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  - CONF
AU  - Jovanović, Zorana
AU  - Annighöfer, Burkhard
AU  - Dudzinski, Daniel
AU  - Gligorijević, Nikola
AU  - Nikolić, Milan
AU  - Pavlović, Vladimir B.
AU  - Lević, Steva
AU  - Brûlet, Annie
AU  - Assifaoui, Ali
AU  - Combet, Sophie
AU  - Minić, Simeon
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7521
AB  - Our study aimed to preserve the natural blue dye of C-phycocyanin (C-PC)
phycobiliprotein from Spirulina microalgae due to its importance in the food industry. We
incorporated C-PC into hydrogels formed by combining starch and β-lactoglobulin (BLG)
using high-pressure (HP) processing to achieve this objective. Notably, thermal treatment
resulted in the complete loss of colour derived from C-PC.
We performed a comprehensive characterization of the resulting HP gels by rheology
measurements, texture profile analysis (TPA), small-angle X-ray scattering (SAXS), and
scanning electron microscopy (SEM).
Different compositions of binary (BLG/C-PC) and ternary (starch/BLG/C-PC)
systems were processed under high-pressure (HP) conditions reaching up to 4,500 bar. The
C-PC pigment was effectively preserved by mixing BLG and starch with C-PC at pH 7,
maintaining concentrations of 180, 5, and 10 mg/mL, respectively. The same concentrations
of components were retained in the binary systems.
Rheological properties of the gels were determined using a rheometer with
plane/plane geometry, and texture analysis was conducted through TPA. These findings
enabled the assessment of food gel's properties, such as hardness, springiness, chewiness, and
cohesiveness. The structural characteristics of the gels were determined by SAXS, offering
insights into the interactions between C-PC, BLG, and starch after HP processing. Adding CPC
and starch formed solid gels with a larger mesh than the pure BLG gels. SEM scans of the
gel surface revealed that all components influenced the overall morphology of gels. Even at
low concentrations, the addition of starch notably influenced the gels' visual appearance and
mechanical properties. Our investigation highlights the superior effectiveness of HP treatment
in the preservation of C-PC compared to high-temperature treatment, evident in the sustained
colour integrity of the C-PC blue dye.
PB  - Faculty of Technology and Metallurgy, University of Belgrade
C3  - Book of abstracts - International Conference on Biochemical Engineering and Biotechnology for Young Scientists, Belgrade
T1  - The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin
SP  - 60
EP  - 60
UR  - https://hdl.handle.net/21.15107/rcub_cer_7521
ER  - 

@conference{
author = "Jovanović, Zorana and Annighöfer, Burkhard and Dudzinski, Daniel and Gligorijević, Nikola and Nikolić, Milan and Pavlović, Vladimir B. and Lević, Steva and Brûlet, Annie and Assifaoui, Ali and Combet, Sophie and Minić, Simeon",
year = "2023",
abstract = "Our study aimed to preserve the natural blue dye of C-phycocyanin (C-PC)
phycobiliprotein from Spirulina microalgae due to its importance in the food industry. We
incorporated C-PC into hydrogels formed by combining starch and β-lactoglobulin (BLG)
using high-pressure (HP) processing to achieve this objective. Notably, thermal treatment
resulted in the complete loss of colour derived from C-PC.
We performed a comprehensive characterization of the resulting HP gels by rheology
measurements, texture profile analysis (TPA), small-angle X-ray scattering (SAXS), and
scanning electron microscopy (SEM).
Different compositions of binary (BLG/C-PC) and ternary (starch/BLG/C-PC)
systems were processed under high-pressure (HP) conditions reaching up to 4,500 bar. The
C-PC pigment was effectively preserved by mixing BLG and starch with C-PC at pH 7,
maintaining concentrations of 180, 5, and 10 mg/mL, respectively. The same concentrations
of components were retained in the binary systems.
Rheological properties of the gels were determined using a rheometer with
plane/plane geometry, and texture analysis was conducted through TPA. These findings
enabled the assessment of food gel's properties, such as hardness, springiness, chewiness, and
cohesiveness. The structural characteristics of the gels were determined by SAXS, offering
insights into the interactions between C-PC, BLG, and starch after HP processing. Adding CPC
and starch formed solid gels with a larger mesh than the pure BLG gels. SEM scans of the
gel surface revealed that all components influenced the overall morphology of gels. Even at
low concentrations, the addition of starch notably influenced the gels' visual appearance and
mechanical properties. Our investigation highlights the superior effectiveness of HP treatment
in the preservation of C-PC compared to high-temperature treatment, evident in the sustained
colour integrity of the C-PC blue dye.",
publisher = "Faculty of Technology and Metallurgy, University of Belgrade",
journal = "Book of abstracts - International Conference on Biochemical Engineering and Biotechnology for Young Scientists, Belgrade",
title = "The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin",
pages = "60-60",
url = "https://hdl.handle.net/21.15107/rcub_cer_7521"
}

Jovanović, Z., Annighöfer, B., Dudzinski, D., Gligorijević, N., Nikolić, M., Pavlović, V. B., Lević, S., Brûlet, A., Assifaoui, A., Combet, S.,& Minić, S.. (2023). The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin. in Book of abstracts - International Conference on Biochemical Engineering and Biotechnology for Young Scientists, Belgrade
Faculty of Technology and Metallurgy, University of Belgrade., 60-60.
https://hdl.handle.net/21.15107/rcub_cer_7521

Jovanović Z, Annighöfer B, Dudzinski D, Gligorijević N, Nikolić M, Pavlović VB, Lević S, Brûlet A, Assifaoui A, Combet S, Minić S. The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin. in Book of abstracts - International Conference on Biochemical Engineering and Biotechnology for Young Scientists, Belgrade. 2023;:60-60.
https://hdl.handle.net/21.15107/rcub_cer_7521 .

Jovanović, Zorana, Annighöfer, Burkhard, Dudzinski, Daniel, Gligorijević, Nikola, Nikolić, Milan, Pavlović, Vladimir B., Lević, Steva, Brûlet, Annie, Assifaoui, Ali, Combet, Sophie, Minić, Simeon, "The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin" in Book of abstracts - International Conference on Biochemical Engineering and Biotechnology for Young Scientists, Belgrade (2023):60-60,
https://hdl.handle.net/21.15107/rcub_cer_7521 .

