Vasović, Tamara

Link to this page

Authority KeyName Variants
a36bc409-7502-412a-a993-bdaa48106011
  • Vasović, Tamara (7)
Projects

Author's Bibliography

Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2

Đukić, Teodora; Mladenović, Maja; Stanić-Vučinić, Dragana; Radosavljević, Jelena; Smiljanić, Katarina; Sabljić, Ljiljana; Dević, Marija; Ćujić, Danica; Vasović, Tamara; Simović, Ana; Radomirović, Mirjana Ž.; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - JOUR
AU  - Đukić, Teodora
AU  - Mladenović, Maja
AU  - Stanić-Vučinić, Dragana
AU  - Radosavljević, Jelena
AU  - Smiljanić, Katarina
AU  - Sabljić, Ljiljana
AU  - Dević, Marija
AU  - Ćujić, 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/123456789/4330
AB  - Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production.

SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified 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.
PB  - Elsevier
T2  - Virology journal
T1  - Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2
VL  - 557
SP  - 15
EP  - 22
DO  - 10.1016/j.virol.2021.01.004
ER  - 
@article{
author = "Đukić, Teodora and Mladenović, Maja and Stanić-Vučinić, Dragana and Radosavljević, Jelena and Smiljanić, Katarina and Sabljić, Ljiljana and Dević, Marija and Ćujić, Danica and Vasović, Tamara and Simović, Ana and Radomirović, Mirjana Ž. and Ćirković-Veličković, Tanja",
year = "2021",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4330",
abstract = "Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production.

SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified 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.",
publisher = "Elsevier",
journal = "Virology journal",
title = "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2",
volume = "557",
pages = "15-22",
doi = "10.1016/j.virol.2021.01.004"
}
Đukić, T., Mladenović, M., Stanić-Vučinić, D., Radosavljević, J., Smiljanić, K., Sabljić, L., Dević, M., Ćujić, D., Vasović, T., Simović, A., Radomirović, M. Ž.,& Ćirković-Veličković, T. (2021). Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2.
Virology journalElsevier., 557, 15-22.
https://doi.org/10.1016/j.virol.2021.01.004
Đukić T, Mladenović M, Stanić-Vučinić D, Radosavljević J, Smiljanić K, Sabljić L, Dević M, Ćujić D, Vasović T, Simović A, Radomirović MŽ, Ćirković-Veličković T. Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2. Virology journal. 2021;557:15-22
Đukić Teodora, Mladenović Maja, Stanić-Vučinić Dragana, Radosavljević Jelena, Smiljanić Katarina, Sabljić Ljiljana, Dević Marija, Ćujić Danica, Vasović Tamara, Simović Ana, Radomirović Mirjana Ž., Ćirković-Veličković Tanja, "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2" 557 (2021):15-22,
https://doi.org/10.1016/j.virol.2021.01.004 .
4

Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2

Đukić, Teodora; Mladenović, Maja; Stanić-Vučinić, Dragana; Radosavljević, Jelena; Smiljanić, Katarina; Sabljić, Ljiljana; Dević, Marija; Ćujić, Danica; Vasović, Tamara; Simović, Ana; Radomirović, Mirjana Ž.; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - JOUR
AU  - Đukić, Teodora
AU  - Mladenović, Maja
AU  - Stanić-Vučinić, Dragana
AU  - Radosavljević, Jelena
AU  - Smiljanić, Katarina
AU  - Sabljić, Ljiljana
AU  - Dević, Marija
AU  - Ćujić, 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/123456789/4331
AB  - Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production.SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified 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.
PB  - Elsevier
T2  - Virology journal
T1  - Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2
VL  - 557
SP  - 15
EP  - 22
DO  - 10.1016/j.virol.2021.01.004
ER  - 
@article{
author = "Đukić, Teodora and Mladenović, Maja and Stanić-Vučinić, Dragana and Radosavljević, Jelena and Smiljanić, Katarina and Sabljić, Ljiljana and Dević, Marija and Ćujić, Danica and Vasović, Tamara and Simović, Ana and Radomirović, Mirjana Ž. and Ćirković-Veličković, Tanja",
year = "2021",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4331",
abstract = "Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production.SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified 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.",
publisher = "Elsevier",
journal = "Virology journal",
title = "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2",
volume = "557",
pages = "15-22",
doi = "10.1016/j.virol.2021.01.004"
}
Đukić, T., Mladenović, M., Stanić-Vučinić, D., Radosavljević, J., Smiljanić, K., Sabljić, L., Dević, M., Ćujić, D., Vasović, T., Simović, A., Radomirović, M. Ž.,& Ćirković-Veličković, T. (2021). Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2.
Virology journalElsevier., 557, 15-22.
https://doi.org/10.1016/j.virol.2021.01.004
Đukić T, Mladenović M, Stanić-Vučinić D, Radosavljević J, Smiljanić K, Sabljić L, Dević M, Ćujić D, Vasović T, Simović A, Radomirović MŽ, Ćirković-Veličković T. Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2. Virology journal. 2021;557:15-22
Đukić Teodora, Mladenović Maja, Stanić-Vučinić Dragana, Radosavljević Jelena, Smiljanić Katarina, Sabljić Ljiljana, Dević Marija, Ćujić Danica, Vasović Tamara, Simović Ana, Radomirović Mirjana Ž., Ćirković-Veličković Tanja, "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2" 557 (2021):15-22,
https://doi.org/10.1016/j.virol.2021.01.004 .
4

Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation

Gligorijević, Nikola; Vasović, Tamara; Lević, Steva M.; Miljević, Čedo; Nedić, Olgica; Nikolić, Milan

(Elsevier, 2020)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Vasović, Tamara
AU  - Lević, Steva M.
AU  - Miljević, Čedo
AU  - Nedić, Olgica
AU  - Nikolić, Milan
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3886
AB  - Clozapine is an atypical antipsychotic used for the treatment of schizophrenia. The prescribed target daily doses may reach 900 mg. Literature studies report a connection between clozapine usage and thrombosis development. Our in vitro study aimed to provide insight into molecular bases of this observation, investigating clozapine binding to fibrinogen, the main plasma protein involved in hemostasis. Fibrinogen/clozapine interaction was confirmed by protein fluorescence quenching, with an affinity constant of 1.7 × 105 M−1. Direct interactions did not affect the structure of fibrinogen, nor fibrinogen melting temperature. Clozapine binding affected fibrin formation by reducing coagulation speed and thickness of fibrin fibers suggesting that in the presence of clozapine, fibrinogen may acquire thrombogenic characteristics. Although no difference in fibrin gel porosity was detected, other factors present in the blood may act synergistically with altered fibrin formation to modify fibrin clot, thus increasing the risk for development of thrombosis in patients on clozapine treatment. ORAC and HORAC assays showed that clozapine reduced free radical-induced oxidation of fibrinogen. All observed effects of clozapine on fibrinogen are dose-dependent, with the effect on fibrin formation being more pronounced.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation
VL  - 154
SP  - 142
EP  - 149
DO  - 10.1016/j.ijbiomac.2020.03.119
ER  - 
@article{
author = "Gligorijević, Nikola and Vasović, Tamara and Lević, Steva M. and Miljević, Čedo and Nedić, Olgica and Nikolić, Milan",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3886",
abstract = "Clozapine is an atypical antipsychotic used for the treatment of schizophrenia. The prescribed target daily doses may reach 900 mg. Literature studies report a connection between clozapine usage and thrombosis development. Our in vitro study aimed to provide insight into molecular bases of this observation, investigating clozapine binding to fibrinogen, the main plasma protein involved in hemostasis. Fibrinogen/clozapine interaction was confirmed by protein fluorescence quenching, with an affinity constant of 1.7 × 105 M−1. Direct interactions did not affect the structure of fibrinogen, nor fibrinogen melting temperature. Clozapine binding affected fibrin formation by reducing coagulation speed and thickness of fibrin fibers suggesting that in the presence of clozapine, fibrinogen may acquire thrombogenic characteristics. Although no difference in fibrin gel porosity was detected, other factors present in the blood may act synergistically with altered fibrin formation to modify fibrin clot, thus increasing the risk for development of thrombosis in patients on clozapine treatment. ORAC and HORAC assays showed that clozapine reduced free radical-induced oxidation of fibrinogen. All observed effects of clozapine on fibrinogen are dose-dependent, with the effect on fibrin formation being more pronounced.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation",
volume = "154",
pages = "142-149",
doi = "10.1016/j.ijbiomac.2020.03.119"
}
Gligorijević, N., Vasović, T., Lević, S. M., Miljević, Č., Nedić, O.,& Nikolić, M. (2020). Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation.
International Journal of Biological MacromoleculesElsevier., 154, 142-149.
https://doi.org/10.1016/j.ijbiomac.2020.03.119
Gligorijević N, Vasović T, Lević SM, Miljević Č, Nedić O, Nikolić M. Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation. International Journal of Biological Macromolecules. 2020;154:142-149
Gligorijević Nikola, Vasović Tamara, Lević Steva M., Miljević Čedo, Nedić Olgica, Nikolić Milan, "Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation" 154 (2020):142-149,
https://doi.org/10.1016/j.ijbiomac.2020.03.119 .
2
1
2

Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation

Gligorijević, Nikola; Vasović, Tamara; Lević, Steva M.; Miljević, Čedo; Nedić, Olgica; Nikolić, Milan

(Elsevier, 2020)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Vasović, Tamara
AU  - Lević, Steva M.
AU  - Miljević, Čedo
AU  - Nedić, Olgica
AU  - Nikolić, Milan
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3896
AB  - Clozapine is an atypical antipsychotic used for the treatment of schizophrenia. The prescribed target daily doses may reach 900 mg. Literature studies report a connection between clozapine usage and thrombosis development. Our in vitro study aimed to provide insight into molecular bases of this observation, investigating clozapine binding to fibrinogen, the main plasma protein involved in hemostasis. Fibrinogen/clozapine interaction was confirmed by protein fluorescence quenching, with an affinity constant of 1.7 × 105 M−1. Direct interactions did not affect the structure of fibrinogen, nor fibrinogen melting temperature. Clozapine binding affected fibrin formation by reducing coagulation speed and thickness of fibrin fibers suggesting that in the presence of clozapine, fibrinogen may acquire thrombogenic characteristics. Although no difference in fibrin gel porosity was detected, other factors present in the blood may act synergistically with altered fibrin formation to modify fibrin clot, thus increasing the risk for development of thrombosis in patients on clozapine treatment. ORAC and HORAC assays showed that clozapine reduced free radical-induced oxidation of fibrinogen. All observed effects of clozapine on fibrinogen are dose-dependent, with the effect on fibrin formation being more pronounced.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation
VL  - 154
SP  - 142
EP  - 149
DO  - 10.1016/j.ijbiomac.2020.03.119
ER  - 
@article{
author = "Gligorijević, Nikola and Vasović, Tamara and Lević, Steva M. and Miljević, Čedo and Nedić, Olgica and Nikolić, Milan",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3896",
abstract = "Clozapine is an atypical antipsychotic used for the treatment of schizophrenia. The prescribed target daily doses may reach 900 mg. Literature studies report a connection between clozapine usage and thrombosis development. Our in vitro study aimed to provide insight into molecular bases of this observation, investigating clozapine binding to fibrinogen, the main plasma protein involved in hemostasis. Fibrinogen/clozapine interaction was confirmed by protein fluorescence quenching, with an affinity constant of 1.7 × 105 M−1. Direct interactions did not affect the structure of fibrinogen, nor fibrinogen melting temperature. Clozapine binding affected fibrin formation by reducing coagulation speed and thickness of fibrin fibers suggesting that in the presence of clozapine, fibrinogen may acquire thrombogenic characteristics. Although no difference in fibrin gel porosity was detected, other factors present in the blood may act synergistically with altered fibrin formation to modify fibrin clot, thus increasing the risk for development of thrombosis in patients on clozapine treatment. ORAC and HORAC assays showed that clozapine reduced free radical-induced oxidation of fibrinogen. All observed effects of clozapine on fibrinogen are dose-dependent, with the effect on fibrin formation being more pronounced.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation",
volume = "154",
pages = "142-149",
doi = "10.1016/j.ijbiomac.2020.03.119"
}
Gligorijević, N., Vasović, T., Lević, S. M., Miljević, Č., Nedić, O.,& Nikolić, M. (2020). Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation.
International Journal of Biological MacromoleculesElsevier., 154, 142-149.
https://doi.org/10.1016/j.ijbiomac.2020.03.119
Gligorijević N, Vasović T, Lević SM, Miljević Č, Nedić O, Nikolić M. Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation. International Journal of Biological Macromolecules. 2020;154:142-149
Gligorijević Nikola, Vasović Tamara, Lević Steva M., Miljević Čedo, Nedić Olgica, Nikolić Milan, "Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation" 154 (2020):142-149,
https://doi.org/10.1016/j.ijbiomac.2020.03.119 .
2
1
2

Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions

Minić, Simeon L.; Radomirović, Mirjana Ž.; Savković, Nina; Radibratović, Milica; Mihailović-Vesić, Jelena; Vasović, Tamara; Nikolić, Milan; Milčić, Miloš K.; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2018)

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Savković, Nina
AU  - Radibratović, Milica
AU  - Mihailović-Vesić, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3186
AB  - In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions
VL  - 269
SP  - 43
EP  - 52
DO  - 10.1016/j.foodchem.2018.06.138
ER  - 
@article{
author = "Minić, Simeon L. and Radomirović, Mirjana Ž. and Savković, Nina and Radibratović, Milica and Mihailović-Vesić, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3186",
abstract = "In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions",
volume = "269",
pages = "43-52",
doi = "10.1016/j.foodchem.2018.06.138"
}
Minić, S. L., Radomirović, M. Ž., Savković, N., Radibratović, M., Mihailović-Vesić, J., Vasović, T., Nikolić, M., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2018). Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions.
Food ChemistryElsevier Sci Ltd, Oxford., 269, 43-52.
https://doi.org/10.1016/j.foodchem.2018.06.138
Minić SL, Radomirović MŽ, Savković N, Radibratović M, Mihailović-Vesić J, Vasović T, Nikolić M, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. Food Chemistry. 2018;269:43-52
Minić Simeon L., Radomirović Mirjana Ž., Savković Nina, Radibratović Milica, Mihailović-Vesić Jelena, Vasović Tamara, Nikolić Milan, Milčić Miloš K., Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions" 269 (2018):43-52,
https://doi.org/10.1016/j.foodchem.2018.06.138 .
1
3
2
2

Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138

Minić, Simeon L.; Radomirović, Mirjana Ž.; Savković, Nina; Radibratović, Milica; Mihailović-Vesić, Jelena; Vasović, Tamara; Nikolić, Milan; Milčić, Miloš K.; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2018)

TY  - BOOK
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Savković, Nina
AU  - Radibratović, Milica
AU  - Mihailović-Vesić, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3187
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138
ER  - 
@book{
author = "Minić, Simeon L. and Radomirović, Mirjana Ž. and Savković, Nina and Radibratović, Milica and Mihailović-Vesić, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3187",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138"
}
Minić, S. L., Radomirović, M. Ž., Savković, N., Radibratović, M., Mihailović-Vesić, J., Vasović, T., Nikolić, M., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2018). Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138.
Food ChemistryElsevier Sci Ltd, Oxford..
Minić SL, Radomirović MŽ, Savković N, Radibratović M, Mihailović-Vesić J, Vasović T, Nikolić M, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138. Food Chemistry. 2018;
Minić Simeon L., Radomirović Mirjana Ž., Savković Nina, Radibratović Milica, Mihailović-Vesić Jelena, Vasović Tamara, Nikolić Milan, Milčić Miloš K., Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138" (2018)

Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions

Minić, Simeon L.; Radomirović, Mirjana Ž.; Savković, Nina; Radibratović, Milica; Mihailović-Vesić, Jelena; Vasović, Tamara; Nikolić, Milan; Milčić, Miloš K.; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2018)

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Savković, Nina
AU  - Radibratović, Milica
AU  - Mihailović-Vesić, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2197
AB  - In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions
VL  - 269
SP  - 43
EP  - 52
DO  - 10.1016/j.foodchem.2018.06.138
ER  - 
@article{
author = "Minić, Simeon L. and Radomirović, Mirjana Ž. and Savković, Nina and Radibratović, Milica and Mihailović-Vesić, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2197",
abstract = "In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions",
volume = "269",
pages = "43-52",
doi = "10.1016/j.foodchem.2018.06.138"
}
Minić, S. L., Radomirović, M. Ž., Savković, N., Radibratović, M., Mihailović-Vesić, J., Vasović, T., Nikolić, M., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2018). Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions.
Food ChemistryElsevier Sci Ltd, Oxford., 269, 43-52.
https://doi.org/10.1016/j.foodchem.2018.06.138
Minić SL, Radomirović MŽ, Savković N, Radibratović M, Mihailović-Vesić J, Vasović T, Nikolić M, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. Food Chemistry. 2018;269:43-52
Minić Simeon L., Radomirović Mirjana Ž., Savković Nina, Radibratović Milica, Mihailović-Vesić Jelena, Vasović Tamara, Nikolić Milan, Milčić Miloš K., Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions" 269 (2018):43-52,
https://doi.org/10.1016/j.foodchem.2018.06.138 .
1
3
2
2