Nikolić, Milan

Link to this page

Authority KeyName Variants
orcid::0000-0003-0932-889X
  • Nikolić, Milan (57)
Projects
Molecular properties and modifications of some respiratory and nutritional allergens Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research
Rational design and synthesis of biologically active and coordination compounds and functional materials, relevant for (bio)nanotechnology The study of physicochemical and biochemical processes in living environment that have impacts on pollution and the investigation of possibilities for minimizing the consequences
Molecular mechanisms of redox signalling in homeostasis: adaptation and pathology Structural characterisation of the insulin-like growth factor (IGF) binding proteins and IGF receptors, their interactions with other physiological molecules and alterations in metabolic disorders
Hemijske i biohemijske konsekvence metal-ligand interakcija, II. deo Interactions of natural products, their derivatives and coordination compounds with proteins and nucleic acids
FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics Allergens, antibodies, enzymes and small physiologically important molecules: design, structure, function and relevance
COST COST Action [CA15135]
COST Action [FA 1005] Estonian Ministry for Education and Research [IUT34-14]
German Research Foundation (DFG) [INST 208/664-1 FUGG] Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200168 (University of Belgrade, Faculty of Chemistry)
Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200288 (Innovation Center of the Faculty of Chemistry) The Role of Redox-Active Substances in the Maintenance of Homeostasis
Spanish Government financial support through project PGC2018-094503-B-C22 (MCIU/AEI/FEDER, UE). The synthesis of aminoquinoline-based antimalarials and botulinum neurotoxin A inhibitors
Natural products of plants and lichens: isolation, identification, biological activity and application Interactive role of dyslipidemia, oxidative stress and inflammation in atherosclerosis and other diseases: genetic and biochemical markers
Teorijska istraživanja osobina jako korelisanih sistema sa složenim strukturama Razvoj novih terapijskih postupaka u prevenciji i lečenju bolesti jetre: Uloga i mehanizam delovanja polinezasićenih masnih kiselina

Author's Bibliography

Supplementary data for the article: Araškov, J. B.; Nikolić, M.; Armaković, S.; Armaković, S.; Rodić, M.; Višnjevac, A.; Padrón, J. M.; Todorović, T. R.; Filipović, N. R. Structural, Antioxidant, Antiproliferative and In‒silico Study of Pyridine-Based Hydrazonyl‒selenazoles and Their Sulphur Isosteres. Journal of Molecular Structure 2021, 1240, 130512. https://doi.org/10.1016/j.molstruc.2021.130512.

Araškov, Jovana B.; Nikolić, Milan; Armaković, Stevan; Armaković, Sanja; Rodić, Marko; Višnjevac, Aleksandar; Padrón, José M.; Todorović, Tamara R.; Filipović, Nenad R.

(Elsevier, 2021)

TY  - DATA
AU  - Araškov, Jovana B.
AU  - Nikolić, Milan
AU  - Armaković, Stevan
AU  - Armaković, Sanja
AU  - Rodić, Marko
AU  - Višnjevac, Aleksandar
AU  - Padrón, José M.
AU  - Todorović, Tamara R.
AU  - Filipović, Nenad R.
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S0022286021006451
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4540
PB  - Elsevier
T2  - Journal of Molecular Structure
T1  - Supplementary data for the article: Araškov, J. B.; Nikolić, M.; Armaković, S.; Armaković, S.; Rodić, M.; Višnjevac, A.; Padrón, J. M.; Todorović, T. R.; Filipović, N. R. Structural, Antioxidant, Antiproliferative and In‒silico Study of Pyridine-Based Hydrazonyl‒selenazoles and Their Sulphur Isosteres. Journal of Molecular Structure 2021, 1240, 130512. https://doi.org/10.1016/j.molstruc.2021.130512.
ER  - 
@misc{
author = "Araškov, Jovana B. and Nikolić, Milan and Armaković, Stevan and Armaković, Sanja and Rodić, Marko and Višnjevac, Aleksandar and Padrón, José M. and Todorović, Tamara R. and Filipović, Nenad R.",
year = "2021",
publisher = "Elsevier",
journal = "Journal of Molecular Structure",
title = "Supplementary data for the article: Araškov, J. B.; Nikolić, M.; Armaković, S.; Armaković, S.; Rodić, M.; Višnjevac, A.; Padrón, J. M.; Todorović, T. R.; Filipović, N. R. Structural, Antioxidant, Antiproliferative and In‒silico Study of Pyridine-Based Hydrazonyl‒selenazoles and Their Sulphur Isosteres. Journal of Molecular Structure 2021, 1240, 130512. https://doi.org/10.1016/j.molstruc.2021.130512."
}
Araškov, J. B., Nikolić, M., Armaković, S., Armaković, S., Rodić, M., Višnjevac, A., Padrón, J. M., Todorović, T. R.,& Filipović, N. R.. (2021). Supplementary data for the article: Araškov, J. B.; Nikolić, M.; Armaković, S.; Armaković, S.; Rodić, M.; Višnjevac, A.; Padrón, J. M.; Todorović, T. R.; Filipović, N. R. Structural, Antioxidant, Antiproliferative and In‒silico Study of Pyridine-Based Hydrazonyl‒selenazoles and Their Sulphur Isosteres. Journal of Molecular Structure 2021, 1240, 130512. https://doi.org/10.1016/j.molstruc.2021.130512.. in Journal of Molecular Structure
Elsevier..
Araškov JB, Nikolić M, Armaković S, Armaković S, Rodić M, Višnjevac A, Padrón JM, Todorović TR, Filipović NR. Supplementary data for the article: Araškov, J. B.; Nikolić, M.; Armaković, S.; Armaković, S.; Rodić, M.; Višnjevac, A.; Padrón, J. M.; Todorović, T. R.; Filipović, N. R. Structural, Antioxidant, Antiproliferative and In‒silico Study of Pyridine-Based Hydrazonyl‒selenazoles and Their Sulphur Isosteres. Journal of Molecular Structure 2021, 1240, 130512. https://doi.org/10.1016/j.molstruc.2021.130512.. in Journal of Molecular Structure. 2021;..
Araškov, Jovana B., Nikolić, Milan, Armaković, Stevan, Armaković, Sanja, Rodić, Marko, Višnjevac, Aleksandar, Padrón, José M., Todorović, Tamara R., Filipović, Nenad R., "Supplementary data for the article: Araškov, J. B.; Nikolić, M.; Armaković, S.; Armaković, S.; Rodić, M.; Višnjevac, A.; Padrón, J. M.; Todorović, T. R.; Filipović, N. R. Structural, Antioxidant, Antiproliferative and In‒silico Study of Pyridine-Based Hydrazonyl‒selenazoles and Their Sulphur Isosteres. Journal of Molecular Structure 2021, 1240, 130512. https://doi.org/10.1016/j.molstruc.2021.130512." in Journal of Molecular Structure (2021).

Structural, antioxidant, antiproliferative and in‒silico study of pyridine-based hydrazonyl‒selenazoles and their sulphur isosteres

Araškov, Jovana B.; Nikolić, Milan; Armaković, Stevan; Armaković, Sanja; Rodić, Marko; Višnjevac, Aleksandar; Padrón, José M.; Todorović, Tamara R.; Filipović, Nenad R.

(Elsevier, 2021)

