TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Jovanović, Zorana
AU  - Cvijetić, Ilija
AU  - Šunderić, Miloš
AU  - Veličković, Luka
AU  - Katrlík, Jaroslav
AU  - Holazová, Alena
AU  - Nikolić, Milan
AU  - Minić, Simeon
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7298
AB  - Blue C-phycocyanin (C-PC), the major Spirulina protein with innumerable
health-promoting benefits, is an attractive colourant and food supplement. A crucial obstacle to its
more extensive use is its relatively low stability. This study aimed to screen various food-derived
ligands for their ability to bind and stabilise C-PC, utilising spectroscopic techniques and molecular
docking. Among twelve examined ligands, the protein fluorescence quenching revealed that
only quercetin, coenzyme Q10 and resveratrol had a moderate affinity to C-PC (Ka of 2.2 to 3.7 × 105
M–1). Docking revealed these three ligands bind more strongly to the C-PC hexamer than the trimer,
with the binding sites located at the interface of two (αβ)3 trimers. UV/VIS absorption spectroscopy
demonstrated the changes in the C-PC absorption spectra in a complex with quercetin
and resveratrol compared to the spectra of free protein and ligands. Selected ligands did not affect
the secondary structure content, but they induced changes in the tertiary protein structure in the
CD study. A fluorescence-based thermal stability assay demonstrated quercetin and coenzyme Q10
increased the C-PC melting point by nearly 5 °C. Our study identified food-derived ligands that
interact with C-PC and improve its thermal stability, indicating their potential as stabilising agents
for C-PC in the food industry.
PB  - MDPI
T2  - International Journal of Molecular Sciences
T1  - Investigation of the Potential of Selected Food-Derived Antioxidants to Bind and Stabilise the Bioactive Blue Protein C-Phycocyanin from Cyanobacteria Spirulina
VL  - 25
IS  - 1
SP  - 229
DO  - 10.3390/ijms25010229
ER  - 

@article{
author = "Gligorijević, Nikola and Jovanović, Zorana and Cvijetić, Ilija and Šunderić, Miloš and Veličković, Luka and Katrlík, Jaroslav and Holazová, Alena and Nikolić, Milan and Minić, Simeon",
year = "2024",
abstract = "Blue C-phycocyanin (C-PC), the major Spirulina protein with innumerable
health-promoting benefits, is an attractive colourant and food supplement. A crucial obstacle to its
more extensive use is its relatively low stability. This study aimed to screen various food-derived
ligands for their ability to bind and stabilise C-PC, utilising spectroscopic techniques and molecular
docking. Among twelve examined ligands, the protein fluorescence quenching revealed that
only quercetin, coenzyme Q10 and resveratrol had a moderate affinity to C-PC (Ka of 2.2 to 3.7 × 105
M–1). Docking revealed these three ligands bind more strongly to the C-PC hexamer than the trimer,
with the binding sites located at the interface of two (αβ)3 trimers. UV/VIS absorption spectroscopy
demonstrated the changes in the C-PC absorption spectra in a complex with quercetin
and resveratrol compared to the spectra of free protein and ligands. Selected ligands did not affect
the secondary structure content, but they induced changes in the tertiary protein structure in the
CD study. A fluorescence-based thermal stability assay demonstrated quercetin and coenzyme Q10
increased the C-PC melting point by nearly 5 °C. Our study identified food-derived ligands that
interact with C-PC and improve its thermal stability, indicating their potential as stabilising agents
for C-PC in the food industry.",
publisher = "MDPI",
journal = "International Journal of Molecular Sciences",
title = "Investigation of the Potential of Selected Food-Derived Antioxidants to Bind and Stabilise the Bioactive Blue Protein C-Phycocyanin from Cyanobacteria Spirulina",
volume = "25",
number = "1",
pages = "229",
doi = "10.3390/ijms25010229"
}

Gligorijević, N., Jovanović, Z., Cvijetić, I., Šunderić, M., Veličković, L., Katrlík, J., Holazová, A., Nikolić, M.,& Minić, S.. (2024). Investigation of the Potential of Selected Food-Derived Antioxidants to Bind and Stabilise the Bioactive Blue Protein C-Phycocyanin from Cyanobacteria Spirulina. in International Journal of Molecular Sciences
MDPI., 25(1), 229.
https://doi.org/10.3390/ijms25010229

Gligorijević N, Jovanović Z, Cvijetić I, Šunderić M, Veličković L, Katrlík J, Holazová A, Nikolić M, Minić S. Investigation of the Potential of Selected Food-Derived Antioxidants to Bind and Stabilise the Bioactive Blue Protein C-Phycocyanin from Cyanobacteria Spirulina. in International Journal of Molecular Sciences. 2024;25(1):229.
doi:10.3390/ijms25010229 .

Gligorijević, Nikola, Jovanović, Zorana, Cvijetić, Ilija, Šunderić, Miloš, Veličković, Luka, Katrlík, Jaroslav, Holazová, Alena, Nikolić, Milan, Minić, Simeon, "Investigation of the Potential of Selected Food-Derived Antioxidants to Bind and Stabilise the Bioactive Blue Protein C-Phycocyanin from Cyanobacteria Spirulina" in International Journal of Molecular Sciences, 25, no. 1 (2024):229,
https://doi.org/10.3390/ijms25010229 . .