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  - JOUR
AU  - Veličković, Luka
AU  - Simović, Ana
AU  - Gligorijević, Nikola
AU  - Thureau, Aurelien
AU  - Obradović, Milica
AU  - Vasović, Tamara
AU  - Sotiroudis, Georgios
AU  - Zoumpanioti, Maria
AU  - Brulet, Annie
AU  - Ćirković Veličković, Tanja
AU  - Combet, Sophie
AU  - Nikolić, Milan
AU  - Minić, Simeon
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6473
AB  - This study aimed to purify, characterise and stabilise the natural food colourant, R-phycocyanin (R-PC), from the red algae Porphyra spp. (Nori). We purified R-PC from dried Nori flakes with a high purity ratio (A618/A280 ≥ 3.4) in native form (α-helix content 53%). SAXS measurements revealed that R-PC is trimeric ((αβ)3) in solution. The thermal denaturation of α-helix revealed one transition (Tm at 52 ◦C), while the pH stability study showed R-PC is stable in the pH range 4–8. The thermal treatment of R-PC at 60 °C has detrimental and irreversible effects on RPC colour and antioxidant capacity (22 % of residual capacity). However, immobilisation of R-PC within calcium alginate beads completely preserves R-PC colour and mainly retains its antioxidant ability (78 % of residual
capacity). Results give new insights into the stability of R-PC and preservation of its purple colour and bioactivity by encapsulation in calcium alginate beads.
PB  - Elsevier Ltd.
T2  - Food Chemistry
T1  - Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant
VL  - 426
SP  - 136669
DO  - 10.1016/j.foodchem.2023.136669
ER  - 

@article{
author = "Veličković, Luka and Simović, Ana and Gligorijević, Nikola and Thureau, Aurelien and Obradović, Milica and Vasović, Tamara and Sotiroudis, Georgios and Zoumpanioti, Maria and Brulet, Annie and Ćirković Veličković, Tanja and Combet, Sophie and Nikolić, Milan and Minić, Simeon",
year = "2023",
abstract = "This study aimed to purify, characterise and stabilise the natural food colourant, R-phycocyanin (R-PC), from the red algae Porphyra spp. (Nori). We purified R-PC from dried Nori flakes with a high purity ratio (A618/A280 ≥ 3.4) in native form (α-helix content 53%). SAXS measurements revealed that R-PC is trimeric ((αβ)3) in solution. The thermal denaturation of α-helix revealed one transition (Tm at 52 ◦C), while the pH stability study showed R-PC is stable in the pH range 4–8. The thermal treatment of R-PC at 60 °C has detrimental and irreversible effects on RPC colour and antioxidant capacity (22 % of residual capacity). However, immobilisation of R-PC within calcium alginate beads completely preserves R-PC colour and mainly retains its antioxidant ability (78 % of residual
capacity). Results give new insights into the stability of R-PC and preservation of its purple colour and bioactivity by encapsulation in calcium alginate beads.",
publisher = "Elsevier Ltd.",
journal = "Food Chemistry",
title = "Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant",
volume = "426",
pages = "136669",
doi = "10.1016/j.foodchem.2023.136669"
}

Veličković, L., Simović, A., Gligorijević, N., Thureau, A., Obradović, M., Vasović, T., Sotiroudis, G., Zoumpanioti, M., Brulet, A., Ćirković Veličković, T., Combet, S., Nikolić, M.,& Minić, S.. (2023). Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant. in Food Chemistry
Elsevier Ltd.., 426, 136669.
https://doi.org/10.1016/j.foodchem.2023.136669

Veličković L, Simović A, Gligorijević N, Thureau A, Obradović M, Vasović T, Sotiroudis G, Zoumpanioti M, Brulet A, Ćirković Veličković T, Combet S, Nikolić M, Minić S. Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant. in Food Chemistry. 2023;426:136669.
doi:10.1016/j.foodchem.2023.136669 .

Veličković, Luka, Simović, Ana, Gligorijević, Nikola, Thureau, Aurelien, Obradović, Milica, Vasović, Tamara, Sotiroudis, Georgios, Zoumpanioti, Maria, Brulet, Annie, Ćirković Veličković, Tanja, Combet, Sophie, Nikolić, Milan, Minić, Simeon, "Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant" in Food Chemistry, 426 (2023):136669,
https://doi.org/10.1016/j.foodchem.2023.136669 . .

TY  - JOUR
AU  - Platanić Arizanović, Lena
AU  - Gligorijević, Nikola
AU  - Cvijetić, Ilija
AU  - Mijatović, Aleksandar
AU  - Krstić Ristivojević, Maja
AU  - Minić, Simeon
AU  - Nikolić Kokić, Aleksandra
AU  - Miljević, Čedo
AU  - Nikolić, Milan
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6482
AB  - Packed with hemoglobin, an essential protein for oxygen transport, human erythrocytes
are a suitable model system for testing the pleiotropic effects of lipophilic drugs. Our study investigated the interaction between antipsychotic drugs clozapine, ziprasidone, sertindole, and human hemoglobin under simulated physiological conditions. Analysis of protein fluorescence quenching at different temperatures and data obtained from the van’t Hoff diagram and molecular docking indicate that the interactions are static and that the tetrameric human hemoglobin has one binding site for all drugs in the central cavity near αβ  interfaces and is dominantly mediated through hydrophobic forces. The association constants were lower-moderate strength (~10^4 M^-1), the highest observed for clozapine (2.2 x 10^4 M^-1 at 25 °C). The clozapine binding showed “friendly” effects: increased α-helical content, a higher melting point, and protein protection from free radical-mediated oxidation. On the other hand, bound ziprasidone and sertindole had a slightly pro-oxidative effect, increasing ferrihemoglobin content, a possible “foe”. Since the interaction of proteins with drugs plays a vital role in their pharmacokinetic and pharmacodynamic properties, the physiological significance of the obtained findings is briefly discussed.
PB  - Multidisciplinary Digital Publishing Institute (MDPI)
T2  - International Journal of Molecular Sciences
T1  - Human Hemoglobin and Antipsychotics Clozapine, Ziprasidone and Sertindole: Friends or Foes?
VL  - 24
IS  - 10
SP  - 8921
DO  - 10.3390/ijms24108921
ER  - 