TY  - JOUR
AU  - Araškov, Jovana B.
AU  - Nikolić, Milan
AU  - Armaković, Stevan
AU  - Armaković, Sanja
AU  - Rodić, Marko
AU  - Višnjevac, Aleksandar
AU  - Padrón, José M.
AU  - Todorović, Tamara R.
AU  - Filipović, Nenad R.
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S0022286021006451
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4539
AB  - To evaluate the impact of chalcogen atom type, we performed a comparative study of antioxidant capacity and antiproliferative activity of a focused library of three pyridine-based hydrazonyl-1,3-selenazoles and their sulfur isosteres in five antioxidant assays and in six human solid tumor cell lines, respectively. In-silico calculations were further used to check pharmacokinetic profiles of investigated compounds such as drug-likeness parameters and interaction with water. Generally, selenium compounds appear to be more potent in comparison to sulfur isosteres in the performed essays.
PB  - Elsevier
T2  - Journal of Molecular Structure
T1  - Structural, antioxidant, antiproliferative and in‒silico study of pyridine-based hydrazonyl‒selenazoles and their sulphur isosteres
VL  - 1240
SP  - 130512
DO  - 10.1016/j.molstruc.2021.130512
ER  - 
@article{
author = "Araškov, Jovana B. and Nikolić, Milan and Armaković, Stevan and Armaković, Sanja and Rodić, Marko and Višnjevac, Aleksandar and Padrón, José M. and Todorović, Tamara R. and Filipović, Nenad R.",
year = "2021",
abstract = "To evaluate the impact of chalcogen atom type, we performed a comparative study of antioxidant capacity and antiproliferative activity of a focused library of three pyridine-based hydrazonyl-1,3-selenazoles and their sulfur isosteres in five antioxidant assays and in six human solid tumor cell lines, respectively. In-silico calculations were further used to check pharmacokinetic profiles of investigated compounds such as drug-likeness parameters and interaction with water. Generally, selenium compounds appear to be more potent in comparison to sulfur isosteres in the performed essays.",
publisher = "Elsevier",
journal = "Journal of Molecular Structure",
title = "Structural, antioxidant, antiproliferative and in‒silico study of pyridine-based hydrazonyl‒selenazoles and their sulphur isosteres",
volume = "1240",
pages = "130512",
doi = "10.1016/j.molstruc.2021.130512"
}
Araškov, J. B., Nikolić, M., Armaković, S., Armaković, S., Rodić, M., Višnjevac, A., Padrón, J. M., Todorović, T. R.,& Filipović, N. R.. (2021). Structural, antioxidant, antiproliferative and in‒silico study of pyridine-based hydrazonyl‒selenazoles and their sulphur isosteres. in Journal of Molecular Structure
Elsevier., 1240, 130512.
https://doi.org/10.1016/j.molstruc.2021.130512
Araškov JB, Nikolić M, Armaković S, Armaković S, Rodić M, Višnjevac A, Padrón JM, Todorović TR, Filipović NR. Structural, antioxidant, antiproliferative and in‒silico study of pyridine-based hydrazonyl‒selenazoles and their sulphur isosteres. in Journal of Molecular Structure. 2021;1240:130512.
doi:10.1016/j.molstruc.2021.130512 .
Araškov, Jovana B., Nikolić, Milan, Armaković, Stevan, Armaković, Sanja, Rodić, Marko, Višnjevac, Aleksandar, Padrón, José M., Todorović, Tamara R., Filipović, Nenad R., "Structural, antioxidant, antiproliferative and in‒silico study of pyridine-based hydrazonyl‒selenazoles and their sulphur isosteres" in Journal of Molecular Structure, 1240 (2021):130512,
https://doi.org/10.1016/j.molstruc.2021.130512 . .
8
1

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",
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. in International Journal of Biological Macromolecules
Elsevier., 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. in International Journal of Biological Macromolecules. 2020;154:142-149.
doi:10.1016/j.ijbiomac.2020.03.119 .
Gligorijević, Nikola, Vasović, Tamara, Lević, Steva M., Miljević, Čedo, Nedić, Olgica, Nikolić, Milan, "Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation" in International Journal of Biological Macromolecules, 154 (2020):142-149,
https://doi.org/10.1016/j.ijbiomac.2020.03.119 . .
2
2
3

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",
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. in International Journal of Biological Macromolecules
Elsevier., 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. in International Journal of Biological Macromolecules. 2020;154:142-149.
doi:10.1016/j.ijbiomac.2020.03.119 .
Gligorijević, Nikola, Vasović, Tamara, Lević, Steva M., Miljević, Čedo, Nedić, Olgica, Nikolić, Milan, "Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation" in International Journal of Biological Macromolecules, 154 (2020):142-149,
https://doi.org/10.1016/j.ijbiomac.2020.03.119 . .
2
2
3

Позитрон - 20

Savić, Slađana; Jakovljević, Danijel; Holik, Ana-Andrea; Šišaković, Isidora; Milenković, Tamara; Kravljanac, Pavle; Nikolić, Milan

(Универзитет у Београду – Хемијски факултет, 2020)

TY  - GEN
AU  - Savić, Slađana
AU  - Jakovljević, Danijel
AU  - Holik, Ana-Andrea
AU  - Šišaković, Isidora
AU  - Milenković, Tamara
AU  - Kravljanac, Pavle
AU  - Nikolić, Milan
PY  - 2020
UR  - http://chem.bg.ac.rs/studorg/
UR  - https://www.facebook.com/pozitroncasopis/
UR  - https://www.instagram.com/pozitroncasopis/
UR  - pozitron@chem.bg.ac.rs
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4122
AB  - Представљамо вам преглед важних дешавања на Хемијском факултету у протекла три месеца, међу које се убраја и избор новог декана, проф. др Горана Роглића. Како су недеље иза нас и даље обележене пандемијом, доносимо вам приче којима је управо то заједничко. Читајте како су се снашли овогодишњи дипломци, о КОВИД пројекту на Катедри за биохемију, али и о томе шта нас чека у предстојећем семестру у оквиру онлајн наставе (упознајте платформу Teams). О алумнистима сте већ чули, и овог пута вам доносимо још један занимљив разговор. У претходном броју смо започели причу о томе шта је потребно да постанете теоретичар завере, а други део интерјвуа са др Оливером Тошковићем можете прочитати у овом броју. Писали сте нам! Ако се питате шта је то микроинкапсулација или како су повезани уметност и хемија, ово издање часописа има одговоре за вас. Један недавно дипломирани хемичар дели са нама своје искуство о студирању на Хемијском факултету. Доцент др Милан Николић започиње могућу нову рубрику у којој упознајемо професоре и асистенте кроз музику коју слушају.
PB  - Универзитет у Београду – Хемијски факултет
T1  - Позитрон - 20
VL  - 20
SP  - 1
EP  - 28
ER  - 
@misc{
author = "Savić, Slađana and Jakovljević, Danijel and Holik, Ana-Andrea and Šišaković, Isidora and Milenković, Tamara and Kravljanac, Pavle and Nikolić, Milan",
year = "2020",
abstract = "Представљамо вам преглед важних дешавања на Хемијском факултету у протекла три месеца, међу које се убраја и избор новог декана, проф. др Горана Роглића. Како су недеље иза нас и даље обележене пандемијом, доносимо вам приче којима је управо то заједничко. Читајте како су се снашли овогодишњи дипломци, о КОВИД пројекту на Катедри за биохемију, али и о томе шта нас чека у предстојећем семестру у оквиру онлајн наставе (упознајте платформу Teams). О алумнистима сте већ чули, и овог пута вам доносимо још један занимљив разговор. У претходном броју смо започели причу о томе шта је потребно да постанете теоретичар завере, а други део интерјвуа са др Оливером Тошковићем можете прочитати у овом броју. Писали сте нам! Ако се питате шта је то микроинкапсулација или како су повезани уметност и хемија, ово издање часописа има одговоре за вас. Један недавно дипломирани хемичар дели са нама своје искуство о студирању на Хемијском факултету. Доцент др Милан Николић започиње могућу нову рубрику у којој упознајемо професоре и асистенте кроз музику коју слушају.",
publisher = "Универзитет у Београду – Хемијски факултет",
title = "Позитрон - 20",
volume = "20",
pages = "1-28"
}
Savić, S., Jakovljević, D., Holik, A., Šišaković, I., Milenković, T., Kravljanac, P.,& Nikolić, M.. (2020). Позитрон - 20. 
Универзитет у Београду – Хемијски факултет., 20, 1-28.
Savić S, Jakovljević D, Holik A, Šišaković I, Milenković T, Kravljanac P, Nikolić M. Позитрон - 20. 2020;20:1-28..
Savić, Slađana, Jakovljević, Danijel, Holik, Ana-Andrea, Šišaković, Isidora, Milenković, Tamara, Kravljanac, Pavle, Nikolić, Milan, "Позитрон - 20", 20 (2020):1-28.

Characterisation and the effects of bilirubin binding to human fibrinogen

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

(2019)

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

Characterisation and the effects of bilirubin binding to human fibrinogen

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

(2019)

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

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

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

(2019)

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

Computational Analysis of Non-covalent Interactions in Phycocyanin Subunit Interfaces

Breberina, Luka M.; Zlatović, Mario; Nikolić, Milan; Stojanović, Srđan Đ.

(Willey, 2019)