TY  - JOUR
AU  - Šunderić, Miloš
AU  - Gligorijević, Nikola
AU  - Milčić, Miloš
AU  - Minić, Simeon
AU  - Nedić, Olgica
AU  - Nikolić, Milan
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6471
AB  - Under simulated physiological conditions, this study investigates the interaction between nutraceutical phycocyanobilin (PCB) and the universal anti-protease protein human alpha-2-macroglobulin (a2M). Extensive molecular docking analyses on multiple a2M conformations, spectroscopic techniques, and a2M activity assays were utilized to examine the complex formation. The results revealed that for every protein conformation, two high energy binding sites exist: the first, conformationally independent, at the interface region between two monomer chains and the second, conformationally dependent, in the pocket composed of amino acids from four distinct domains (TED, RBD, CUB, and MG2) of the single protein chain. Spectrofluorimetric measurements indicated a moderate affinity between a2M and PCB with a moderately high binding constant of 6.3 x 10^5 M^-1 at 25 °C. The binding of PCB to a2M resulted in minor changes in the secondary structure content of a2M. Furthermore, PCB protected a2M from oxidation and preserved its anti-protease activity in the oxidative environment. These findings suggest that PCB binding could indirectly impact the body’s response to oxidative stress by influencing a2M’s role in controlling enzyme activity during the inflammatory process.
PB  - Taylor & Francis Group
T2  - Journal of Biomolecular Structure and Dynamics
T1  - Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress
DO  - 10.1080/07391102.2023.2248273
ER  - 

@article{
author = "Šunderić, Miloš and Gligorijević, Nikola and Milčić, Miloš and Minić, Simeon and Nedić, Olgica and Nikolić, Milan",
year = "2023",
abstract = "Under simulated physiological conditions, this study investigates the interaction between nutraceutical phycocyanobilin (PCB) and the universal anti-protease protein human alpha-2-macroglobulin (a2M). Extensive molecular docking analyses on multiple a2M conformations, spectroscopic techniques, and a2M activity assays were utilized to examine the complex formation. The results revealed that for every protein conformation, two high energy binding sites exist: the first, conformationally independent, at the interface region between two monomer chains and the second, conformationally dependent, in the pocket composed of amino acids from four distinct domains (TED, RBD, CUB, and MG2) of the single protein chain. Spectrofluorimetric measurements indicated a moderate affinity between a2M and PCB with a moderately high binding constant of 6.3 x 10^5 M^-1 at 25 °C. The binding of PCB to a2M resulted in minor changes in the secondary structure content of a2M. Furthermore, PCB protected a2M from oxidation and preserved its anti-protease activity in the oxidative environment. These findings suggest that PCB binding could indirectly impact the body’s response to oxidative stress by influencing a2M’s role in controlling enzyme activity during the inflammatory process.",
publisher = "Taylor & Francis Group",
journal = "Journal of Biomolecular Structure and Dynamics",
title = "Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress",
doi = "10.1080/07391102.2023.2248273"
}

Šunderić, M., Gligorijević, N., Milčić, M., Minić, S., Nedić, O.,& Nikolić, M.. (2023). Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress. in Journal of Biomolecular Structure and Dynamics
Taylor & Francis Group..
https://doi.org/10.1080/07391102.2023.2248273

Šunderić M, Gligorijević N, Milčić M, Minić S, Nedić O, Nikolić M. Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress. in Journal of Biomolecular Structure and Dynamics. 2023;.
doi:10.1080/07391102.2023.2248273 .

Šunderić, Miloš, Gligorijević, Nikola, Milčić, Miloš, Minić, Simeon, Nedić, Olgica, Nikolić, Milan, "Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress" in Journal of Biomolecular Structure and Dynamics (2023),
https://doi.org/10.1080/07391102.2023.2248273 . .

TY  - CONF
AU  - Šunderić, Miloš
AU  - Veličković, Luka
AU  - Gligorijević, Nikola
AU  - Aleksić, Ljubodrag
AU  - Nikolić, Milan
AU  - Takić, Marija
AU  - Minić, Simeon
PY  - 2023
UR  - https://euroanalysis2023.ch/
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6592
AB  - C-Phycocyanin (C-PC) is a phycobiliprotein from cyanobacteria, where it harvests light energy that is then transferred to chlorophylls during photosynthesis. It has an intense blue color due to a covalently bonded tetrapyrrole chromophore, and owing to this property is used in the food industry as a good natural alternative for food coloring. In addition to its coloring properties, C-PC has anti-inflammatory, antioxidant, anti-cancer, and immune-enhancing effects that qualify it as a dietary supplement already included in various formulations, mainly Spirulina extract powders. Since it is used as a food colorant and as a dietary supplement, it may interact with food ingredients, affecting its stability, digestibility, or antioxidant properties. Palmitic acid and linoleic acid (which can be metabolized to linolenic acid) are abundant in meat, milk, and edible oils, so that they could interact with C-PC. C-Phycocyanin isolated from the cyanobacterium Arthrospira platensis (Spirulina) was incubated with increasing concentrations of these three fatty acids, and its fluorescence intensity was monitored. Incubation resulted in a fluorescence quenching effect, indicating that binding had occurred. The binding equations indicated that the association constants were of the same order of magnitude and that the number of approximate binding sites was more than one (Ka = 4.64 x 10⁴ M-¹, n = 1.5 for linoleic acid; Ka = 2.88 x 10⁴ M–¹, n = 1.9 for linolenic acid; Ka = 0.44 x 10⁴ M–¹, n = 0.8 for palmitic acid). This moderate interaction between C-PC and fatty acids could influence its behavior as a nutraceutical and food colorant.
PB  - European Chemical Society
C3  - Euroanalysis 2023 - Analytical Probing of Complex Systems, Abstract book, August 27th - 31st, 2023, Geneva, Switzerland
T1  - Dietary fatty acids as a new binding partner of C - phycocyanin: a fluorimetric study
SP  - 332
EP  - 333
UR  - https://hdl.handle.net/21.15107/rcub_cer_6592
ER  - 