@article{
author = "Platanić Arizanović, Lena and Gligorijević, Nikola and Cvijetić, Ilija and Mijatović, Aleksandar and Krstić Ristivojević, Maja and Minić, Simeon and Nikolić Kokić, Aleksandra and Miljević, Čedo and Nikolić, Milan",
year = "2023",
abstract = "Packed with hemoglobin, an essential protein for oxygen transport, human erythrocytes
are a suitable model system for testing the pleiotropic effects of lipophilic drugs. Our study investigated the interaction between antipsychotic drugs clozapine, ziprasidone, sertindole, and human hemoglobin under simulated physiological conditions. Analysis of protein fluorescence quenching at different temperatures and data obtained from the van’t Hoff diagram and molecular docking indicate that the interactions are static and that the tetrameric human hemoglobin has one binding site for all drugs in the central cavity near αβ  interfaces and is dominantly mediated through hydrophobic forces. The association constants were lower-moderate strength (~10^4 M^-1), the highest observed for clozapine (2.2 x 10^4 M^-1 at 25 °C). The clozapine binding showed “friendly” effects: increased α-helical content, a higher melting point, and protein protection from free radical-mediated oxidation. On the other hand, bound ziprasidone and sertindole had a slightly pro-oxidative effect, increasing ferrihemoglobin content, a possible “foe”. Since the interaction of proteins with drugs plays a vital role in their pharmacokinetic and pharmacodynamic properties, the physiological significance of the obtained findings is briefly discussed.",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "International Journal of Molecular Sciences",
title = "Human Hemoglobin and Antipsychotics Clozapine, Ziprasidone and Sertindole: Friends or Foes?",
volume = "24",
number = "10",
pages = "8921",
doi = "10.3390/ijms24108921"
}

Platanić Arizanović, L., Gligorijević, N., Cvijetić, I., Mijatović, A., Krstić Ristivojević, M., Minić, S., Nikolić Kokić, A., Miljević, Č.,& Nikolić, M.. (2023). Human Hemoglobin and Antipsychotics Clozapine, Ziprasidone and Sertindole: Friends or Foes?. in International Journal of Molecular Sciences
Multidisciplinary Digital Publishing Institute (MDPI)., 24(10), 8921.
https://doi.org/10.3390/ijms24108921

Platanić Arizanović L, Gligorijević N, Cvijetić I, Mijatović A, Krstić Ristivojević M, Minić S, Nikolić Kokić A, Miljević Č, Nikolić M. Human Hemoglobin and Antipsychotics Clozapine, Ziprasidone and Sertindole: Friends or Foes?. in International Journal of Molecular Sciences. 2023;24(10):8921.
doi:10.3390/ijms24108921 .

Platanić Arizanović, Lena, Gligorijević, Nikola, Cvijetić, Ilija, Mijatović, Aleksandar, Krstić Ristivojević, Maja, Minić, Simeon, Nikolić Kokić, Aleksandra, Miljević, Čedo, Nikolić, Milan, "Human Hemoglobin and Antipsychotics Clozapine, Ziprasidone and Sertindole: Friends or Foes?" in International Journal of Molecular Sciences, 24, no. 10 (2023):8921,
https://doi.org/10.3390/ijms24108921 . .

TY  - JOUR
AU  - Nedić, Olgica
AU  - Penezić, Ana
AU  - Minić, Simeon
AU  - Radomirović, Mirjana
AU  - Nikolić, Milan
AU  - Ćirković Veličković, Tanja
AU  - Gligorijević, Nikola
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6485
AB  - Common to all biological systems and living organisms are molecular interactions, which
may lead to specific physiological events. Most often, a cascade of events occurs, establishing an
equilibrium between possibly competing and/or synergistic processes. Biochemical pathways that
sustain life depend on multiple intrinsic and extrinsic factors contributing to aging and/or diseases.
This article deals with food antioxidants and human proteins from the circulation, their interaction,
their effect on the structure, properties, and function of antioxidant-bound proteins, and the possible
impact of complex formation on antioxidants. An overview of studies examining interactions between
individual antioxidant compounds and major blood proteins is presented with findings. Investigating
antioxidant/protein interactions at the level of the human organism and determining antioxidant
distribution between proteins and involvement in the particular physiological role is a very complex
and challenging task. However, by knowing the role of a particular protein in certain pathology or
aging, and the effect exerted by a particular antioxidant bound to it, it is possible to recommend
specific food intake or resistance to it to improve the condition or slow down the process.
PB  - Multidisciplinary Digital Publishing Institute (MDPI)
T2  - Antioxidants
T1  - Food Antioxidants and Their Interaction with Human Proteins
VL  - 12
IS  - 4
SP  - 815
DO  - 10.3390/antiox12040815
ER  - 

@article{
author = "Nedić, Olgica and Penezić, Ana and Minić, Simeon and Radomirović, Mirjana and Nikolić, Milan and Ćirković Veličković, Tanja and Gligorijević, Nikola",
year = "2023",
abstract = "Common to all biological systems and living organisms are molecular interactions, which
may lead to specific physiological events. Most often, a cascade of events occurs, establishing an
equilibrium between possibly competing and/or synergistic processes. Biochemical pathways that
sustain life depend on multiple intrinsic and extrinsic factors contributing to aging and/or diseases.
This article deals with food antioxidants and human proteins from the circulation, their interaction,
their effect on the structure, properties, and function of antioxidant-bound proteins, and the possible
impact of complex formation on antioxidants. An overview of studies examining interactions between
individual antioxidant compounds and major blood proteins is presented with findings. Investigating
antioxidant/protein interactions at the level of the human organism and determining antioxidant
distribution between proteins and involvement in the particular physiological role is a very complex
and challenging task. However, by knowing the role of a particular protein in certain pathology or
aging, and the effect exerted by a particular antioxidant bound to it, it is possible to recommend
specific food intake or resistance to it to improve the condition or slow down the process.",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "Antioxidants",
title = "Food Antioxidants and Their Interaction with Human Proteins",
volume = "12",
number = "4",
pages = "815",
doi = "10.3390/antiox12040815"
}

Nedić, O., Penezić, A., Minić, S., Radomirović, M., Nikolić, M., Ćirković Veličković, T.,& Gligorijević, N.. (2023). Food Antioxidants and Their Interaction with Human Proteins. in Antioxidants
Multidisciplinary Digital Publishing Institute (MDPI)., 12(4), 815.
https://doi.org/10.3390/antiox12040815

Nedić O, Penezić A, Minić S, Radomirović M, Nikolić M, Ćirković Veličković T, Gligorijević N. Food Antioxidants and Their Interaction with Human Proteins. in Antioxidants. 2023;12(4):815.
doi:10.3390/antiox12040815 .