TY  - JOUR
AU  - Breberina, Luka M.
AU  - Zlatović, Mario
AU  - Nikolić, Milan
AU  - Stojanović, Srđan Đ.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3790
AB  - Protein-protein interactions are an important phenomenon in biological processes and functions. We used the manually curated non-redundant dataset of 118 phycocyanin interfaces to gain additional insight into this phenomenon using a robust inter-atomic non-covalent interaction analyzing tool PPCheck. Our observations indicate that there is a relatively high composition of hydrophobic residues at the interfaces. Most of the interface residues are clustered at the middle of the range which we call “standard-size” interfaces. Furthermore, the multiple interaction patterns founded in the present study indicate that more than half of the residues involved in these interactions participate in multiple and water-bridged hydrogen bonds. Thus, hydrogen bonds contribute maximally towards the stability of protein-protein complexes. The analysis shows that hydrogen bond energies contribute to about 88 % to the total energy and it also increases with interface size. Van der Waals (vdW) energy contributes to 9.3 %±1.7 % on average in these complexes. Moreover, there is about 1.9 %±1.5 % contribution by electrostatic energy. Nevertheless, the role by vdW and electrostatic energy could not be ignored in interface binding. Results show that the total binding energy is more for large phycocyanin interfaces. The normalized energy per residue was less than −16 kJ mol−1, while most of them have energy in the range from −6 to −14 kJ mol−1. The non-covalent interacting residues in these proteins were found to be highly conserved. Obtained results might contribute to the understanding of structural stability of this class of evolutionary essential proteins with increased practical application and future designs of novel protein-bioactive compound interactions.
PB  - Willey
T2  - Molecular Informatics
T1  - Computational Analysis of Non-covalent Interactions in Phycocyanin Subunit Interfaces
VL  - 38
IS  - 11-12
SP  - 1800145
DO  - 10.1002/minf.201800145
ER  - 
@article{
author = "Breberina, Luka M. and Zlatović, Mario and Nikolić, Milan and Stojanović, Srđan Đ.",
year = "2019",
abstract = "Protein-protein interactions are an important phenomenon in biological processes and functions. We used the manually curated non-redundant dataset of 118 phycocyanin interfaces to gain additional insight into this phenomenon using a robust inter-atomic non-covalent interaction analyzing tool PPCheck. Our observations indicate that there is a relatively high composition of hydrophobic residues at the interfaces. Most of the interface residues are clustered at the middle of the range which we call “standard-size” interfaces. Furthermore, the multiple interaction patterns founded in the present study indicate that more than half of the residues involved in these interactions participate in multiple and water-bridged hydrogen bonds. Thus, hydrogen bonds contribute maximally towards the stability of protein-protein complexes. The analysis shows that hydrogen bond energies contribute to about 88 % to the total energy and it also increases with interface size. Van der Waals (vdW) energy contributes to 9.3 %±1.7 % on average in these complexes. Moreover, there is about 1.9 %±1.5 % contribution by electrostatic energy. Nevertheless, the role by vdW and electrostatic energy could not be ignored in interface binding. Results show that the total binding energy is more for large phycocyanin interfaces. The normalized energy per residue was less than −16 kJ mol−1, while most of them have energy in the range from −6 to −14 kJ mol−1. The non-covalent interacting residues in these proteins were found to be highly conserved. Obtained results might contribute to the understanding of structural stability of this class of evolutionary essential proteins with increased practical application and future designs of novel protein-bioactive compound interactions.",
publisher = "Willey",
journal = "Molecular Informatics",
title = "Computational Analysis of Non-covalent Interactions in Phycocyanin Subunit Interfaces",
volume = "38",
number = "11-12",
pages = "1800145",
doi = "10.1002/minf.201800145"
}
Breberina, L. M., Zlatović, M., Nikolić, M.,& Stojanović, S. Đ.. (2019). Computational Analysis of Non-covalent Interactions in Phycocyanin Subunit Interfaces. in Molecular Informatics
Willey., 38(11-12), 1800145.
https://doi.org/10.1002/minf.201800145
Breberina LM, Zlatović M, Nikolić M, Stojanović SĐ. Computational Analysis of Non-covalent Interactions in Phycocyanin Subunit Interfaces. in Molecular Informatics. 2019;38(11-12):1800145.
doi:10.1002/minf.201800145 .
Breberina, Luka M., Zlatović, Mario, Nikolić, Milan, Stojanović, Srđan Đ., "Computational Analysis of Non-covalent Interactions in Phycocyanin Subunit Interfaces" in Molecular Informatics, 38, no. 11-12 (2019):1800145,
https://doi.org/10.1002/minf.201800145 . .

Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content

Uzelac, Tamara N.; Nikolić-Kokić, Aleksandra; Spasić, Snežana; Mačvanin, Mirjana T.; Nikolić, Milan; Mandić, Ljuba M.; Jovanović, Vesna B.

(2019)

TY  - JOUR
AU  - Uzelac, Tamara N.
AU  - Nikolić-Kokić, Aleksandra
AU  - Spasić, Snežana
AU  - Mačvanin, Mirjana T.
AU  - Nikolić, Milan
AU  - Mandić, Ljuba M.
AU  - Jovanović, Vesna B.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3333
AB  - Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of its reactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.
T2  - Chemico-Biological Interactions
T1  - Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content
VL  - 311
SP  - 1
EP  - 7
DO  - 10.1016/j.cbi.2019.108787
ER  - 
@article{
author = "Uzelac, Tamara N. and Nikolić-Kokić, Aleksandra and Spasić, Snežana and Mačvanin, Mirjana T. and Nikolić, Milan and Mandić, Ljuba M. and Jovanović, Vesna B.",
year = "2019",
abstract = "Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of its reactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.",
journal = "Chemico-Biological Interactions",
title = "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content",
volume = "311",
pages = "1-7",
doi = "10.1016/j.cbi.2019.108787"
}
Uzelac, T. N., Nikolić-Kokić, A., Spasić, S., Mačvanin, M. T., Nikolić, M., Mandić, L. M.,& Jovanović, V. B.. (2019). Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions, 311, 1-7.
https://doi.org/10.1016/j.cbi.2019.108787
Uzelac TN, Nikolić-Kokić A, Spasić S, Mačvanin MT, Nikolić M, Mandić LM, Jovanović VB. Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions. 2019;311:1-7.
doi:10.1016/j.cbi.2019.108787 .
Uzelac, Tamara N., Nikolić-Kokić, Aleksandra, Spasić, Snežana, Mačvanin, Mirjana T., Nikolić, Milan, Mandić, Ljuba M., Jovanović, Vesna B., "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content" in Chemico-Biological Interactions, 311 (2019):1-7,
https://doi.org/10.1016/j.cbi.2019.108787 . .

Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. B. Opposite Clozapine and Ziprasidone Effects on the Reactivity of Plasma Albumin SH-Group Are the Consequence of Their Different Binding Properties Dependent on Protein Fatty Acids Content. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787

Uzelac, Tamara N.; Nikolić-Kokić, Aleksandra; Spasić, Snežana; Mačvanin, Mirjana T.; Nikolić, Milan; Mandić, Ljuba M.; Jovanović, Vesna B.

(2019)

TY  - DATA
AU  - Uzelac, Tamara N.
AU  - Nikolić-Kokić, Aleksandra
AU  - Spasić, Snežana
AU  - Mačvanin, Mirjana T.
AU  - Nikolić, Milan
AU  - Mandić, Ljuba M.
AU  - Jovanović, Vesna B.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3335
T2  - Chemico-Biological Interactions
T1  - Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. B. Opposite Clozapine and Ziprasidone Effects on the Reactivity of Plasma Albumin SH-Group Are the Consequence of Their Different Binding Properties Dependent on Protein Fatty Acids Content. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787
ER  - 
@misc{
author = "Uzelac, Tamara N. and Nikolić-Kokić, Aleksandra and Spasić, Snežana and Mačvanin, Mirjana T. and Nikolić, Milan and Mandić, Ljuba M. and Jovanović, Vesna B.",
year = "2019",
journal = "Chemico-Biological Interactions",
title = "Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. B. Opposite Clozapine and Ziprasidone Effects on the Reactivity of Plasma Albumin SH-Group Are the Consequence of Their Different Binding Properties Dependent on Protein Fatty Acids Content. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787"
}
Uzelac, T. N., Nikolić-Kokić, A., Spasić, S., Mačvanin, M. T., Nikolić, M., Mandić, L. M.,& Jovanović, V. B.. (2019). Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. B. Opposite Clozapine and Ziprasidone Effects on the Reactivity of Plasma Albumin SH-Group Are the Consequence of Their Different Binding Properties Dependent on Protein Fatty Acids Content. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787. in Chemico-Biological Interactions.
Uzelac TN, Nikolić-Kokić A, Spasić S, Mačvanin MT, Nikolić M, Mandić LM, Jovanović VB. Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. B. Opposite Clozapine and Ziprasidone Effects on the Reactivity of Plasma Albumin SH-Group Are the Consequence of Their Different Binding Properties Dependent on Protein Fatty Acids Content. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787. in Chemico-Biological Interactions. 2019;..
Uzelac, Tamara N., Nikolić-Kokić, Aleksandra, Spasić, Snežana, Mačvanin, Mirjana T., Nikolić, Milan, Mandić, Ljuba M., Jovanović, Vesna B., "Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. B. Opposite Clozapine and Ziprasidone Effects on the Reactivity of Plasma Albumin SH-Group Are the Consequence of Their Different Binding Properties Dependent on Protein Fatty Acids Content. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787" in Chemico-Biological Interactions (2019).

Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content

Uzelac, Tamara N.; Nikolić-Kokić, Aleksandra; Spasić, Snežana; Mačvanin, Mirjana T.; Nikolić, Milan; Mandić, Ljuba M.; Jovanović, Vesna B.