@conference{
author = "Šunderić, Miloš and Veličković, Luka and Gligorijević, Nikola and Aleksić, Ljubodrag and Nikolić, Milan and Takić, Marija and Minić, Simeon",
year = "2023",
abstract = "C-Phycocyanin (C-PC) is a phycobiliprotein from cyanobacteria, where it harvests light energy that is then transferred to chlorophylls during photosynthesis. It has an intense blue color due to a covalently bonded tetrapyrrole chromophore, and owing to this property is used in the food industry as a good natural alternative for food coloring. In addition to its coloring properties, C-PC has anti-inflammatory, antioxidant, anti-cancer, and immune-enhancing effects that qualify it as a dietary supplement already included in various formulations, mainly Spirulina extract powders. Since it is used as a food colorant and as a dietary supplement, it may interact with food ingredients, affecting its stability, digestibility, or antioxidant properties. Palmitic acid and linoleic acid (which can be metabolized to linolenic acid) are abundant in meat, milk, and edible oils, so that they could interact with C-PC. C-Phycocyanin isolated from the cyanobacterium Arthrospira platensis (Spirulina) was incubated with increasing concentrations of these three fatty acids, and its fluorescence intensity was monitored. Incubation resulted in a fluorescence quenching effect, indicating that binding had occurred. The binding equations indicated that the association constants were of the same order of magnitude and that the number of approximate binding sites was more than one (Ka = 4.64 x 10⁴ M-¹, n = 1.5 for linoleic acid; Ka = 2.88 x 10⁴ M–¹, n = 1.9 for linolenic acid; Ka = 0.44 x 10⁴ M–¹, n = 0.8 for palmitic acid). This moderate interaction between C-PC and fatty acids could influence its behavior as a nutraceutical and food colorant.",
publisher = "European Chemical Society",
journal = "Euroanalysis 2023 - Analytical Probing of Complex Systems, Abstract book, August 27th - 31st, 2023, Geneva, Switzerland",
title = "Dietary fatty acids as a new binding partner of C - phycocyanin: a fluorimetric study",
pages = "332-333",
url = "https://hdl.handle.net/21.15107/rcub_cer_6592"
}

Šunderić, M., Veličković, L., Gligorijević, N., Aleksić, L., Nikolić, M., Takić, M.,& Minić, S.. (2023). Dietary fatty acids as a new binding partner of C - phycocyanin: a fluorimetric study. in Euroanalysis 2023 - Analytical Probing of Complex Systems, Abstract book, August 27th - 31st, 2023, Geneva, Switzerland
European Chemical Society., 332-333.
https://hdl.handle.net/21.15107/rcub_cer_6592

Šunderić M, Veličković L, Gligorijević N, Aleksić L, Nikolić M, Takić M, Minić S. Dietary fatty acids as a new binding partner of C - phycocyanin: a fluorimetric study. in Euroanalysis 2023 - Analytical Probing of Complex Systems, Abstract book, August 27th - 31st, 2023, Geneva, Switzerland. 2023;:332-333.
https://hdl.handle.net/21.15107/rcub_cer_6592 .

Šunderić, Miloš, Veličković, Luka, Gligorijević, Nikola, Aleksić, Ljubodrag, Nikolić, Milan, Takić, Marija, Minić, Simeon, "Dietary fatty acids as a new binding partner of C - phycocyanin: a fluorimetric study" in Euroanalysis 2023 - Analytical Probing of Complex Systems, Abstract book, August 27th - 31st, 2023, Geneva, Switzerland (2023):332-333,
https://hdl.handle.net/21.15107/rcub_cer_6592 .

TY  - CONF
AU  - Aleksić, Ljubodrag
AU  - Veličković, Luka
AU  - Gligorijević, Nikola
AU  - Šunderić, Miloš
AU  - Takić, Marija
AU  - Nikolić, Milan
AU  - Minić, Simeon
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6667
AB  - Cultured meat requires less land and water and is less polluting, but still costly. The critical
challenge in cultivated meat science is identifying and developing bovine serum albumin
alternatives as the key component in cell media. Phycobiliproteins (PBPs) from micro- and
macroalgae are promising candidates for albumin replacement due to their high abundance
and well-known excellent antioxidative and metal-binding activities of covalently attached
tetrapyrrole chromophores. Considering the importance of fatty acids (FA) binding by
albumin for cell cultivation, the additional prerequisites for developing PBPs as albumin
replacement components is their validation for the ability to bind FA. This study aims to
examine the ability of C-phycocyanin (C-PC), the major PBP of microalgae Arthrospira
platensis, to bind seven fatty acids (stearic, palmitic, oleic, elaidic, linoleic, linolenic and
docosahexaenoic acid). For this purpose, we employed various optical spectroscopy
techniques (fluorescence, CD, and VIS absorption spectroscopy). The protein fluorescence
quenching approach demonstrated FA binding affinities ranging from 0.42 to 2.4 x 105
M−1, with the ability of FA to bind at different sites on C-PC. Fatty acid binding induces
substantial changes in the VIS absorption spectra of C-PC, indicating the FA are attached
in the vicinity of C-PC chromophores. On the other hand, CD spectroscopy did not show
significant effects of FA binding on C-PC secondary structure content. Overall, this study
revealed C-PC's significant potential in binding FA, the critical prerequisite to replacing
albumin for developing animal-free cell media for meat cultivation.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
T1  - Examining fatty acid interactions with Arthrospira platensis-derived C-phycocyanin
SP  - 121
EP  - 121
UR  - https://hdl.handle.net/21.15107/rcub_cer_6667
ER  - 