Nedić, Olgica, Penezić, Ana, Minić, Simeon, Radomirović, Mirjana, Nikolić, Milan, Ćirković Veličković, Tanja, Gligorijević, Nikola, "Food Antioxidants and Their Interaction with Human Proteins" in Antioxidants, 12, no. 4 (2023):815,
https://doi.org/10.3390/antiox12040815 . .

TY  - CONF
AU  - Veličković, Luka
AU  - Simović, Ana
AU  - Gligorijević, Nikola
AU  - Obradović, Milica
AU  - Sotiroudis, Georgios
AU  - Zoumpanioti, Maria
AU  - Minić, Simeon
AU  - Nikolić, Milan
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6505
AB  - Purple R-phycocyanin is a protein from red algae with the potential for application in the food industry (colorant) and wastewater treatment (binding of heavy metals). Analytical grade R-phycocyanin was purified from the buffered extract of dried Nori flakes (Porphyra spp.) by combining ammonium sulfate precipitation, hydroxyapatite, and DEAE-Sepharose column chromatography. The multimeric protein had absorption maxima characteristic for phycoerythrobilin (at 580 nm) and phycocyanobilin (at 640 nm) chromophores, high α- helical content, and melting temperature of 52°C. The secondary R-PC structure was stable under a wide range of pH values (3–9). R-phycocyanin immobilized in calcium alginate beads showed increased thermal stability and preserved antioxidant activity.
AB  - Ljubičasti R-fikocijanin je protein crvenih algi sa mogućnostima primene u industriji hrane (kolorant) i za tretman otpadnih voda (vezuje teške metale). R-fikocijanin analitičke čistoće je izolovan iz puferisanog ekstrakta osušenih Nori algi (Porphyra spp.), kombinacijom taloženja amonijum-sulfatom, hidroksiapatitne i hromatografije na DEAE-Sepharose koloni. Multimerni protein imao je apsorpcione maksimume karakteristične za fikoeritrobilinsku (na 580 nm) i fikocijanobilinsku (na 640 nm) hromoforu, visok sadržaj α-zavojnica i temperaturu topljenja od 52°C. Sekundarna struktura proteina bila je stabilna u širokom rasponu pH vrednosti (3–9). R-fikocijanin imobilisan u kuglice kalcijum-alginata pokazao je povećanu toplotnu stabilnost i očuvana antioksidativna svojstva.
PB  - Belgrade : Serbian Chemical Society
C3  - Kratki izvodi radova, knjiga radova - 59. Savetovanje Srpskog hemijskog društva, 1. i 2. jun 2023. godine, Novi Sad / Book of Abstracts, Proceedings - 59th Meeting of the Serbian Chemical Society, June 1-2, 2023, Novi Sad, Serbia
T1  - Purification and structural characterization of R-phycocyanin
T1  - Prečišćavanje i strukturna karakterizacija R-fikocijanina
SP  - 53
EP  - 53
UR  - https://hdl.handle.net/21.15107/rcub_cer_6505
ER  - 

@conference{
author = "Veličković, Luka and Simović, Ana and Gligorijević, Nikola and Obradović, Milica and Sotiroudis, Georgios and Zoumpanioti, Maria and Minić, Simeon and Nikolić, Milan",
year = "2023",
abstract = "Purple R-phycocyanin is a protein from red algae with the potential for application in the food industry (colorant) and wastewater treatment (binding of heavy metals). Analytical grade R-phycocyanin was purified from the buffered extract of dried Nori flakes (Porphyra spp.) by combining ammonium sulfate precipitation, hydroxyapatite, and DEAE-Sepharose column chromatography. The multimeric protein had absorption maxima characteristic for phycoerythrobilin (at 580 nm) and phycocyanobilin (at 640 nm) chromophores, high α- helical content, and melting temperature of 52°C. The secondary R-PC structure was stable under a wide range of pH values (3–9). R-phycocyanin immobilized in calcium alginate beads showed increased thermal stability and preserved antioxidant activity., Ljubičasti R-fikocijanin je protein crvenih algi sa mogućnostima primene u industriji hrane (kolorant) i za tretman otpadnih voda (vezuje teške metale). R-fikocijanin analitičke čistoće je izolovan iz puferisanog ekstrakta osušenih Nori algi (Porphyra spp.), kombinacijom taloženja amonijum-sulfatom, hidroksiapatitne i hromatografije na DEAE-Sepharose koloni. Multimerni protein imao je apsorpcione maksimume karakteristične za fikoeritrobilinsku (na 580 nm) i fikocijanobilinsku (na 640 nm) hromoforu, visok sadržaj α-zavojnica i temperaturu topljenja od 52°C. Sekundarna struktura proteina bila je stabilna u širokom rasponu pH vrednosti (3–9). R-fikocijanin imobilisan u kuglice kalcijum-alginata pokazao je povećanu toplotnu stabilnost i očuvana antioksidativna svojstva.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Kratki izvodi radova, knjiga radova - 59. Savetovanje Srpskog hemijskog društva, 1. i 2. jun 2023. godine, Novi Sad / Book of Abstracts, Proceedings - 59th Meeting of the Serbian Chemical Society, June 1-2, 2023, Novi Sad, Serbia",
title = "Purification and structural characterization of R-phycocyanin, Prečišćavanje i strukturna karakterizacija R-fikocijanina",
pages = "53-53",
url = "https://hdl.handle.net/21.15107/rcub_cer_6505"
}

Veličković, L., Simović, A., Gligorijević, N., Obradović, M., Sotiroudis, G., Zoumpanioti, M., Minić, S.,& Nikolić, M.. (2023). Purification and structural characterization of R-phycocyanin. in Kratki izvodi radova, knjiga radova - 59. Savetovanje Srpskog hemijskog društva, 1. i 2. jun 2023. godine, Novi Sad / Book of Abstracts, Proceedings - 59th Meeting of the Serbian Chemical Society, June 1-2, 2023, Novi Sad, Serbia
Belgrade : Serbian Chemical Society., 53-53.
https://hdl.handle.net/21.15107/rcub_cer_6505

Veličković L, Simović A, Gligorijević N, Obradović M, Sotiroudis G, Zoumpanioti M, Minić S, Nikolić M. Purification and structural characterization of R-phycocyanin. in Kratki izvodi radova, knjiga radova - 59. Savetovanje Srpskog hemijskog društva, 1. i 2. jun 2023. godine, Novi Sad / Book of Abstracts, Proceedings - 59th Meeting of the Serbian Chemical Society, June 1-2, 2023, Novi Sad, Serbia. 2023;:53-53.
https://hdl.handle.net/21.15107/rcub_cer_6505 .

