Ćirković-Veličković, Tanja, "Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting" in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021 (2021):71-71,
https://hdl.handle.net/21.15107/rcub_cherry_5716 .

TY  - CONF
AU  - Đukić, Teodora
AU  - Mladenović, Maja
AU  - Stanić-Vučinić, Dragana
AU  - Radosavljević, Jelena
AU  - Smiljanić, Katarina
AU  - Sabljić, Ljiljana
AU  - Gnjatović, Marija Lj.
AU  - Cujić, Danica
AU  - Vasović, Tamara
AU  - Simović, Ana
AU  - Radomirović, Mirjana Ž.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5735
AB  - Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARSCoV-2) infection and for assessment of immunological response after the vaccination. Nucleocapsid (N) protein is the most abundant virus protein and strong immunogen. The aim was develop efficient, low-cost production of N protein large fragment and to characterize it with bottom-up, high-resolution tandem mass spectrometry and immunologically.
SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form and purified by several chromatographic steps and was subjected to SDS-PAGE and in-gel digested with trypsin.
rfNP was tested in immunoblot using sera of COVID-19 convalescent patients. ELISA was optimized with sera of RT-PCR confirmed positive symptomatic patients and healthy individuals. IgG detection sensitivity was 96% (47/50) and specificity 97% (67/68), while IgM detection was slightly lower. Identity of rfNP was confirmed with high scores and peptide coverage above 80%. Estimation from the value of areas under ion extracted chromatographic curves is that only up to 0,03% of the total band protein quantity belongs to host proteins, while rfNP share is well above 99,9%, resulting in highly pure nucleocapsid protein preparation.
C3  - Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021
T1  - Proteomic and immunological characterization of recombinantly expressed nucleocapsid SARS-CoV 2 protein fragment in E. coli
SP  - 50
EP  - 50
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5735
ER  - 

@conference{
author = "Đukić, Teodora and Mladenović, Maja and Stanić-Vučinić, Dragana and Radosavljević, Jelena and Smiljanić, Katarina and Sabljić, Ljiljana and Gnjatović, Marija Lj. and Cujić, Danica and Vasović, Tamara and Simović, Ana and Radomirović, Mirjana Ž. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARSCoV-2) infection and for assessment of immunological response after the vaccination. Nucleocapsid (N) protein is the most abundant virus protein and strong immunogen. The aim was develop efficient, low-cost production of N protein large fragment and to characterize it with bottom-up, high-resolution tandem mass spectrometry and immunologically.
SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form and purified by several chromatographic steps and was subjected to SDS-PAGE and in-gel digested with trypsin.
rfNP was tested in immunoblot using sera of COVID-19 convalescent patients. ELISA was optimized with sera of RT-PCR confirmed positive symptomatic patients and healthy individuals. IgG detection sensitivity was 96% (47/50) and specificity 97% (67/68), while IgM detection was slightly lower. Identity of rfNP was confirmed with high scores and peptide coverage above 80%. Estimation from the value of areas under ion extracted chromatographic curves is that only up to 0,03% of the total band protein quantity belongs to host proteins, while rfNP share is well above 99,9%, resulting in highly pure nucleocapsid protein preparation.",
journal = "Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021",
title = "Proteomic and immunological characterization of recombinantly expressed nucleocapsid SARS-CoV 2 protein fragment in E. coli",
pages = "50-50",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5735"
}

Đukić, T., Mladenović, M., Stanić-Vučinić, D., Radosavljević, J., Smiljanić, K., Sabljić, L., Gnjatović, M. Lj., Cujić, D., Vasović, T., Simović, A., Radomirović, M. Ž.,& Ćirković-Veličković, T.. (2021). Proteomic and immunological characterization of recombinantly expressed nucleocapsid SARS-CoV 2 protein fragment in E. coli. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021, 50-50.
https://hdl.handle.net/21.15107/rcub_cherry_5735

Đukić T, Mladenović M, Stanić-Vučinić D, Radosavljević J, Smiljanić K, Sabljić L, Gnjatović ML, Cujić D, Vasović T, Simović A, Radomirović MŽ, Ćirković-Veličković T. Proteomic and immunological characterization of recombinantly expressed nucleocapsid SARS-CoV 2 protein fragment in E. coli. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021. 2021;:50-50.
https://hdl.handle.net/21.15107/rcub_cherry_5735 .