@conference{
author = "Aleksić, Ljubodrag and Veličković, Luka and Gligorijević, Nikola and Šunderić, Miloš and Takić, Marija and Nikolić, Milan and Minić, Simeon",
year = "2023",
abstract = "Cultured meat requires less land and water and is less polluting, but still costly. The critical
challenge in cultivated meat science is identifying and developing bovine serum albumin
alternatives as the key component in cell media. Phycobiliproteins (PBPs) from micro- and
macroalgae are promising candidates for albumin replacement due to their high abundance
and well-known excellent antioxidative and metal-binding activities of covalently attached
tetrapyrrole chromophores. Considering the importance of fatty acids (FA) binding by
albumin for cell cultivation, the additional prerequisites for developing PBPs as albumin
replacement components is their validation for the ability to bind FA. This study aims to
examine the ability of C-phycocyanin (C-PC), the major PBP of microalgae Arthrospira
platensis, to bind seven fatty acids (stearic, palmitic, oleic, elaidic, linoleic, linolenic and
docosahexaenoic acid). For this purpose, we employed various optical spectroscopy
techniques (fluorescence, CD, and VIS absorption spectroscopy). The protein fluorescence
quenching approach demonstrated FA binding affinities ranging from 0.42 to 2.4 x 105
M−1, with the ability of FA to bind at different sites on C-PC. Fatty acid binding induces
substantial changes in the VIS absorption spectra of C-PC, indicating the FA are attached
in the vicinity of C-PC chromophores. On the other hand, CD spectroscopy did not show
significant effects of FA binding on C-PC secondary structure content. Overall, this study
revealed C-PC's significant potential in binding FA, the critical prerequisite to replacing
albumin for developing animal-free cell media for meat cultivation.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia",
title = "Examining fatty acid interactions with Arthrospira platensis-derived C-phycocyanin",
pages = "121-121",
url = "https://hdl.handle.net/21.15107/rcub_cer_6667"
}

Aleksić, L., Veličković, L., Gligorijević, N., Šunderić, M., Takić, M., Nikolić, M.,& Minić, S.. (2023). Examining fatty acid interactions with Arthrospira platensis-derived C-phycocyanin. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
Serbian Biochemical Society., 121-121.
https://hdl.handle.net/21.15107/rcub_cer_6667

Aleksić L, Veličković L, Gligorijević N, Šunderić M, Takić M, Nikolić M, Minić S. Examining fatty acid interactions with Arthrospira platensis-derived C-phycocyanin. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia. 2023;:121-121.
https://hdl.handle.net/21.15107/rcub_cer_6667 .

Aleksić, Ljubodrag, Veličković, Luka, Gligorijević, Nikola, Šunderić, Miloš, Takić, Marija, Nikolić, Milan, Minić, Simeon, "Examining fatty acid interactions with Arthrospira platensis-derived C-phycocyanin" in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia (2023):121-121,
https://hdl.handle.net/21.15107/rcub_cer_6667 .

TY  - CONF
AU  - Miljuš, Goran
AU  - Penezić, Ana
AU  - Noe, Dragana
AU  - Dobrijević, Zorana
AU  - Baralić, Marko
AU  - Robajac, Dragana
AU  - Šunderić, Miloš
AU  - Gligorijević, Nikola
AU  - Dimitrijević, Ivan
AU  - Barišić, Goran
AU  - Nedić, Olgica
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6664
AB  - Human serum tansferrin (hsTf) is a major circulatory protein crucial for the
transport/metabolism of Fe3+ ions. By sequestering and delivering ferric ions to target
tissues/cells hsTf maintains redox homeostasis. Oxidative stress (OS), one of the hallmarks
of (patho)physiological conditions, alters protein structure and function. The main role of
hsTf hinges on specific interaction with cellular Tf receptor (TfR) while other interactions
contribute to diverse functions. The aim of this study was to profile interacting partners of
hsTf in the samples of serum coming from patients diagnosed with a wide range of
pathological conditions with underlying OS status. Anti-hsTf pull-down samples were
analysed using mass spectrometry. Data went through analysis by appropriate
bioinformatic tools. Results reveal differences in expression of hsTf interacting proteins in
sample groups of patients suffering from kidney insufficiency subjected to dialysis
treatment (peritoneal-PD or hemo-HD) also with patients with gestational diabetes
compared to respective healthy sample groups. Colorectal cancer stage T3 versus T2 stage
shows an inverse distribution of expression profiles in comparison to healthy samples.
Most prominent differences are seen in hsTf interacting partners involved in the
complement and coagulation cascades and cholesterol metabolic pathways, suggesting a
multifaceted role of hsTf in these processes throughout the course of the disease.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
T1  - Proteomic profiling of anti-transferrin pull-down in patients with underlying oxidative stress
SP  - 69
EP  - 69
UR  - https://hdl.handle.net/21.15107/rcub_cer_6664
ER  - 