Veličković, Luka, Simović, Ana, Gligorijević, Nikola, Obradović, Milica, Sotiroudis, Georgios, Zoumpanioti, Maria, Minić, Simeon, Nikolić, Milan, "Purification and structural characterization of R-phycocyanin" in Kratki izvodi radova, knjiga radova - 59. Savetovanje Srpskog hemijskog društva, 1. i 2. jun 2023. godine, Novi Sad / Book of Abstracts, Proceedings - 59th Meeting of the Serbian Chemical Society, June 1-2, 2023, Novi Sad, Serbia (2023):53-53,
https://hdl.handle.net/21.15107/rcub_cer_6505 .

TY  - CONF
AU  - Gligorijević, Nikola
AU  - Veličković, Luka
AU  - Svrzić, Nikola
AU  - Jovanović, Zorana
AU  - Minić, Simeon
AU  - Nikolić, Milan
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6519
AB  - C-Phycocyanin (C-PC), the major protein of cyanobacteria Arthrospira platensis, is a phycobiliprotein with potent biological activity. It has several beneficial effects, including anti-oxidant, anti-inflammatory, immunomodulatory, and anti-cancer. A significant challenge for the broader application of C-PC in the food industry is its stability in food processing conditions, such
as increased light exposure, temperature, and high pressure and drying. This work aimed to investigate if the immobilization of C-PC onto alginate beads could improve its stability. C-PC was
immobilized by dropping the solution of C-PC and 1% alginate (final concentration) in the solution of 2% CaCl2. Both protein/alginate mixture and CaCl2 were kept at pH 4. Immobilized CPC
was treated for 30 min at 65°C, by high pressure up to 4500 bar, and incubated under light exposure for a month. Alginate beads with immobilized C-PC were also left to dry in the fridge and kept for a month. C-PC was extracted from alginate beads by immersing them in 20 mM phosphate buffer, pH 7. The stability of C-PC was assessed by a color change and UV-VIS spectroscopy. Immobilized C-PC was stable under all tested conditions, with only small aggregation and color change appearing
after high-pressure treatment. Immobilization of C-PC by alginate thus shows promise for its efficient stabilization under food processing conditions.
PB  - Wiley
C3  - FEBS Open Bio
T1  - Stabilization of C-phycocyanin by immobilization in alginate beads
VL  - 13
IS  - S2
SP  - 234
EP  - 234
DO  - 10.1002/2211-5463.13646
ER  - 

@conference{
author = "Gligorijević, Nikola and Veličković, Luka and Svrzić, Nikola and Jovanović, Zorana and Minić, Simeon and Nikolić, Milan",
year = "2023",
abstract = "C-Phycocyanin (C-PC), the major protein of cyanobacteria Arthrospira platensis, is a phycobiliprotein with potent biological activity. It has several beneficial effects, including anti-oxidant, anti-inflammatory, immunomodulatory, and anti-cancer. A significant challenge for the broader application of C-PC in the food industry is its stability in food processing conditions, such
as increased light exposure, temperature, and high pressure and drying. This work aimed to investigate if the immobilization of C-PC onto alginate beads could improve its stability. C-PC was
immobilized by dropping the solution of C-PC and 1% alginate (final concentration) in the solution of 2% CaCl2. Both protein/alginate mixture and CaCl2 were kept at pH 4. Immobilized CPC
was treated for 30 min at 65°C, by high pressure up to 4500 bar, and incubated under light exposure for a month. Alginate beads with immobilized C-PC were also left to dry in the fridge and kept for a month. C-PC was extracted from alginate beads by immersing them in 20 mM phosphate buffer, pH 7. The stability of C-PC was assessed by a color change and UV-VIS spectroscopy. Immobilized C-PC was stable under all tested conditions, with only small aggregation and color change appearing
after high-pressure treatment. Immobilization of C-PC by alginate thus shows promise for its efficient stabilization under food processing conditions.",
publisher = "Wiley",
journal = "FEBS Open Bio",
title = "Stabilization of C-phycocyanin by immobilization in alginate beads",
volume = "13",
number = "S2",
pages = "234-234",
doi = "10.1002/2211-5463.13646"
}

Gligorijević, N., Veličković, L., Svrzić, N., Jovanović, Z., Minić, S.,& Nikolić, M.. (2023). Stabilization of C-phycocyanin by immobilization in alginate beads. in FEBS Open Bio
Wiley., 13(S2), 234-234.
https://doi.org/10.1002/2211-5463.13646

Gligorijević N, Veličković L, Svrzić N, Jovanović Z, Minić S, Nikolić M. Stabilization of C-phycocyanin by immobilization in alginate beads. in FEBS Open Bio. 2023;13(S2):234-234.
doi:10.1002/2211-5463.13646 .

Gligorijević, Nikola, Veličković, Luka, Svrzić, Nikola, Jovanović, Zorana, Minić, Simeon, Nikolić, Milan, "Stabilization of C-phycocyanin by immobilization in alginate beads" in FEBS Open Bio, 13, no. S2 (2023):234-234,
https://doi.org/10.1002/2211-5463.13646 . .