Đukić, Teodora, Mladenović, Maja, Stanić-Vučinić, Dragana, Radosavljević, Jelena, Smiljanić, Katarina, Sabljić, Ljiljana, Gnjatović, Marija Lj., Cujić, Danica, Vasović, Tamara, Simović, Ana, Radomirović, Mirjana Ž., Ćirković-Veličković, Tanja, "Proteomic and immunological characterization of recombinantly expressed nucleocapsid SARS-CoV 2 protein fragment in E. coli" in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021 (2021):50-50,
https://hdl.handle.net/21.15107/rcub_cherry_5735 .

TY  - CONF
AU  - Maja, Mladenović
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Stanić-Vučinić, Dragana
AU  - Smiljanić, Katarina
AU  - Radosavljević, Jelena
AU  - Sabljić, Ljiljana
AU  - Dević, Marija
AU  - Cujić, Danica
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5737
AB  - Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARSCoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production, suitable for serological diagnosis. SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified by immobilized metal ion affinity chromatography and strong cation exchange chromatography after which it was analyzed by Mass and CD spectrometry and characterized biochemically and immunologically. Purified rfNP has secondary structure of full-length recombinant N protein, with high percentage of disordered structure (34.2%) and of β-sheet (40.7%). rfNP was tested in immunoblot using sera of COVID-19 convalescent patients. ELISA was optimized with sera of RT-PCR confirmed positive symptomatic patients and healthy individuals. IgG detection sensitivity was 96% (47/50) and specificity 97% (67/68), while IgM detection was
slightly lower (94% and 96.5%, respectively). Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection.
C3  - FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia
T1  - Expression, purification and immunological characterization of recombinant protein fragment from SARS-CoV-2
SP  - 33
EP  - 33
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5737
ER  - 

@conference{
author = "Maja, Mladenović and Đukić, Teodora and Vasović, Tamara and Stanić-Vučinić, Dragana and Smiljanić, Katarina and Radosavljević, Jelena and Sabljić, Ljiljana and Dević, Marija and Cujić, Danica and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARSCoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production, suitable for serological diagnosis. SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified by immobilized metal ion affinity chromatography and strong cation exchange chromatography after which it was analyzed by Mass and CD spectrometry and characterized biochemically and immunologically. Purified rfNP has secondary structure of full-length recombinant N protein, with high percentage of disordered structure (34.2%) and of β-sheet (40.7%). rfNP was tested in immunoblot using sera of COVID-19 convalescent patients. ELISA was optimized with sera of RT-PCR confirmed positive symptomatic patients and healthy individuals. IgG detection sensitivity was 96% (47/50) and specificity 97% (67/68), while IgM detection was
slightly lower (94% and 96.5%, respectively). Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection.",
journal = "FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia",
title = "Expression, purification and immunological characterization of recombinant protein fragment from SARS-CoV-2",
pages = "33-33",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5737"
}

Maja, M., Đukić, T., Vasović, T., Stanić-Vučinić, D., Smiljanić, K., Radosavljević, J., Sabljić, L., Dević, M., Cujić, D.,& Ćirković-Veličković, T.. (2021). Expression, purification and immunological characterization of recombinant protein fragment from SARS-CoV-2. in FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia, 33-33.
https://hdl.handle.net/21.15107/rcub_cherry_5737

Maja M, Đukić T, Vasović T, Stanić-Vučinić D, Smiljanić K, Radosavljević J, Sabljić L, Dević M, Cujić D, Ćirković-Veličković T. Expression, purification and immunological characterization of recombinant protein fragment from SARS-CoV-2. in FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia. 2021;:33-33.
https://hdl.handle.net/21.15107/rcub_cherry_5737 .

Maja, Mladenović, Đukić, Teodora, Vasović, Tamara, Stanić-Vučinić, Dragana, Smiljanić, Katarina, Radosavljević, Jelena, Sabljić, Ljiljana, Dević, Marija, Cujić, Danica, Ćirković-Veličković, Tanja, "Expression, purification and immunological characterization of recombinant protein fragment from SARS-CoV-2" in FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia (2021):33-33,
https://hdl.handle.net/21.15107/rcub_cherry_5737 .