@conference{
author = "Miljuš, Goran and Penezić, Ana and Noe, Dragana and Dobrijević, Zorana and Baralić, Marko and Robajac, Dragana and Šunderić, Miloš and Gligorijević, Nikola and Dimitrijević, Ivan and Barišić, Goran and Nedić, Olgica",
year = "2023",
abstract = "Human serum tansferrin (hsTf) is a major circulatory protein crucial for the
transport/metabolism of Fe3+ ions. By sequestering and delivering ferric ions to target
tissues/cells hsTf maintains redox homeostasis. Oxidative stress (OS), one of the hallmarks
of (patho)physiological conditions, alters protein structure and function. The main role of
hsTf hinges on specific interaction with cellular Tf receptor (TfR) while other interactions
contribute to diverse functions. The aim of this study was to profile interacting partners of
hsTf in the samples of serum coming from patients diagnosed with a wide range of
pathological conditions with underlying OS status. Anti-hsTf pull-down samples were
analysed using mass spectrometry. Data went through analysis by appropriate
bioinformatic tools. Results reveal differences in expression of hsTf interacting proteins in
sample groups of patients suffering from kidney insufficiency subjected to dialysis
treatment (peritoneal-PD or hemo-HD) also with patients with gestational diabetes
compared to respective healthy sample groups. Colorectal cancer stage T3 versus T2 stage
shows an inverse distribution of expression profiles in comparison to healthy samples.
Most prominent differences are seen in hsTf interacting partners involved in the
complement and coagulation cascades and cholesterol metabolic pathways, suggesting a
multifaceted role of hsTf in these processes throughout the course of the disease.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia",
title = "Proteomic profiling of anti-transferrin pull-down in patients with underlying oxidative stress",
pages = "69-69",
url = "https://hdl.handle.net/21.15107/rcub_cer_6664"
}

Miljuš, G., Penezić, A., Noe, D., Dobrijević, Z., Baralić, M., Robajac, D., Šunderić, M., Gligorijević, N., Dimitrijević, I., Barišić, G.,& Nedić, O.. (2023). Proteomic profiling of anti-transferrin pull-down in patients with underlying oxidative stress. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
Serbian Biochemical Society., 69-69.
https://hdl.handle.net/21.15107/rcub_cer_6664

Miljuš G, Penezić A, Noe D, Dobrijević Z, Baralić M, Robajac D, Šunderić M, Gligorijević N, Dimitrijević I, Barišić G, Nedić O. Proteomic profiling of anti-transferrin pull-down in patients with underlying oxidative stress. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia. 2023;:69-69.
https://hdl.handle.net/21.15107/rcub_cer_6664 .

Miljuš, Goran, Penezić, Ana, Noe, Dragana, Dobrijević, Zorana, Baralić, Marko, Robajac, Dragana, Šunderić, Miloš, Gligorijević, Nikola, Dimitrijević, Ivan, Barišić, Goran, Nedić, Olgica, "Proteomic profiling of anti-transferrin pull-down in patients with underlying oxidative stress" in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia (2023):69-69,
https://hdl.handle.net/21.15107/rcub_cer_6664 .

TY  - JOUR
AU  - Baralić, Marko
AU  - Robajac, Dragana
AU  - Penezić, Ana
AU  - Brković, Voin
AU  - Gligorijević, Nikola
AU  - Bontić, Ana
AU  - Pavlović, Jelena
AU  - Nikolić, Jelena
AU  - Miljuš, Goran
AU  - Dobrijević, Zorana
AU  - Šunderić, Miloš
AU  - Pažitna, Lucija
AU  - Katrlík, Jaroslav
AU  - Nedić, Olgica
AU  - Laušević, Mirjana
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6445
AB  - In previous publications, we pointed out the importance of mannosylation of fibrinogen for the development of cardiovascular complications and fucosylation as a predictor of peritoneal membrane dysfunction in patients on peritoneal dialysis (PD). After a follow-up period of 30 months from the onset of the COVID-19 pandemic, we evaluated the significance of 1,25-dihydroxyvitamin D3 (calcitriol) therapy, primary disease, biochemical and hematologic analyzes, and previously performed glycan analysis by lectin-based microarray as predictors of mortality in this patient group. After univariate Cox regression analysis, diabetes mellitus (DM) and calcitriol therapy were found to be potential predictors of mortality. Additional multivariate Cox regression analysis confirmed that only DM was a predictor of mortality. Nevertheless, the use of calcitriol in therapy significantly reduced mortality in this patient group, as shown by the Kaplan–Meier survival curve. The presence of DM as a concomitant disease proved to be a strong predictor of fatal outcome in PD patients infected with SARS-CoV-2. This is the first study to indicate the importance and beneficial effect of calcitriol therapy on survival in PD patients with COVID-19 infection. In addition, this study points to the possibility that adverse thrombogenic events observed in PD patients during the pandemic may be caused by aberrant fibrinogen glycosylation.
PB  - Switzerland : Multidisciplinary Digital Publishing Institute (MDPI)
T2  - Nutrients
T1  - Significance of 1,25-Dihydroxyvitamin D3 on Overall Mortality in Peritoneal Dialysis Patients with COVID-19
VL  - 15
IS  - 9
SP  - 2050
DO  - 10.3390/nu15092050
ER  - 