(Elsevier, 2019)

TY  - JOUR
AU  - Uzelac, Tamara N.
AU  - Nikolić-Kokić, Aleksandra
AU  - Spasić, Snežana
AU  - Mačvanin, Mirjana T.
AU  - Nikolić, Milan
AU  - Mandić, Ljuba M.
AU  - Jovanović, Vesna B.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3865
AB  - Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of its reactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.
PB  - Elsevier
T2  - Chemico-Biological Interactions
T1  - Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content
VL  - 311
IS  - 108787
DO  - 10.1016/j.cbi.2019.108787
ER  - 
@article{
author = "Uzelac, Tamara N. and Nikolić-Kokić, Aleksandra and Spasić, Snežana and Mačvanin, Mirjana T. and Nikolić, Milan and Mandić, Ljuba M. and Jovanović, Vesna B.",
year = "2019",
abstract = "Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of its reactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.",
publisher = "Elsevier",
journal = "Chemico-Biological Interactions",
title = "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content",
volume = "311",
number = "108787",
doi = "10.1016/j.cbi.2019.108787"
}
Uzelac, T. N., Nikolić-Kokić, A., Spasić, S., Mačvanin, M. T., Nikolić, M., Mandić, L. M.,& Jovanović, V. B.. (2019). Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions
Elsevier., 311(108787).
https://doi.org/10.1016/j.cbi.2019.108787
Uzelac TN, Nikolić-Kokić A, Spasić S, Mačvanin MT, Nikolić M, Mandić LM, Jovanović VB. Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions. 2019;311(108787).
doi:10.1016/j.cbi.2019.108787 .
Uzelac, Tamara N., Nikolić-Kokić, Aleksandra, Spasić, Snežana, Mačvanin, Mirjana T., Nikolić, Milan, Mandić, Ljuba M., Jovanović, Vesna B., "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content" in Chemico-Biological Interactions, 311, no. 108787 (2019),
https://doi.org/10.1016/j.cbi.2019.108787 . .

Pd(II) complexes with N-heteroaromatic hydrazone ligands: Anticancer activity, in silico and experimental target identification

Bjelogrlić, Snežana K.; Todorović, Tamara; Kojić, Milan O.; Senćanski, Milan; Nikolić, Milan; Višnjevac, Aleksandar; Araškov, Jovana; Miljković, Marija; Muller, Christian D.; Filipović, Nenad R.

(Elsevier, 2019)

TY  - JOUR
AU  - Bjelogrlić, Snežana K.
AU  - Todorović, Tamara
AU  - Kojić, Milan O.
AU  - Senćanski, Milan
AU  - Nikolić, Milan
AU  - Višnjevac, Aleksandar
AU  - Araškov, Jovana
AU  - Miljković, Marija
AU  - Muller, Christian D.
AU  - Filipović, Nenad R.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3318
AB  - Anticancer activity of Pd complexes 1–5 with bidentate N-heteroaromatic hydrazone ligands was investigated on human acute monocytic leukemia (THP-1; cells in a suspension) and human mammary adenocarcinoma (MCF-7; two-dimensional layer and three-dimensional spheroid tumor model) cell lines. For the Pd(II) complexes with condensation products of ethyl hydrazainoacetate and quinoline-8-carboxaldehyde (complex 1) and 2-formylpyridine (complex 3), for which apoptosis was determined as a mechanism of anticancer activity, further investigation revealed that they arrest the cell cycle in G0/G1 phase, induce generation of reactive oxygen species and inhibit Topoisomerase I in vitro. In silico studies corroborate experimental findings that these complexes show topoisomerase inhibition activity in the micromolar range and indicate binding to a DNA's minor groove as another potential target. Based on the results obtained by circular dichroism and fluorescence spectroscopy measurements, the most active complexes are suitable to be delivered to a blood stream via human serum albumin.
PB  - Elsevier
T2  - Journal of Inorganic Biochemistry
T1  - Pd(II) complexes with N-heteroaromatic hydrazone ligands: Anticancer activity, in silico and experimental target identification
VL  - 199
DO  - 10.1016/j.jinorgbio.2019.110758
ER  - 
@article{
author = "Bjelogrlić, Snežana K. and Todorović, Tamara and Kojić, Milan O. and Senćanski, Milan and Nikolić, Milan and Višnjevac, Aleksandar and Araškov, Jovana and Miljković, Marija and Muller, Christian D. and Filipović, Nenad R.",
year = "2019",
abstract = "Anticancer activity of Pd complexes 1–5 with bidentate N-heteroaromatic hydrazone ligands was investigated on human acute monocytic leukemia (THP-1; cells in a suspension) and human mammary adenocarcinoma (MCF-7; two-dimensional layer and three-dimensional spheroid tumor model) cell lines. For the Pd(II) complexes with condensation products of ethyl hydrazainoacetate and quinoline-8-carboxaldehyde (complex 1) and 2-formylpyridine (complex 3), for which apoptosis was determined as a mechanism of anticancer activity, further investigation revealed that they arrest the cell cycle in G0/G1 phase, induce generation of reactive oxygen species and inhibit Topoisomerase I in vitro. In silico studies corroborate experimental findings that these complexes show topoisomerase inhibition activity in the micromolar range and indicate binding to a DNA's minor groove as another potential target. Based on the results obtained by circular dichroism and fluorescence spectroscopy measurements, the most active complexes are suitable to be delivered to a blood stream via human serum albumin.",
publisher = "Elsevier",
journal = "Journal of Inorganic Biochemistry",
title = "Pd(II) complexes with N-heteroaromatic hydrazone ligands: Anticancer activity, in silico and experimental target identification",
volume = "199",
doi = "10.1016/j.jinorgbio.2019.110758"
}
Bjelogrlić, S. K., Todorović, T., Kojić, M. O., Senćanski, M., Nikolić, M., Višnjevac, A., Araškov, J., Miljković, M., Muller, C. D.,& Filipović, N. R.. (2019). Pd(II) complexes with N-heteroaromatic hydrazone ligands: Anticancer activity, in silico and experimental target identification. in Journal of Inorganic Biochemistry
Elsevier., 199.
https://doi.org/10.1016/j.jinorgbio.2019.110758
Bjelogrlić SK, Todorović T, Kojić MO, Senćanski M, Nikolić M, Višnjevac A, Araškov J, Miljković M, Muller CD, Filipović NR. Pd(II) complexes with N-heteroaromatic hydrazone ligands: Anticancer activity, in silico and experimental target identification. in Journal of Inorganic Biochemistry. 2019;199.
doi:10.1016/j.jinorgbio.2019.110758 .
Bjelogrlić, Snežana K., Todorović, Tamara, Kojić, Milan O., Senćanski, Milan, Nikolić, Milan, Višnjevac, Aleksandar, Araškov, Jovana, Miljković, Marija, Muller, Christian D., Filipović, Nenad R., "Pd(II) complexes with N-heteroaromatic hydrazone ligands: Anticancer activity, in silico and experimental target identification" in Journal of Inorganic Biochemistry, 199 (2019),
https://doi.org/10.1016/j.jinorgbio.2019.110758 . .
5
5
4

Supplementary data for the article: Bjelogrlić, S. K.; Todorović, T. R.; Kojić, M.; Senćanski, M.; Nikolić, M.; Višnjevac, A.; Araškov, J.; Miljković, M.; Muller, C. D.; Filipović, N. R. Pd(II) Complexes with N-Heteroaromatic Hydrazone Ligands: Anticancer Activity, in Silico and Experimental Target Identification. Journal of Inorganic Biochemistry 2019, 199. https://doi.org/10.1016/j.jinorgbio.2019.110758

Bjelogrlić, Snežana K.; Todorović, Tamara; Kojić, Milan O.; Senćanski, Milan; Nikolić, Milan; Višnjevac, Aleksandar; Araškov, Jovana; Miljković, Marija; Muller, Christian D.; Filipović, Nenad R.

(Elsevier, 2019)