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  - Ivanov, Aleksandar
AU  - Veličković, Luka
AU  - Jovanović, Zorana
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Nikolić, Milan
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6665
AB  - C-phycocyanin (C-PC) is a photosynthetic protein from Arthrospira platensis
(cyanobacteria). Due to its intense blue colour, which is very rare in nature, C-PC has
industrial applications as a food colourant as a substitute for synthetic food colourants.
Disadvantages of C-PC as a food colourant are its poor stability at high temperatures
(during thermal treatment of the food) and its sensibility to change pH value. The binding
of food-derived small molecules, such as vitamins, could stabilize the structure of C-PC at
high temperatures and wide pH ranges. In this study, we characterized the binding of
selected vitamins to C-PC, purified from the commercial powder of Arthrospira platensis.
We used hydrophilic vitamins (B1, B2, B7, B9, B12), lipophilic vitamins (A, D3) and
provitamin (β-carotene). Fluorescent spectroscopy showed a decrease in fluorescence of CPC
i n t he p resence o f v itamin A, v itamin D3 a nd β -carotene (lipophilic molecules)
compared to the control. In contrast, the fluorescence of C-PC in the presence of
hydrophilic vitamins showed minimal change. The protein fluorescence quenching
approach demonstrated hydrophobic (pro)vitamins binding affinities ranging from 0.02 to
5.9 x 105 M-1, with the ability of hydrophobic (pro)vitamins to bind at the different sites on
C-PC. UV-VIS spectrophotometry showed that the binding of hydrophobic (pro)vitamins
does not affect the protein colour, while CD spectroscopy revealed that the binding of
chosen molecules does not significantly influence the secondary structure of C-PC.
Overall, this study demonstrated C-PC's significant potential in binding hydrophobic
(pro)vitamins, while further research is required to test if these ligands could improve CPC
stability.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
T1  - Examination of C-phycocyanin interactions with selected vitamins
SP  - 106
EP  - 106
UR  - https://hdl.handle.net/21.15107/rcub_cer_6665
ER  - 

@conference{
author = "Ivanov, Aleksandar and Veličković, Luka and Jovanović, Zorana and Gligorijević, Nikola and Minić, Simeon and Nikolić, Milan",
year = "2023",
abstract = "C-phycocyanin (C-PC) is a photosynthetic protein from Arthrospira platensis
(cyanobacteria). Due to its intense blue colour, which is very rare in nature, C-PC has
industrial applications as a food colourant as a substitute for synthetic food colourants.
Disadvantages of C-PC as a food colourant are its poor stability at high temperatures
(during thermal treatment of the food) and its sensibility to change pH value. The binding
of food-derived small molecules, such as vitamins, could stabilize the structure of C-PC at
high temperatures and wide pH ranges. In this study, we characterized the binding of
selected vitamins to C-PC, purified from the commercial powder of Arthrospira platensis.
We used hydrophilic vitamins (B1, B2, B7, B9, B12), lipophilic vitamins (A, D3) and
provitamin (β-carotene). Fluorescent spectroscopy showed a decrease in fluorescence of CPC
i n t he p resence o f v itamin A, v itamin D3 a nd β -carotene (lipophilic molecules)
compared to the control. In contrast, the fluorescence of C-PC in the presence of
hydrophilic vitamins showed minimal change. The protein fluorescence quenching
approach demonstrated hydrophobic (pro)vitamins binding affinities ranging from 0.02 to
5.9 x 105 M-1, with the ability of hydrophobic (pro)vitamins to bind at the different sites on
C-PC. UV-VIS spectrophotometry showed that the binding of hydrophobic (pro)vitamins
does not affect the protein colour, while CD spectroscopy revealed that the binding of
chosen molecules does not significantly influence the secondary structure of C-PC.
Overall, this study demonstrated C-PC's significant potential in binding hydrophobic
(pro)vitamins, while further research is required to test if these ligands could improve CPC
stability.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia",
title = "Examination of C-phycocyanin interactions with selected vitamins",
pages = "106-106",
url = "https://hdl.handle.net/21.15107/rcub_cer_6665"
}

Ivanov, A., Veličković, L., Jovanović, Z., Gligorijević, N., Minić, S.,& Nikolić, M.. (2023). Examination of C-phycocyanin interactions with selected vitamins. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
Serbian Biochemical Society., 106-106.
https://hdl.handle.net/21.15107/rcub_cer_6665

Ivanov A, Veličković L, Jovanović Z, Gligorijević N, Minić S, Nikolić M. Examination of C-phycocyanin interactions with selected vitamins. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia. 2023;:106-106.
https://hdl.handle.net/21.15107/rcub_cer_6665 .

Ivanov, Aleksandar, Veličković, Luka, Jovanović, Zorana, Gligorijević, Nikola, Minić, Simeon, Nikolić, Milan, "Examination of C-phycocyanin interactions with selected vitamins" in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia (2023):106-106,
https://hdl.handle.net/21.15107/rcub_cer_6665 .

TY  - CONF
AU  - Radović, Jelena
AU  - Popović, Dragana
AU  - Ćurčić, Tatjana
AU  - Nikolić, Milan
AU  - Minić, Simeon
AU  - Gligorijević, Nikola
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6666
AB  - This study aimed to improve chitosan polymer's capabilities to absorb mercury by
immobilising phycobiliproteins (PBPs) onto the surface of chitosan beads (chitosan–
PBPs). Phycobiliproteins, light-harvesting proteins from algae and cyanobacteria, have
several industrially essential applications. These proteins can bind heavy metals with high
affinities. Protein extracts obtained from both Arthrospira platensis, with C-phycocyanin
as the dominant phycobiliprotein and Neoporphyra haitanensis, with R-phycocyanin and
R-phycoerythrin as the dominant PBPs, were covalently immobilised onto chitosan beads.
Binding analysis showed that, on average, 54 μg of PBPs were immobilised per bead.
Immobilised proteins were still in their native state, with no visible colour change after
immobilisation. Chitosan–PBPs and chitosan alone were tested for mercury adsorption at
pH 4 and pH 7 by atomic absorption spectroscopy. The tested concentration range of
mercury was from 1 to 70 ppm. Affinity, calculated using Henry's binding isotherm, of
chitosan–PBPs for mercury was higher at both pH values than chitosan alone.
Furthermore, chitosan–PBPs beads were able to absorb significantly more mercury than
chitosan alone. These results show that the covalent immobilisation of PBPs onto chitosan
improves its mercury adsorption characteristics and creates a more efficient eco-friendly
adsorbent for removing mercury ions in the tested concentration range.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
T1  - Applying immobilised phycobiliproteins onto chitosan for efficient mercury removal
SP  - 116
EP  - 116
UR  - https://hdl.handle.net/21.15107/rcub_cer_6666
ER  - 