@article{
author = "Baralić, Marko and Robajac, Dragana and Penezić, Ana and Brković, Voin and Gligorijević, Nikola and Bontić, Ana and Pavlović, Jelena and Nikolić, Jelena and Miljuš, Goran and Dobrijević, Zorana and Šunderić, Miloš and Pažitna, Lucija and Katrlík, Jaroslav and Nedić, Olgica and Laušević, Mirjana",
year = "2023",
abstract = "In previous publications, we pointed out the importance of mannosylation of fibrinogen for the development of cardiovascular complications and fucosylation as a predictor of peritoneal membrane dysfunction in patients on peritoneal dialysis (PD). After a follow-up period of 30 months from the onset of the COVID-19 pandemic, we evaluated the significance of 1,25-dihydroxyvitamin D3 (calcitriol) therapy, primary disease, biochemical and hematologic analyzes, and previously performed glycan analysis by lectin-based microarray as predictors of mortality in this patient group. After univariate Cox regression analysis, diabetes mellitus (DM) and calcitriol therapy were found to be potential predictors of mortality. Additional multivariate Cox regression analysis confirmed that only DM was a predictor of mortality. Nevertheless, the use of calcitriol in therapy significantly reduced mortality in this patient group, as shown by the Kaplan–Meier survival curve. The presence of DM as a concomitant disease proved to be a strong predictor of fatal outcome in PD patients infected with SARS-CoV-2. This is the first study to indicate the importance and beneficial effect of calcitriol therapy on survival in PD patients with COVID-19 infection. In addition, this study points to the possibility that adverse thrombogenic events observed in PD patients during the pandemic may be caused by aberrant fibrinogen glycosylation.",
publisher = "Switzerland : Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "Nutrients",
title = "Significance of 1,25-Dihydroxyvitamin D3 on Overall Mortality in Peritoneal Dialysis Patients with COVID-19",
volume = "15",
number = "9",
pages = "2050",
doi = "10.3390/nu15092050"
}

Baralić, M., Robajac, D., Penezić, A., Brković, V., Gligorijević, N., Bontić, A., Pavlović, J., Nikolić, J., Miljuš, G., Dobrijević, Z., Šunderić, M., Pažitna, L., Katrlík, J., Nedić, O.,& Laušević, M.. (2023). Significance of 1,25-Dihydroxyvitamin D3 on Overall Mortality in Peritoneal Dialysis Patients with COVID-19. in Nutrients
Switzerland : Multidisciplinary Digital Publishing Institute (MDPI)., 15(9), 2050.
https://doi.org/10.3390/nu15092050

Baralić M, Robajac D, Penezić A, Brković V, Gligorijević N, Bontić A, Pavlović J, Nikolić J, Miljuš G, Dobrijević Z, Šunderić M, Pažitna L, Katrlík J, Nedić O, Laušević M. Significance of 1,25-Dihydroxyvitamin D3 on Overall Mortality in Peritoneal Dialysis Patients with COVID-19. in Nutrients. 2023;15(9):2050.
doi:10.3390/nu15092050 .

Baralić, Marko, Robajac, Dragana, Penezić, Ana, Brković, Voin, Gligorijević, Nikola, Bontić, Ana, Pavlović, Jelena, Nikolić, Jelena, Miljuš, Goran, Dobrijević, Zorana, Šunderić, Miloš, Pažitna, Lucija, Katrlík, Jaroslav, Nedić, Olgica, Laušević, Mirjana, "Significance of 1,25-Dihydroxyvitamin D3 on Overall Mortality in Peritoneal Dialysis Patients with COVID-19" in Nutrients, 15, no. 9 (2023):2050,
https://doi.org/10.3390/nu15092050 . .

TY  - CONF
AU  - Gligorijević, Nikola
AU  - Šunderić, Miloš
AU  - Minić, Simeon
AU  - Nedić, Olgica
AU  - Nikolić, Milan
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6822
AB  - The interaction between phycocyanobilin (PCB), a bioactive
chromophore of blue-green cyanobacteria Spirulina’s phycobiliproteins,
and human alpha-2-macroglobulin (a2M), a universal
anti-proteinase, was investigated in this study under simulated
physiological conditions using spectroscopic techniques and a2M
activity assay. Protein a2M was found to bind PCB with a moderate
affinity, as assessed by spectrofluorimetric titration. The
binding constant was calculated to be 6.39105 M
 1 at 25°C. The
binding of PCB to a2M did not cause significant change in the
secondary structure of the protein, as determined by circular
dichroism. PCB protected a2M from oxidative damage in the
presence of AAPH-induced free radical overproduction. PCB
binding also effectively preserved a2M anti-proteinase activity.
Since a2M is involved in controlling the action of enzymes during
the inflammatory process, the protection that PCB expresses
could indirectly influence the intensity and direction of the body
response to impaired homeostasis, especially under oxidative
stress.
PB  - Wiley
C3  - FEBS Open Bio
T1  - Interaction between alpha-2-macroglobulin and phycocyanobilin – structural and physiological implications
VL  - 12
IS  - Supplement 1
SP  - 304
EP  - 304
DO  - 10.1002/2211-5463.13440
ER  - 

@conference{
author = "Gligorijević, Nikola and Šunderić, Miloš and Minić, Simeon and Nedić, Olgica and Nikolić, Milan",
year = "2022",
abstract = "The interaction between phycocyanobilin (PCB), a bioactive
chromophore of blue-green cyanobacteria Spirulina’s phycobiliproteins,
and human alpha-2-macroglobulin (a2M), a universal
anti-proteinase, was investigated in this study under simulated
physiological conditions using spectroscopic techniques and a2M
activity assay. Protein a2M was found to bind PCB with a moderate
affinity, as assessed by spectrofluorimetric titration. The
binding constant was calculated to be 6.39105 M
 1 at 25°C. The
binding of PCB to a2M did not cause significant change in the
secondary structure of the protein, as determined by circular
dichroism. PCB protected a2M from oxidative damage in the
presence of AAPH-induced free radical overproduction. PCB
binding also effectively preserved a2M anti-proteinase activity.
Since a2M is involved in controlling the action of enzymes during
the inflammatory process, the protection that PCB expresses
could indirectly influence the intensity and direction of the body
response to impaired homeostasis, especially under oxidative
stress.",
publisher = "Wiley",
journal = "FEBS Open Bio",
title = "Interaction between alpha-2-macroglobulin and phycocyanobilin – structural and physiological implications",
volume = "12",
number = "Supplement 1",
pages = "304-304",
doi = "10.1002/2211-5463.13440"
}