TY  - DATA
AU  - Bjelogrlić, Snežana K.
AU  - Todorović, Tamara
AU  - Kojić, Milan O.
AU  - Senćanski, Milan
AU  - Nikolić, Milan
AU  - Višnjevac, Aleksandar
AU  - Araškov, Jovana
AU  - Miljković, Marija
AU  - Muller, Christian D.
AU  - Filipović, Nenad R.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3319
PB  - Elsevier
T2  - Journal of Inorganic Biochemistry
T1  - Supplementary data for the article: Bjelogrlić, S. K.; Todorović, T. R.; Kojić, M.; Senćanski, M.; Nikolić, M.; Višnjevac, A.; Araškov, J.; Miljković, M.; Muller, C. D.; Filipović, N. R. Pd(II) Complexes with N-Heteroaromatic Hydrazone Ligands: Anticancer Activity, in Silico and Experimental Target Identification. Journal of Inorganic Biochemistry 2019, 199. https://doi.org/10.1016/j.jinorgbio.2019.110758
ER  - 
@misc{
author = "Bjelogrlić, Snežana K. and Todorović, Tamara and Kojić, Milan O. and Senćanski, Milan and Nikolić, Milan and Višnjevac, Aleksandar and Araškov, Jovana and Miljković, Marija and Muller, Christian D. and Filipović, Nenad R.",
year = "2019",
publisher = "Elsevier",
journal = "Journal of Inorganic Biochemistry",
title = "Supplementary data for the article: Bjelogrlić, S. K.; Todorović, T. R.; Kojić, M.; Senćanski, M.; Nikolić, M.; Višnjevac, A.; Araškov, J.; Miljković, M.; Muller, C. D.; Filipović, N. R. Pd(II) Complexes with N-Heteroaromatic Hydrazone Ligands: Anticancer Activity, in Silico and Experimental Target Identification. Journal of Inorganic Biochemistry 2019, 199. https://doi.org/10.1016/j.jinorgbio.2019.110758"
}
Bjelogrlić, S. K., Todorović, T., Kojić, M. O., Senćanski, M., Nikolić, M., Višnjevac, A., Araškov, J., Miljković, M., Muller, C. D.,& Filipović, N. R.. (2019). Supplementary data for the article: Bjelogrlić, S. K.; Todorović, T. R.; Kojić, M.; Senćanski, M.; Nikolić, M.; Višnjevac, A.; Araškov, J.; Miljković, M.; Muller, C. D.; Filipović, N. R. Pd(II) Complexes with N-Heteroaromatic Hydrazone Ligands: Anticancer Activity, in Silico and Experimental Target Identification. Journal of Inorganic Biochemistry 2019, 199. https://doi.org/10.1016/j.jinorgbio.2019.110758. in Journal of Inorganic Biochemistry
Elsevier..
Bjelogrlić SK, Todorović T, Kojić MO, Senćanski M, Nikolić M, Višnjevac A, Araškov J, Miljković M, Muller CD, Filipović NR. Supplementary data for the article: Bjelogrlić, S. K.; Todorović, T. R.; Kojić, M.; Senćanski, M.; Nikolić, M.; Višnjevac, A.; Araškov, J.; Miljković, M.; Muller, C. D.; Filipović, N. R. Pd(II) Complexes with N-Heteroaromatic Hydrazone Ligands: Anticancer Activity, in Silico and Experimental Target Identification. Journal of Inorganic Biochemistry 2019, 199. https://doi.org/10.1016/j.jinorgbio.2019.110758. in Journal of Inorganic Biochemistry. 2019;..
Bjelogrlić, Snežana K., Todorović, Tamara, Kojić, Milan O., Senćanski, Milan, Nikolić, Milan, Višnjevac, Aleksandar, Araškov, Jovana, Miljković, Marija, Muller, Christian D., Filipović, Nenad R., "Supplementary data for the article: Bjelogrlić, S. K.; Todorović, T. R.; Kojić, M.; Senćanski, M.; Nikolić, M.; Višnjevac, A.; Araškov, J.; Miljković, M.; Muller, C. D.; Filipović, N. R. Pd(II) Complexes with N-Heteroaromatic Hydrazone Ligands: Anticancer Activity, in Silico and Experimental Target Identification. Journal of Inorganic Biochemistry 2019, 199. https://doi.org/10.1016/j.jinorgbio.2019.110758" in Journal of Inorganic Biochemistry (2019).

Use of cyclic voltammetry to determine the antioxidant capacity of berry fruits: Correlation with spectrophotometric assays

Nikolić, Milan; Pavlović, Aleksandra; Mitić, S.S.; Tošić, S.B.; Mitić, M.N.; Kaličanin, B.M.; Manojlović, Dragan D.; Stanković, Dalibor

(INT SOC HORTICULTURAL SCIENCE-ISHS, 2019)

TY  - JOUR
AU  - Nikolić, Milan
AU  - Pavlović, Aleksandra
AU  - Mitić, S.S.
AU  - Tošić, S.B.
AU  - Mitić, M.N.
AU  - Kaličanin, B.M.
AU  - Manojlović, Dragan D.
AU  - Stanković, Dalibor
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3315
AB  - Background of the study – Among fruits, berry fruits contain a very large complex of chemical compounds that are responsible for their antioxidant properties. As far as we know there is no data available from cyclic voltammetry studies of berry fruits. Objectives – The first objective of the present work was to investigate the electrochemical properties of antioxidants present in four types of berry fruits: strawberries, blackberries, blueberries and red raspberries. The second objective was to establish the correlation between antioxidant capacities obtained from cyclic voltammograms with those obtained using spectrophotometric techniques. Methods – Evaluation of antioxidant activity of 15 berry samples (strawberry, blackberry, blueberry and raspberry) has been carried out using cyclic voltammetry (CV). CVs were taken in the potential range between 0 mV and 800 mV with a scan rate of 100 mV s-1. Results – A pronounced anodic current peak observed between 0.524 V and 0.540 V in all analyzed berry samples can be ascribed to anthocyanins, which are the major contributors to the antioxidant capacity of investigated berries. Results obtained from CVs were compared with those obtained by using DPPH, ABTS, FRAP and RP assays. ACI parameters were determined for each berry sample by assigning all the assays an equal weight. According to obtained results, the highest ACI had blueberry samples, followed by blackberry, raspberry and strawberry samples. Also, high positive correlations were found between antioxidant capacities deduced from CVs with those obtained using FRAP (R2 = 0.8630, p = 0.0006), RP (R2 = 0.7426, p = 0.0004), DPPH (R2 = 0.7680, p = 0.0001) and ABTS (R2 = 0.8710, p = 0.000002). In addition, high positive correlations were also found between total phenols, flavonoids, anthocyanins and CV antioxidant capacity (R2 = 0.8091, p = 0.0005; R2 = 0.8341, p = 0.0002; R2 = 0.7163, p = 0.0007), respectively. Conclusion – Obtained results showed that the cyclic voltammetry is a suitable method for the determination of the reducing capacity based on the electrochemical properties of compounds under the test.
PB  - INT SOC HORTICULTURAL SCIENCE-ISHS
T2  - European Journal of Horticultural Science
T1  - Use of cyclic voltammetry to determine the antioxidant capacity of berry fruits: Correlation with spectrophotometric assays
VL  - 84
IS  - 3
SP  - 152
EP  - 160
DO  - 10.17660/eJHS.2019/84.3.5
ER  - 
@article{
author = "Nikolić, Milan and Pavlović, Aleksandra and Mitić, S.S. and Tošić, S.B. and Mitić, M.N. and Kaličanin, B.M. and Manojlović, Dragan D. and Stanković, Dalibor",
year = "2019",
abstract = "Background of the study – Among fruits, berry fruits contain a very large complex of chemical compounds that are responsible for their antioxidant properties. As far as we know there is no data available from cyclic voltammetry studies of berry fruits. Objectives – The first objective of the present work was to investigate the electrochemical properties of antioxidants present in four types of berry fruits: strawberries, blackberries, blueberries and red raspberries. The second objective was to establish the correlation between antioxidant capacities obtained from cyclic voltammograms with those obtained using spectrophotometric techniques. Methods – Evaluation of antioxidant activity of 15 berry samples (strawberry, blackberry, blueberry and raspberry) has been carried out using cyclic voltammetry (CV). CVs were taken in the potential range between 0 mV and 800 mV with a scan rate of 100 mV s-1. Results – A pronounced anodic current peak observed between 0.524 V and 0.540 V in all analyzed berry samples can be ascribed to anthocyanins, which are the major contributors to the antioxidant capacity of investigated berries. Results obtained from CVs were compared with those obtained by using DPPH, ABTS, FRAP and RP assays. ACI parameters were determined for each berry sample by assigning all the assays an equal weight. According to obtained results, the highest ACI had blueberry samples, followed by blackberry, raspberry and strawberry samples. Also, high positive correlations were found between antioxidant capacities deduced from CVs with those obtained using FRAP (R2 = 0.8630, p = 0.0006), RP (R2 = 0.7426, p = 0.0004), DPPH (R2 = 0.7680, p = 0.0001) and ABTS (R2 = 0.8710, p = 0.000002). In addition, high positive correlations were also found between total phenols, flavonoids, anthocyanins and CV antioxidant capacity (R2 = 0.8091, p = 0.0005; R2 = 0.8341, p = 0.0002; R2 = 0.7163, p = 0.0007), respectively. Conclusion – Obtained results showed that the cyclic voltammetry is a suitable method for the determination of the reducing capacity based on the electrochemical properties of compounds under the test.",
publisher = "INT SOC HORTICULTURAL SCIENCE-ISHS",
journal = "European Journal of Horticultural Science",
title = "Use of cyclic voltammetry to determine the antioxidant capacity of berry fruits: Correlation with spectrophotometric assays",
volume = "84",
number = "3",
pages = "152-160",
doi = "10.17660/eJHS.2019/84.3.5"
}
Nikolić, M., Pavlović, A., Mitić, S.S., Tošić, S.B., Mitić, M.N., Kaličanin, B.M., Manojlović, D. D.,& Stanković, D.. (2019). Use of cyclic voltammetry to determine the antioxidant capacity of berry fruits: Correlation with spectrophotometric assays. in European Journal of Horticultural Science
INT SOC HORTICULTURAL SCIENCE-ISHS., 84(3), 152-160.
https://doi.org/10.17660/eJHS.2019/84.3.5
Nikolić M, Pavlović A, Mitić S, Tošić S, Mitić M, Kaličanin B, Manojlović DD, Stanković D. Use of cyclic voltammetry to determine the antioxidant capacity of berry fruits: Correlation with spectrophotometric assays. in European Journal of Horticultural Science. 2019;84(3):152-160.
doi:10.17660/eJHS.2019/84.3.5 .
Nikolić, Milan, Pavlović, Aleksandra, Mitić, S.S., Tošić, S.B., Mitić, M.N., Kaličanin, B.M., Manojlović, Dragan D., Stanković, Dalibor, "Use of cyclic voltammetry to determine the antioxidant capacity of berry fruits: Correlation with spectrophotometric assays" in European Journal of Horticultural Science, 84, no. 3 (2019):152-160,
https://doi.org/10.17660/eJHS.2019/84.3.5 . .
1
5
4
4