@conference{
author = "Radović, Jelena and Popović, Dragana and Ćurčić, Tatjana and Nikolić, Milan and Minić, Simeon and Gligorijević, Nikola",
year = "2023",
abstract = "This study aimed to improve chitosan polymer's capabilities to absorb mercury by
immobilising phycobiliproteins (PBPs) onto the surface of chitosan beads (chitosan–
PBPs). Phycobiliproteins, light-harvesting proteins from algae and cyanobacteria, have
several industrially essential applications. These proteins can bind heavy metals with high
affinities. Protein extracts obtained from both Arthrospira platensis, with C-phycocyanin
as the dominant phycobiliprotein and Neoporphyra haitanensis, with R-phycocyanin and
R-phycoerythrin as the dominant PBPs, were covalently immobilised onto chitosan beads.
Binding analysis showed that, on average, 54 μg of PBPs were immobilised per bead.
Immobilised proteins were still in their native state, with no visible colour change after
immobilisation. Chitosan–PBPs and chitosan alone were tested for mercury adsorption at
pH 4 and pH 7 by atomic absorption spectroscopy. The tested concentration range of
mercury was from 1 to 70 ppm. Affinity, calculated using Henry's binding isotherm, of
chitosan–PBPs for mercury was higher at both pH values than chitosan alone.
Furthermore, chitosan–PBPs beads were able to absorb significantly more mercury than
chitosan alone. These results show that the covalent immobilisation of PBPs onto chitosan
improves its mercury adsorption characteristics and creates a more efficient eco-friendly
adsorbent for removing mercury ions in the tested concentration range.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia",
title = "Applying immobilised phycobiliproteins onto chitosan for efficient mercury removal",
pages = "116-116",
url = "https://hdl.handle.net/21.15107/rcub_cer_6666"
}

Radović, J., Popović, D., Ćurčić, T., Nikolić, M., Minić, S.,& Gligorijević, N.. (2023). Applying immobilised phycobiliproteins onto chitosan for efficient mercury removal. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
Serbian Biochemical Society., 116-116.
https://hdl.handle.net/21.15107/rcub_cer_6666

Radović J, Popović D, Ćurčić T, Nikolić M, Minić S, Gligorijević N. Applying immobilised phycobiliproteins onto chitosan for efficient mercury removal. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia. 2023;:116-116.
https://hdl.handle.net/21.15107/rcub_cer_6666 .

Radović, Jelena, Popović, Dragana, Ćurčić, Tatjana, Nikolić, Milan, Minić, Simeon, Gligorijević, Nikola, "Applying immobilised phycobiliproteins onto chitosan for efficient mercury removal" in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia (2023):116-116,
https://hdl.handle.net/21.15107/rcub_cer_6666 .

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  - Jovanović, Zorana
AU  - Annighöfer, Burkhard
AU  - Dudzinski, Daniel
AU  - Veličković, Luka
AU  - Gligorijević, Nikola
AU  - Nikolić, Milan
AU  - Brûlet, Annie
AU  - Assifaoui, Ali
AU  - Combet, Sophie
AU  - Minić, Simeon
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6669
AB  - The color of food products is an important aspect in food industry, and its preservation
remains a big challenge. We aim to preserve the natural blue dye of C-phycocyanin (C-PC)
phycobiliprotein from Spirulina microalgae. For this purpose, we incorporated C-PC in
combined starch and β-lactoglobulin (BLG) hydrogels by using a high-pressure (HP)
process. Indeed, in thermal treatment, the color derived from C-PC is entirely lost. We
characterized the obtained HP gels by both rheology and small-angle X-ray scattering
(SAXS). Various formulations of binary (BLG/C-PC) and ternary (starch/BLG/C-PC)
systems were tested under HP up to 4,500 bar. A good preservation of the C-PC pigment
was established by mixing BLG and starch with C-PC at pH 7, with concentrations of 180,
5, and 10 mg/mL, respectively. Identical component concentrations were maintained in the
binary systems. Structure of gels was characterized by SAXS providing insight of C-PC
interactions with BLG and starch after HP process which leads to the formation of solid
gels with larger mesh compared to two-component systems. This results in enhanced
mechanical properties, which were determined by amplitude and frequency sweep
measurements using a rheometer with applied plane/plane geometry. Therefore, adding
starch, even at small concentration, significantly improves gel visual appearance and
mechanical properties. Our study reveals that preservation through HP treatment is more
effective than high temperature treatment, as visually observed through the sustained color
integrity of C-PC blue dye.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
T1  - Combined hydrogels of starch and β-lactoglobulin as matrices for the preservation of C-phycocyanin
SP  - 150
EP  - 150
UR  - https://hdl.handle.net/21.15107/rcub_cer_6669
ER  - 

@conference{
author = "Jovanović, Zorana and Annighöfer, Burkhard and Dudzinski, Daniel and Veličković, Luka and Gligorijević, Nikola and Nikolić, Milan and Brûlet, Annie and Assifaoui, Ali and Combet, Sophie and Minić, Simeon",
year = "2023",
abstract = "The color of food products is an important aspect in food industry, and its preservation
remains a big challenge. We aim to preserve the natural blue dye of C-phycocyanin (C-PC)
phycobiliprotein from Spirulina microalgae. For this purpose, we incorporated C-PC in
combined starch and β-lactoglobulin (BLG) hydrogels by using a high-pressure (HP)
process. Indeed, in thermal treatment, the color derived from C-PC is entirely lost. We
characterized the obtained HP gels by both rheology and small-angle X-ray scattering
(SAXS). Various formulations of binary (BLG/C-PC) and ternary (starch/BLG/C-PC)
systems were tested under HP up to 4,500 bar. A good preservation of the C-PC pigment
was established by mixing BLG and starch with C-PC at pH 7, with concentrations of 180,
5, and 10 mg/mL, respectively. Identical component concentrations were maintained in the
binary systems. Structure of gels was characterized by SAXS providing insight of C-PC
interactions with BLG and starch after HP process which leads to the formation of solid
gels with larger mesh compared to two-component systems. This results in enhanced
mechanical properties, which were determined by amplitude and frequency sweep
measurements using a rheometer with applied plane/plane geometry. Therefore, adding
starch, even at small concentration, significantly improves gel visual appearance and
mechanical properties. Our study reveals that preservation through HP treatment is more
effective than high temperature treatment, as visually observed through the sustained color
integrity of C-PC blue dye.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia",
title = "Combined hydrogels of starch and β-lactoglobulin as matrices for the preservation of C-phycocyanin",
pages = "150-150",
url = "https://hdl.handle.net/21.15107/rcub_cer_6669"
}

Jovanović, Z., Annighöfer, B., Dudzinski, D., Veličković, L., Gligorijević, N., Nikolić, M., Brûlet, A., Assifaoui, A., Combet, S.,& Minić, S.. (2023). Combined hydrogels of starch and β-lactoglobulin as matrices for the preservation of C-phycocyanin. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
Serbian Biochemical Society., 150-150.
https://hdl.handle.net/21.15107/rcub_cer_6669

Jovanović Z, Annighöfer B, Dudzinski D, Veličković L, Gligorijević N, Nikolić M, Brûlet A, Assifaoui A, Combet S, Minić S. Combined hydrogels of starch and β-lactoglobulin as matrices for the preservation of C-phycocyanin. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia. 2023;:150-150.
https://hdl.handle.net/21.15107/rcub_cer_6669 .