Gligorijević, N., Šunderić, M., Minić, S., Nedić, O.,& Nikolić, M.. (2022). Interaction between alpha-2-macroglobulin and phycocyanobilin – structural and physiological implications. in FEBS Open Bio
Wiley., 12(Supplement 1), 304-304.
https://doi.org/10.1002/2211-5463.13440

Gligorijević N, Šunderić M, Minić S, Nedić O, Nikolić M. Interaction between alpha-2-macroglobulin and phycocyanobilin – structural and physiological implications. in FEBS Open Bio. 2022;12(Supplement 1):304-304.
doi:10.1002/2211-5463.13440 .

Gligorijević, Nikola, Šunderić, Miloš, Minić, Simeon, Nedić, Olgica, Nikolić, Milan, "Interaction between alpha-2-macroglobulin and phycocyanobilin – structural and physiological implications" in FEBS Open Bio, 12, no. Supplement 1 (2022):304-304,
https://doi.org/10.1002/2211-5463.13440 . .

TY  - CONF
AU  - Šunderić, Miloš
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Nedić, Olgica
AU  - Nikolić, Milan
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7289
AB  - In this study, the interaction between phycocyanobilin (PCB)1, a bioactive chromophore of
blue-green algae Spirulina's phycobiliproteins, and alpha-2-macroglobulin (α2M)2, a
universal anti-proteinase, was investigated under simulated physiological conditions using
spectroscopic techniques and α2M activity assay. Using spectrofluorimetric measurements,
we found that α2M binds PCB with a moderate affinity, with a binding constant of 6.3×
105 M−1 at 25°C. The binding of PCB to α2M does not cause any significant change in the
secondary structure of the protein (circular dichroism measurements). Besides, PCB
protects α2M from structural oxidative alterations under AAPH-induced free radical
overproduction. Further, PCB binding effectively preserves α2M anti-proteinase activity.
Since α2M is involved in controlling the action of enzymes during the inflammatory
process, the protection that PCB expresses could indirectly influence the intensity and
direction of body response to impaired homeostasis, especially under oxidative stress.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Tenth Conference with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia
T1  - Interaction between alpha-2-macroglobulin and phycocyanobilin – structural and physiological implications
SP  - 163
EP  - 163
UR  - https://hdl.handle.net/21.15107/rcub_cer_7289
ER  - 

@conference{
author = "Šunderić, Miloš and Gligorijević, Nikola and Minić, Simeon and Nedić, Olgica and Nikolić, Milan",
year = "2021",
abstract = "In this study, the interaction between phycocyanobilin (PCB)1, a bioactive chromophore of
blue-green algae Spirulina's phycobiliproteins, and alpha-2-macroglobulin (α2M)2, a
universal anti-proteinase, was investigated under simulated physiological conditions using
spectroscopic techniques and α2M activity assay. Using spectrofluorimetric measurements,
we found that α2M binds PCB with a moderate affinity, with a binding constant of 6.3×
105 M−1 at 25°C. The binding of PCB to α2M does not cause any significant change in the
secondary structure of the protein (circular dichroism measurements). Besides, PCB
protects α2M from structural oxidative alterations under AAPH-induced free radical
overproduction. Further, PCB binding effectively preserves α2M anti-proteinase activity.
Since α2M is involved in controlling the action of enzymes during the inflammatory
process, the protection that PCB expresses could indirectly influence the intensity and
direction of body response to impaired homeostasis, especially under oxidative stress.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Tenth Conference with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia",
title = "Interaction between alpha-2-macroglobulin and phycocyanobilin – structural and physiological implications",
pages = "163-163",
url = "https://hdl.handle.net/21.15107/rcub_cer_7289"
}

Šunderić, M., Gligorijević, N., Minić, S., Nedić, O.,& Nikolić, M.. (2021). Interaction between alpha-2-macroglobulin and phycocyanobilin – structural and physiological implications. in Serbian Biochemical Society Tenth Conference with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia
Serbian Biochemical Society., 163-163.
https://hdl.handle.net/21.15107/rcub_cer_7289

Šunderić M, Gligorijević N, Minić S, Nedić O, Nikolić M. Interaction between alpha-2-macroglobulin and phycocyanobilin – structural and physiological implications. in Serbian Biochemical Society Tenth Conference with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia. 2021;:163-163.
https://hdl.handle.net/21.15107/rcub_cer_7289 .

Šunderić, Miloš, Gligorijević, Nikola, Minić, Simeon, Nedić, Olgica, Nikolić, Milan, "Interaction between alpha-2-macroglobulin and phycocyanobilin – structural and physiological implications" in Serbian Biochemical Society Tenth Conference with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia (2021):163-163,
https://hdl.handle.net/21.15107/rcub_cer_7289 .