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  - DATA
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  - 
@misc{
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",
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. in Food Chemistry
Elsevier 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. in 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" in Food Chemistry (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/123456789/3186
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
UR  - Kon_3528
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",
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",
url = "Kon_3528"
}
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. in Food Chemistry
Elsevier Sci Ltd, Oxford., 269, 43-52.
https://doi.org/10.1016/j.foodchem.2018.06.138
Kon_3528
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. in Food Chemistry. 2018;269:43-52.
doi:10.1016/j.foodchem.2018.06.138
Kon_3528 .
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" in Food Chemistry, 269 (2018):43-52,
https://doi.org/10.1016/j.foodchem.2018.06.138 .,
Kon_3528 .
1
3
2
2

Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.; Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099. https://doi.org/10.1016/j.foodchem.2017.07.066

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

(Elsevier, 2018)

TY  - DATA
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana Ž.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3139
PB  - Elsevier
T2  - Food Chemistry
T1  - Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066
ER  - 
@misc{
author = "Minić, Simeon L. and Stanić-Vučinić, Dragana and Radomirović, Mirjana Ž. and Radibratović, Milica and Milčić, Miloš K. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2018",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066"
}
Minić, S. L., Stanić-Vučinić, D., Radomirović, M. Ž., Radibratović, M., Milčić, M. K., Nikolić, M.,& Ćirković-Veličković, T.. (2018). Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066. in Food Chemistry
Elsevier..
Minić SL, Stanić-Vučinić D, Radomirović MŽ, Radibratović M, Milčić MK, Nikolić M, Ćirković-Veličković T. Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066. in Food Chemistry. 2018;..
Minić, Simeon L., Stanić-Vučinić, Dragana, Radomirović, Mirjana Ž., Radibratović, Milica, Milčić, Miloš K., Nikolić, Milan, Ćirković-Veličković, Tanja, "Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066" in Food Chemistry (2018).

Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects

Radomirović, Mirjana Ž.; Minić, Simeon L.; Savković, Nina; Vasović, T.; Nikolić, Milan; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Minić, Simeon L.
AU  - Savković, Nina
AU  - Vasović, T.
AU  - Nikolić, Milan
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2175
PB  - Wiley, Hoboken
C3  - FEBS OPEN BIO
T1  - Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects
VL  - 8
SP  - 97
EP  - 97
UR  - Kon_3506
ER  - 
@conference{
author = "Radomirović, Mirjana Ž. and Minić, Simeon L. and Savković, Nina and Vasović, T. and Nikolić, Milan and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
publisher = "Wiley, Hoboken",
journal = "FEBS OPEN BIO",
title = "Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects",
volume = "8",
pages = "97-97",
url = "Kon_3506"
}
Radomirović, M. Ž., Minić, S. L., Savković, N., Vasović, T., Nikolić, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2018). Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects. in FEBS OPEN BIO
Wiley, Hoboken., 8, 97-97.
Kon_3506
Radomirović MŽ, Minić SL, Savković N, Vasović T, Nikolić M, Stanić-Vučinić D, Ćirković-Veličković T. Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects. in FEBS OPEN BIO. 2018;8:97-97.
Kon_3506 .
Radomirović, Mirjana Ž., Minić, Simeon L., Savković, Nina, Vasović, T., Nikolić, Milan, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects" in FEBS OPEN BIO, 8 (2018):97-97,
Kon_3506 .

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
UR  - Kon_3528
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",
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",
url = "Kon_3528"
}
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. in Food Chemistry
Elsevier Sci Ltd, Oxford., 269, 43-52.
https://doi.org/10.1016/j.foodchem.2018.06.138
Kon_3528
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. in Food Chemistry. 2018;269:43-52.
doi:10.1016/j.foodchem.2018.06.138
Kon_3528 .
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" in Food Chemistry, 269 (2018):43-52,
https://doi.org/10.1016/j.foodchem.2018.06.138 .,
Kon_3528 .
1
3
2
3

Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin

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

(Elsevier, 2018)

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana Ž.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2515
AB  - Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (K-a = 2 x 10(6) M-1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin. (C) 2017 Elsevier Ltd. All rights reserved.
PB  - Elsevier
T2  - Food Chemistry
T1  - Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin
VL  - 239
SP  - 1090
EP  - 1099
DO  - 10.1016/j.foodchem.2017.07.066
UR  - Kon_3331
ER  - 
@article{
author = "Minić, Simeon L. and Stanić-Vučinić, Dragana and Radomirović, Mirjana Ž. and Radibratović, Milica and Milčić, Miloš K. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (K-a = 2 x 10(6) M-1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin. (C) 2017 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin",
volume = "239",
pages = "1090-1099",
doi = "10.1016/j.foodchem.2017.07.066",
url = "Kon_3331"
}
Minić, S. L., Stanić-Vučinić, D., Radomirović, M. Ž., Radibratović, M., Milčić, M. K., Nikolić, M.,& Ćirković-Veličković, T.. (2018). Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. in Food Chemistry
Elsevier., 239, 1090-1099.
https://doi.org/10.1016/j.foodchem.2017.07.066
Kon_3331
Minić SL, Stanić-Vučinić D, Radomirović MŽ, Radibratović M, Milčić MK, Nikolić M, Ćirković-Veličković T. Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. in Food Chemistry. 2018;239:1090-1099.
doi:10.1016/j.foodchem.2017.07.066
Kon_3331 .
Minić, Simeon L., Stanić-Vučinić, Dragana, Radomirović, Mirjana Ž., Radibratović, Milica, Milčić, Miloš K., Nikolić, Milan, Ćirković-Veličković, Tanja, "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin" in Food Chemistry, 239 (2018):1090-1099,
https://doi.org/10.1016/j.foodchem.2017.07.066 .,
Kon_3331 .
19
19
19

Supplementary material for the article: Elshaflu, H.; Todorović, T. R.; Nikolić, M.; Lolić, A.; Višnjevac, A.; Hagenow, S.; Padrón, J. M.; García-Sosa, A. T.; Djordjevic, I. S.; Grubišic, S.; et al. Selenazolyl-Hydrazones as Novel Selective MAO Inhibitors with Antiproliferative and Antioxidant Activities: Experimental and In-Silico Studies. Frontiers in Chemistry 2018, 6 (JUL). https://doi.org/10.3389/fchem.2018.00247

Elshaflu, Hana; Todorović, Tamara; Nikolić, Milan; Lolić, Aleksandar; Višnjevac, Aleksandar; Hagenow, Stefanie; Padrón, José M.; Garcia-Sosa, Alfonso T.; Đorđević, Ivana S.; Grubišić, Sonja; Stark, Holger; Filipović, Nenad R.

(Frontiers Media Sa, Lausanne, 2018)