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Jovanović, Vesna B.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5773
AB  - Background: We have undertaken study on our porcine-derived trypsin generated
proteomic data of the major peanut allergen Ara h 1 from the raw and roasted peanut, to
assess possible facilitating/hindrance effects on trypsin digestion efficacy caused by post-
translational and chemical modifications (PTMs) positioned on K/R residues. If potential
hindrance effects caused by PTMs are observed with porcine trypsin, then they can be just
augmented and more pronounced within human intestinal digestion. The logic for such
reasoning is in inferior performance of human trypsin compared to porcine-derived used in
proteomic digestion protocols, also the lower trypsin-to-sample ratio and much shorter
digestion times, even though gastric digestion precedes and trypsin is not the sole digestive
enzyme.
Methods: Novel method was developed to decipher outcomes at scissile bonds using PEAKS
Studio-X+ in reassessment of high-resolution tandem mass spectrometry data on 18h-long
trypsin digestion protocol.
Results: In eight modified K/R residues involving methylation, dihydroxy and formylation,
differences in extent of miscleavage between modified and unmodified peptides, were
significantly higher (>10%) in modified peptides.
Conclusion: It is important to elucidate impact of modifications on trypsin digestion
performance, but also on other proteases involved in digestion process due to possible
effects on allergenicity of food proteins/peptides.
PB  - INFOGEST Cost action, INRAE, Teagasc LTD.
C3  - Virtual International Conference on Food Digestion 6th and 7th May, 2021
T1  - Trypsin as a proteomic probe to assess food protein digestibility in relation to post- translational modifications
SP  - 18
EP  - 18
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5773
ER  - 

@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Đukić, Teodora and Vasović, Tamara and Jovanović, Vesna B. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Background: We have undertaken study on our porcine-derived trypsin generated
proteomic data of the major peanut allergen Ara h 1 from the raw and roasted peanut, to
assess possible facilitating/hindrance effects on trypsin digestion efficacy caused by post-
translational and chemical modifications (PTMs) positioned on K/R residues. If potential
hindrance effects caused by PTMs are observed with porcine trypsin, then they can be just
augmented and more pronounced within human intestinal digestion. The logic for such
reasoning is in inferior performance of human trypsin compared to porcine-derived used in
proteomic digestion protocols, also the lower trypsin-to-sample ratio and much shorter
digestion times, even though gastric digestion precedes and trypsin is not the sole digestive
enzyme.
Methods: Novel method was developed to decipher outcomes at scissile bonds using PEAKS
Studio-X+ in reassessment of high-resolution tandem mass spectrometry data on 18h-long
trypsin digestion protocol.
Results: In eight modified K/R residues involving methylation, dihydroxy and formylation,
differences in extent of miscleavage between modified and unmodified peptides, were
significantly higher (>10%) in modified peptides.
Conclusion: It is important to elucidate impact of modifications on trypsin digestion
performance, but also on other proteases involved in digestion process due to possible
effects on allergenicity of food proteins/peptides.",
publisher = "INFOGEST Cost action, INRAE, Teagasc LTD.",
journal = "Virtual International Conference on Food Digestion 6th and 7th May, 2021",
title = "Trypsin as a proteomic probe to assess food protein digestibility in relation to post- translational modifications",
pages = "18-18",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5773"
}

Smiljanić, K., Prodić, I., Đukić, T., Vasović, T., Jovanović, V. B.,& Ćirković-Veličković, T.. (2021). Trypsin as a proteomic probe to assess food protein digestibility in relation to post- translational modifications. in Virtual International Conference on Food Digestion 6th and 7th May, 2021
INFOGEST Cost action, INRAE, Teagasc LTD.., 18-18.
https://hdl.handle.net/21.15107/rcub_cherry_5773

Smiljanić K, Prodić I, Đukić T, Vasović T, Jovanović VB, Ćirković-Veličković T. Trypsin as a proteomic probe to assess food protein digestibility in relation to post- translational modifications. in Virtual International Conference on Food Digestion 6th and 7th May, 2021. 2021;:18-18.
https://hdl.handle.net/21.15107/rcub_cherry_5773 .

Smiljanić, Katarina, Prodić, Ivana, Đukić, Teodora, Vasović, Tamara, Jovanović, Vesna B., Ćirković-Veličković, Tanja, "Trypsin as a proteomic probe to assess food protein digestibility in relation to post- translational modifications" in Virtual International Conference on Food Digestion 6th and 7th May, 2021 (2021):18-18,
https://hdl.handle.net/21.15107/rcub_cherry_5773 .