TY  - CONF
AU  - Gligorijević, Nikola
AU  - Šunderić, Miloš
AU  - Vilotić, Aleksandra
AU  - Baralić, Marko
AU  - Nedić, Olgica
PY  - 2019
UR  - http://www.bds.org.rs/download/SBS_Conference_09_2019.pdf
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7291
AB  - Alpha-2-macroglobulin (α2M) is a homotetrameric blood glycoprotein having molecular
mass of 720 kDa which acts as a general protease inhibitor 1. So far, the methods to
estimate the quantity of α2M and its activity were separate procedures. The quantity is
usually measured by immunochemical assays and the anti-protease activity of α2M by
measuring the activity of trypsin bound to α2M using chromogenic substrate BAPNA 2. A
simple and reliable method for determination of the concentration and function of α2M by
zymography was developed. This method is based on the covalent binding of α2M and
trypsin followed by non-reducing PAGE and zymography with gelatine incorporated in the
electrophoretic gel. The results have shown that α2M binds trypsin in a linear,
concentration-dependent manner. The sensitivity of the method is 125 nM with an intraassay
coefficient of variation 4.2 %. Freezing of α2M induces its partial denaturation,
which can be seen as the reduction in the amount of functional molecule and its reactivity
with trypsin. The method was further tested using α2M from patients with an end-stage
renal disease who are known to be under an increased oxidative stress and inflammation,
which are expected to modify the structure of proteins. Using α2M from these patients,
lower affinity of α2M towards trypsin was detected when compaired to α2M isolated from
healthy persons. The reported zymographic method enables measurement of α2M taking
into consideration both its quantity and function, stressing the importance of determination
of the amount of physiologically active molecules and not just their total amount present in
the sample. Monitoring of the relation quantity/activity becomes very important when the
sample originates from an individual exposed to a stress or with a disease accompanied by
post-translational modifications of proteins such as diabetes, renal disease or cancer 3.
Presented method also enables determination of α2M in the presence of different modifying
chemical substances.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Ninth Conference with international participation,  “Diversity in Biochemistry”, 14-16.11.2019, University of Belgrade – Kolarac Endowment, Belgrade, Serbia
T1  - Quantitation of the active alpha-2-macroglobulin by trypsin protease zymography
SP  - 98
EP  - 98
UR  - https://hdl.handle.net/21.15107/rcub_cer_7291
ER  - 

@conference{
author = "Gligorijević, Nikola and Šunderić, Miloš and Vilotić, Aleksandra and Baralić, Marko and Nedić, Olgica",
year = "2019",
abstract = "Alpha-2-macroglobulin (α2M) is a homotetrameric blood glycoprotein having molecular
mass of 720 kDa which acts as a general protease inhibitor 1. So far, the methods to
estimate the quantity of α2M and its activity were separate procedures. The quantity is
usually measured by immunochemical assays and the anti-protease activity of α2M by
measuring the activity of trypsin bound to α2M using chromogenic substrate BAPNA 2. A
simple and reliable method for determination of the concentration and function of α2M by
zymography was developed. This method is based on the covalent binding of α2M and
trypsin followed by non-reducing PAGE and zymography with gelatine incorporated in the
electrophoretic gel. The results have shown that α2M binds trypsin in a linear,
concentration-dependent manner. The sensitivity of the method is 125 nM with an intraassay
coefficient of variation 4.2 %. Freezing of α2M induces its partial denaturation,
which can be seen as the reduction in the amount of functional molecule and its reactivity
with trypsin. The method was further tested using α2M from patients with an end-stage
renal disease who are known to be under an increased oxidative stress and inflammation,
which are expected to modify the structure of proteins. Using α2M from these patients,
lower affinity of α2M towards trypsin was detected when compaired to α2M isolated from
healthy persons. The reported zymographic method enables measurement of α2M taking
into consideration both its quantity and function, stressing the importance of determination
of the amount of physiologically active molecules and not just their total amount present in
the sample. Monitoring of the relation quantity/activity becomes very important when the
sample originates from an individual exposed to a stress or with a disease accompanied by
post-translational modifications of proteins such as diabetes, renal disease or cancer 3.
Presented method also enables determination of α2M in the presence of different modifying
chemical substances.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Ninth Conference with international participation,  “Diversity in Biochemistry”, 14-16.11.2019, University of Belgrade – Kolarac Endowment, Belgrade, Serbia",
title = "Quantitation of the active alpha-2-macroglobulin by trypsin protease zymography",
pages = "98-98",
url = "https://hdl.handle.net/21.15107/rcub_cer_7291"
}

Gligorijević, N., Šunderić, M., Vilotić, A., Baralić, M.,& Nedić, O.. (2019). Quantitation of the active alpha-2-macroglobulin by trypsin protease zymography. in Serbian Biochemical Society Ninth Conference with international participation,  “Diversity in Biochemistry”, 14-16.11.2019, University of Belgrade – Kolarac Endowment, Belgrade, Serbia
Serbian Biochemical Society., 98-98.
https://hdl.handle.net/21.15107/rcub_cer_7291

Gligorijević N, Šunderić M, Vilotić A, Baralić M, Nedić O. Quantitation of the active alpha-2-macroglobulin by trypsin protease zymography. in Serbian Biochemical Society Ninth Conference with international participation,  “Diversity in Biochemistry”, 14-16.11.2019, University of Belgrade – Kolarac Endowment, Belgrade, Serbia. 2019;:98-98.
https://hdl.handle.net/21.15107/rcub_cer_7291 .

Gligorijević, Nikola, Šunderić, Miloš, Vilotić, Aleksandra, Baralić, Marko, Nedić, Olgica, "Quantitation of the active alpha-2-macroglobulin by trypsin protease zymography" in Serbian Biochemical Society Ninth Conference with international participation,  “Diversity in Biochemistry”, 14-16.11.2019, University of Belgrade – Kolarac Endowment, Belgrade, Serbia (2019):98-98,
https://hdl.handle.net/21.15107/rcub_cer_7291 .