TY  - DATA
AU  - Elshaflu, Hana
AU  - Todorović, Tamara
AU  - Nikolić, Milan
AU  - Lolić, Aleksandar
AU  - Višnjevac, Aleksandar
AU  - Hagenow, Stefanie
AU  - Padrón, José M.
AU  - Garcia-Sosa, Alfonso T.
AU  - Đorđević, Ivana S.
AU  - Grubišić, Sonja
AU  - Stark, Holger
AU  - Filipović, Nenad R.
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3254
PB  - Frontiers Media Sa, Lausanne
T2  - FRONTIERS IN CHEMISTRY
T1  - Supplementary material for the article: Elshaflu, H.; Todorović, T. R.; Nikolić, M.; Lolić, A.; Višnjevac, A.; Hagenow, S.; Padrón, J. M.; García-Sosa, A. T.; Djordjevic, I. S.; Grubišic, S.; et al. Selenazolyl-Hydrazones as Novel Selective MAO Inhibitors with Antiproliferative and Antioxidant Activities: Experimental and In-Silico Studies. Frontiers in Chemistry 2018, 6 (JUL). https://doi.org/10.3389/fchem.2018.00247
ER  - 
@misc{
author = "Elshaflu, Hana and Todorović, Tamara and Nikolić, Milan and Lolić, Aleksandar and Višnjevac, Aleksandar and Hagenow, Stefanie and Padrón, José M. and Garcia-Sosa, Alfonso T. and Đorđević, Ivana S. and Grubišić, Sonja and Stark, Holger and Filipović, Nenad R.",
year = "2018",
publisher = "Frontiers Media Sa, Lausanne",
journal = "FRONTIERS IN CHEMISTRY",
title = "Supplementary material for the article: Elshaflu, H.; Todorović, T. R.; Nikolić, M.; Lolić, A.; Višnjevac, A.; Hagenow, S.; Padrón, J. M.; García-Sosa, A. T.; Djordjevic, I. S.; Grubišic, S.; et al. Selenazolyl-Hydrazones as Novel Selective MAO Inhibitors with Antiproliferative and Antioxidant Activities: Experimental and In-Silico Studies. Frontiers in Chemistry 2018, 6 (JUL). https://doi.org/10.3389/fchem.2018.00247"
}
Elshaflu, H., Todorović, T., Nikolić, M., Lolić, A., Višnjevac, A., Hagenow, S., Padrón, J. M., Garcia-Sosa, A. T., Đorđević, I. S., Grubišić, S., Stark, H.,& Filipović, N. R.. (2018). Supplementary material for the article: Elshaflu, H.; Todorović, T. R.; Nikolić, M.; Lolić, A.; Višnjevac, A.; Hagenow, S.; Padrón, J. M.; García-Sosa, A. T.; Djordjevic, I. S.; Grubišic, S.; et al. Selenazolyl-Hydrazones as Novel Selective MAO Inhibitors with Antiproliferative and Antioxidant Activities: Experimental and In-Silico Studies. Frontiers in Chemistry 2018, 6 (JUL). https://doi.org/10.3389/fchem.2018.00247. in FRONTIERS IN CHEMISTRY
Frontiers Media Sa, Lausanne..
Elshaflu H, Todorović T, Nikolić M, Lolić A, Višnjevac A, Hagenow S, Padrón JM, Garcia-Sosa AT, Đorđević IS, Grubišić S, Stark H, Filipović NR. Supplementary material for the article: Elshaflu, H.; Todorović, T. R.; Nikolić, M.; Lolić, A.; Višnjevac, A.; Hagenow, S.; Padrón, J. M.; García-Sosa, A. T.; Djordjevic, I. S.; Grubišic, S.; et al. Selenazolyl-Hydrazones as Novel Selective MAO Inhibitors with Antiproliferative and Antioxidant Activities: Experimental and In-Silico Studies. Frontiers in Chemistry 2018, 6 (JUL). https://doi.org/10.3389/fchem.2018.00247. in FRONTIERS IN CHEMISTRY. 2018;..
Elshaflu, Hana, Todorović, Tamara, Nikolić, Milan, Lolić, Aleksandar, Višnjevac, Aleksandar, Hagenow, Stefanie, Padrón, José M., Garcia-Sosa, Alfonso T., Đorđević, Ivana S., Grubišić, Sonja, Stark, Holger, Filipović, Nenad R., "Supplementary material for the article: Elshaflu, H.; Todorović, T. R.; Nikolić, M.; Lolić, A.; Višnjevac, A.; Hagenow, S.; Padrón, J. M.; García-Sosa, A. T.; Djordjevic, I. S.; Grubišic, S.; et al. Selenazolyl-Hydrazones as Novel Selective MAO Inhibitors with Antiproliferative and Antioxidant Activities: Experimental and In-Silico Studies. Frontiers in Chemistry 2018, 6 (JUL). https://doi.org/10.3389/fchem.2018.00247" in FRONTIERS IN CHEMISTRY (2018).

Clozapine, ziprasidone, and sertindole-induced morphological changes in the rat heart and their relationship to antioxidant enzymes function

Nikolić-Kokić, Aleksandra; Tatalović, Nikola; Nestorov, Jelena; Mijović, Milica; Mijušković, Ana; Miler, Marko; Oreščanin-Dušić, Zorana; Nikolić, Milan; Milošević, Verica; Blagojević, Duško P.; Spasic, Mihajlo; Miljević, Čedo

(Taylor & Francis Inc, Philadelphia, 2018)

TY  - JOUR
AU  - Nikolić-Kokić, Aleksandra
AU  - Tatalović, Nikola
AU  - Nestorov, Jelena
AU  - Mijović, Milica
AU  - Mijušković, Ana
AU  - Miler, Marko
AU  - Oreščanin-Dušić, Zorana
AU  - Nikolić, Milan
AU  - Milošević, Verica
AU  - Blagojević, Duško P.
AU  - Spasic, Mihajlo
AU  - Miljević, Čedo
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2206
AB  - Atypical antipsychotics produce severe side effects including myocarditis that may be attributed to oxidative stress. The aim of this study was to investigate the influence of clozapine, ziprasidone, and sertindole on rat heart morphology and determine whether redox imbalane plays a role in development of histopathological changes. Adult 3-month-old male Wistar rats were treated with recommended daily dose for selected drugs. After 4week treatment histopathological analysis of the heart was performed and expression and activity of antioxidant enzymes determined. All examined drugs induced histopathological changes that were characterized as toxic myocarditis. Degenerative changes in cardiomyocytes were accompanied by lymphocytic infiltration as well as pericardial histopathological alterations in all treated groups. The least prominent changes were observed in sertindole-treated animals, and most severe with clozapine. Clozapine increased superoxide dismutase 1 (SOD1) activity while ziprasidone reduced glutathione reductase (GR) activity. Sertindole exerted no marked effect on antioxidant enzyme function in the heart even though myocardial degeneration was noted. In conclusion, treatment with clozapine or ziprasidone induced pathophysiological alterations in rat heart, which appeared to be associated disturbances in antioxidant capacity.Abbreviation: AAP, Atypical antipsychotics; ROS, reactive oxygen species; SOD1, Copper-zinc superoxide dismutase; SOD2, Manganese superoxide dismutase; CAT, Catalase; GPx, Glutathione peroxidase; GR, Glutathione reductase; H&E, hematoxylin and eosin stain; TNF- , tumor necrosis factor alpha.
PB  - Taylor & Francis Inc, Philadelphia
T2  - Journal of Toxicology and Environmental Health. Part A
T1  - Clozapine, ziprasidone, and sertindole-induced morphological changes in the rat heart and their relationship to antioxidant enzymes function
VL  - 81
IS  - 17
SP  - 844
EP  - 853
DO  - 10.1080/15287394.2018.1495587
UR  - Kon_3537
ER  - 
@article{
author = "Nikolić-Kokić, Aleksandra and Tatalović, Nikola and Nestorov, Jelena and Mijović, Milica and Mijušković, Ana and Miler, Marko and Oreščanin-Dušić, Zorana and Nikolić, Milan and Milošević, Verica and Blagojević, Duško P. and Spasic, Mihajlo and Miljević, Čedo",
year = "2018",
abstract = "Atypical antipsychotics produce severe side effects including myocarditis that may be attributed to oxidative stress. The aim of this study was to investigate the influence of clozapine, ziprasidone, and sertindole on rat heart morphology and determine whether redox imbalane plays a role in development of histopathological changes. Adult 3-month-old male Wistar rats were treated with recommended daily dose for selected drugs. After 4week treatment histopathological analysis of the heart was performed and expression and activity of antioxidant enzymes determined. All examined drugs induced histopathological changes that were characterized as toxic myocarditis. Degenerative changes in cardiomyocytes were accompanied by lymphocytic infiltration as well as pericardial histopathological alterations in all treated groups. The least prominent changes were observed in sertindole-treated animals, and most severe with clozapine. Clozapine increased superoxide dismutase 1 (SOD1) activity while ziprasidone reduced glutathione reductase (GR) activity. Sertindole exerted no marked effect on antioxidant enzyme function in the heart even though myocardial degeneration was noted. In conclusion, treatment with clozapine or ziprasidone induced pathophysiological alterations in rat heart, which appeared to be associated disturbances in antioxidant capacity.Abbreviation: AAP, Atypical antipsychotics; ROS, reactive oxygen species; SOD1, Copper-zinc superoxide dismutase; SOD2, Manganese superoxide dismutase; CAT, Catalase; GPx, Glutathione peroxidase; GR, Glutathione reductase; H&E, hematoxylin and eosin stain; TNF- , tumor necrosis factor alpha.",
publisher = "Taylor & Francis Inc, Philadelphia",
journal = "Journal of Toxicology and Environmental Health. Part A",
title = "Clozapine, ziprasidone, and sertindole-induced morphological changes in the rat heart and their relationship to antioxidant enzymes function",
volume = "81",
number = "17",
pages = "844-853",
doi = "10.1080/15287394.2018.1495587",
url = "Kon_3537"
}
Nikolić-Kokić, A., Tatalović, N., Nestorov, J., Mijović, M., Mijušković, A., Miler, M., Oreščanin-Dušić, Z., Nikolić, M., Milošević, V., Blagojević, D. P., Spasic, M.,& Miljević, Č.. (2018). Clozapine, ziprasidone, and sertindole-induced morphological changes in the rat heart and their relationship to antioxidant enzymes function. in Journal of Toxicology and Environmental Health. Part A
Taylor & Francis Inc, Philadelphia., 81(17), 844-853.
https://doi.org/10.1080/15287394.2018.1495587
Kon_3537
Nikolić-Kokić A, Tatalović N, Nestorov J, Mijović M, Mijušković A, Miler M, Oreščanin-Dušić Z, Nikolić M, Milošević V, Blagojević DP, Spasic M, Miljević Č. Clozapine, ziprasidone, and sertindole-induced morphological changes in the rat heart and their relationship to antioxidant enzymes function. in Journal of Toxicology and Environmental Health. Part A. 2018;81(17):844-853.
doi:10.1080/15287394.2018.1495587
Kon_3537 .
Nikolić-Kokić, Aleksandra, Tatalović, Nikola, Nestorov, Jelena, Mijović, Milica, Mijušković, Ana, Miler, Marko, Oreščanin-Dušić, Zorana, Nikolić, Milan, Milošević, Verica, Blagojević, Duško P., Spasic, Mihajlo, Miljević, Čedo, "Clozapine, ziprasidone, and sertindole-induced morphological changes in the rat heart and their relationship to antioxidant enzymes function" in Journal of Toxicology and Environmental Health. Part A, 81, no. 17 (2018):844-853,
https://doi.org/10.1080/15287394.2018.1495587 .,
Kon_3537 .
11
8
9

Selenazolyl-hydrazones as Novel Selective MAO Inhibitors With Antiproliferative and Antioxidant Activities: Experimental and In-silico Studies

Elshaflu, Hana; Todorović, Tamara; Nikolić, Milan; Lolić, Aleksandar; Višnjevac, Aleksandar; Hagenow, Stefanie; Padrón, José M.; Garcia-Sosa, Alfonso T.; Đorđević, Ivana S.; Grubišić, Sonja; Stark, Holger; Filipović, Nenad R.

(Frontiers Media Sa, Lausanne, 2018)

TY  - JOUR
AU  - Elshaflu, Hana
AU  - Todorović, Tamara
AU  - Nikolić, Milan
AU  - Lolić, Aleksandar
AU  - Višnjevac, Aleksandar
AU  - Hagenow, Stefanie
AU  - Padrón, José M.
AU  - Garcia-Sosa, Alfonso T.
AU  - Đorđević, Ivana S.
AU  - Grubišić, Sonja
AU  - Stark, Holger
AU  - Filipović, Nenad R.
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2172
AB  - The novel approach in the treatment of complex multifactorial diseases, such as neurodegenerative disorders and cancer, requires a development of efficient multi-targeting oriented drugs. Since oxidative stress significantly contributes to the pathogenesis of cancer and neurodegenerative disorders, potential drug candidates should possess good antioxidant properties Due to promising biological activities shown for structurally related (1,3-thiazol-2-yl)hydrazones, a focused library of 12 structurally related benzylidene-based (1,3-selenazol-2-yl)hydrazones was designed as potential multi-targeting compounds. Monoamine oxidases (MAO) A/B inhibition properties of this class of compounds have been investigated. Surprisingly, the p-nitrophenyl-substituted (1,3-selenazol-2-yl)hydrazone 4 showed MAO B inhibition in a nanomolar concentration range (IC50 = 73 nM). Excellent antioxidant properties were confirmed in a number of different in vitro assays. Antiproliferative activity screening on a panel of six human solid tumor cell lines showed that potencies of some of the investigated compounds was comparable or even better than that of the positive control 5-fluorouracil. In-silico calculations of ADME properties pointed to promising good pharmacokinetic profiles of investigated compounds. Docking studies suggest that some compounds, compared to positive controls, have the ability to strongly interact with targets relevant to cancer such as 5'-nucleotidase, and to neurodegenerative diseases such as the small conductance calcium-activated potassium channel protein 1, in addition to confirmation of inhibitory binding at MAO B.
PB  - Frontiers Media Sa, Lausanne
T2  - FRONTIERS IN CHEMISTRY
T1  - Selenazolyl-hydrazones as Novel Selective MAO Inhibitors With Antiproliferative and Antioxidant Activities: Experimental and In-silico Studies
VL  - 6
DO  - 10.3389/fchem.2018.00247
UR  - Kon_3503
ER  - 
@article{
author = "Elshaflu, Hana and Todorović, Tamara and Nikolić, Milan and Lolić, Aleksandar and Višnjevac, Aleksandar and Hagenow, Stefanie and Padrón, José M. and Garcia-Sosa, Alfonso T. and Đorđević, Ivana S. and Grubišić, Sonja and Stark, Holger and Filipović, Nenad R.",
year = "2018",
abstract = "The novel approach in the treatment of complex multifactorial diseases, such as neurodegenerative disorders and cancer, requires a development of efficient multi-targeting oriented drugs. Since oxidative stress significantly contributes to the pathogenesis of cancer and neurodegenerative disorders, potential drug candidates should possess good antioxidant properties Due to promising biological activities shown for structurally related (1,3-thiazol-2-yl)hydrazones, a focused library of 12 structurally related benzylidene-based (1,3-selenazol-2-yl)hydrazones was designed as potential multi-targeting compounds. Monoamine oxidases (MAO) A/B inhibition properties of this class of compounds have been investigated. Surprisingly, the p-nitrophenyl-substituted (1,3-selenazol-2-yl)hydrazone 4 showed MAO B inhibition in a nanomolar concentration range (IC50 = 73 nM). Excellent antioxidant properties were confirmed in a number of different in vitro assays. Antiproliferative activity screening on a panel of six human solid tumor cell lines showed that potencies of some of the investigated compounds was comparable or even better than that of the positive control 5-fluorouracil. In-silico calculations of ADME properties pointed to promising good pharmacokinetic profiles of investigated compounds. Docking studies suggest that some compounds, compared to positive controls, have the ability to strongly interact with targets relevant to cancer such as 5'-nucleotidase, and to neurodegenerative diseases such as the small conductance calcium-activated potassium channel protein 1, in addition to confirmation of inhibitory binding at MAO B.",
publisher = "Frontiers Media Sa, Lausanne",
journal = "FRONTIERS IN CHEMISTRY",
title = "Selenazolyl-hydrazones as Novel Selective MAO Inhibitors With Antiproliferative and Antioxidant Activities: Experimental and In-silico Studies",
volume = "6",
doi = "10.3389/fchem.2018.00247",
url = "Kon_3503"
}
Elshaflu, H., Todorović, T., Nikolić, M., Lolić, A., Višnjevac, A., Hagenow, S., Padrón, J. M., Garcia-Sosa, A. T., Đorđević, I. S., Grubišić, S., Stark, H.,& Filipović, N. R.. (2018). Selenazolyl-hydrazones as Novel Selective MAO Inhibitors With Antiproliferative and Antioxidant Activities: Experimental and In-silico Studies. in FRONTIERS IN CHEMISTRY
Frontiers Media Sa, Lausanne., 6.
https://doi.org/10.3389/fchem.2018.00247
Kon_3503
Elshaflu H, Todorović T, Nikolić M, Lolić A, Višnjevac A, Hagenow S, Padrón JM, Garcia-Sosa AT, Đorđević IS, Grubišić S, Stark H, Filipović NR. Selenazolyl-hydrazones as Novel Selective MAO Inhibitors With Antiproliferative and Antioxidant Activities: Experimental and In-silico Studies. in FRONTIERS IN CHEMISTRY. 2018;6.
doi:10.3389/fchem.2018.00247
Kon_3503 .
Elshaflu, Hana, Todorović, Tamara, Nikolić, Milan, Lolić, Aleksandar, Višnjevac, Aleksandar, Hagenow, Stefanie, Padrón, José M., Garcia-Sosa, Alfonso T., Đorđević, Ivana S., Grubišić, Sonja, Stark, Holger, Filipović, Nenad R., "Selenazolyl-hydrazones as Novel Selective MAO Inhibitors With Antiproliferative and Antioxidant Activities: Experimental and In-silico Studies" in FRONTIERS IN CHEMISTRY, 6 (2018),
https://doi.org/10.3389/fchem.2018.00247 .,
Kon_3503 .
2
13
14
13

Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin

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

(Elsevier, 2017)

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana Ž.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3035
AB  - Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (Ka = 2 × 106 M−1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin.
PB  - Elsevier
T2  - Food Chemistry
T1  - Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin
VL  - 239
SP  - 1090
EP  - 1099
DO  - 10.1016/j.foodchem.2017.07.066
ER  - 
@article{
author = "Minić, Simeon L. and Stanić-Vučinić, Dragana and Radomirović, Mirjana Ž. and Radibratović, Milica and Milčić, Miloš K. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2017",
abstract = "Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (Ka = 2 × 106 M−1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin",
volume = "239",
pages = "1090-1099",
doi = "10.1016/j.foodchem.2017.07.066"
}
Minić, S. L., Stanić-Vučinić, D., Radomirović, M. Ž., Radibratović, M., Milčić, M. K., Nikolić, M.,& Ćirković-Veličković, T.. (2017). Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. in Food Chemistry
Elsevier., 239, 1090-1099.
https://doi.org/10.1016/j.foodchem.2017.07.066
Minić SL, Stanić-Vučinić D, Radomirović MŽ, Radibratović M, Milčić MK, Nikolić M, Ćirković-Veličković T. Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. in Food Chemistry. 2017;239:1090-1099.
doi:10.1016/j.foodchem.2017.07.066 .
Minić, Simeon L., Stanić-Vučinić, Dragana, Radomirović, Mirjana Ž., Radibratović, Milica, Milčić, Miloš K., Nikolić, Milan, Ćirković-Veličković, Tanja, "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin" in Food Chemistry, 239 (2017):1090-1099,
https://doi.org/10.1016/j.foodchem.2017.07.066 . .
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