Jovanović, Zorana, Annighöfer, Burkhard, Dudzinski, Daniel, Veličković, Luka, Gligorijević, Nikola, Nikolić, Milan, Brûlet, Annie, Assifaoui, Ali, Combet, Sophie, Minić, Simeon, "Combined hydrogels of starch and β-lactoglobulin as matrices for the preservation of C-phycocyanin" in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia (2023):150-150,
https://hdl.handle.net/21.15107/rcub_cer_6669 .

TY  - CONF
AU  - Veličković, Luka
AU  - Sibinčić, Nikolina
AU  - Stojadinović, Marija
AU  - Gligorijević, Nikola
AU  - Nikolić, Milan
AU  - Srdić, Tatjana
AU  - Minić, Simeon
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6671
AB  - This study investigates the impact of Porphyra sp. extracts on HT29 cell line growth and
viability at reduced serum conditions. The concentration-dependent effects of
phycobiliproteins (PBPs) on cell proliferation were examined over various time intervals.
Lower concentrations of PBPs (20 μg/mL) demonstrated an increase in HT29 cell viability
after 48 hours and 5 days of cultivation at reduced serum concentration (final serum
concentration was in the range from 5 to 8%). This suggests a potential positive influence
on cell proliferation, likely due to their antioxidant properties. Conversely, higher
concentrations of PBPs exhibited inhibitory effects on cell growth, possibly due to
cytotoxicity at elevated levels. Remarkably, when HT29 cells were cultured solely in algal
extract without fetal calf serum (FCS), complete growth inhibition was observed after 72
hours. This finding underscores the insufficient nutrient and growth factor provision of
PBPs alone for sustaining cell viability. Morphological differences observed in cells
cultured with 70 μg/mL of PBPs indicated potential alterations in cellular morphology.
Notably, 70 μg/mL of PBPs in RPMI medium with 5% FCS displayed growth inhibition
compared to the control (5% FCS). Furthermore, we assessed HT29 cell adaptability to
changes in FCS concentration and PBP supplementation. Cells incubated under varying
FCS and PBP conditions were subcultured into RPMI medium with lower FCS
concentration and PBPs from Porphyra. The viability of cells following subculturing
indicated sustained adaptability to reduced FCS levels. Overall, this study provides
valuable insights into the concentration-dependent effects of PBPs from Porphyra extracts
on HT29 cell growth and viability. The findings underscore the potential benefits of PBPs
at lower concentrations for cell proliferation at reduced serum conditions and reveal the
adaptability of HT29 cells to changing culture conditions.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
T1  - Exploring if Porphyra sp. extract functions as serum substitute in HT29 cell culture
SP  - 82
EP  - 82
UR  - https://hdl.handle.net/21.15107/rcub_cer_6671
ER  - 

@conference{
author = "Veličković, Luka and Sibinčić, Nikolina and Stojadinović, Marija and Gligorijević, Nikola and Nikolić, Milan and Srdić, Tatjana and Minić, Simeon",
year = "2023",
abstract = "This study investigates the impact of Porphyra sp. extracts on HT29 cell line growth and
viability at reduced serum conditions. The concentration-dependent effects of
phycobiliproteins (PBPs) on cell proliferation were examined over various time intervals.
Lower concentrations of PBPs (20 μg/mL) demonstrated an increase in HT29 cell viability
after 48 hours and 5 days of cultivation at reduced serum concentration (final serum
concentration was in the range from 5 to 8%). This suggests a potential positive influence
on cell proliferation, likely due to their antioxidant properties. Conversely, higher
concentrations of PBPs exhibited inhibitory effects on cell growth, possibly due to
cytotoxicity at elevated levels. Remarkably, when HT29 cells were cultured solely in algal
extract without fetal calf serum (FCS), complete growth inhibition was observed after 72
hours. This finding underscores the insufficient nutrient and growth factor provision of
PBPs alone for sustaining cell viability. Morphological differences observed in cells
cultured with 70 μg/mL of PBPs indicated potential alterations in cellular morphology.
Notably, 70 μg/mL of PBPs in RPMI medium with 5% FCS displayed growth inhibition
compared to the control (5% FCS). Furthermore, we assessed HT29 cell adaptability to
changes in FCS concentration and PBP supplementation. Cells incubated under varying
FCS and PBP conditions were subcultured into RPMI medium with lower FCS
concentration and PBPs from Porphyra. The viability of cells following subculturing
indicated sustained adaptability to reduced FCS levels. Overall, this study provides
valuable insights into the concentration-dependent effects of PBPs from Porphyra extracts
on HT29 cell growth and viability. The findings underscore the potential benefits of PBPs
at lower concentrations for cell proliferation at reduced serum conditions and reveal the
adaptability of HT29 cells to changing culture conditions.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia",
title = "Exploring if Porphyra sp. extract functions as serum substitute in HT29 cell culture",
pages = "82-82",
url = "https://hdl.handle.net/21.15107/rcub_cer_6671"
}

Veličković, L., Sibinčić, N., Stojadinović, M., Gligorijević, N., Nikolić, M., Srdić, T.,& Minić, S.. (2023). Exploring if Porphyra sp. extract functions as serum substitute in HT29 cell culture. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
Serbian Biochemical Society., 82-82.
https://hdl.handle.net/21.15107/rcub_cer_6671

Veličković L, Sibinčić N, Stojadinović M, Gligorijević N, Nikolić M, Srdić T, Minić S. Exploring if Porphyra sp. extract functions as serum substitute in HT29 cell culture. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia. 2023;:82-82.
https://hdl.handle.net/21.15107/rcub_cer_6671 .

Veličković, Luka, Sibinčić, Nikolina, Stojadinović, Marija, Gligorijević, Nikola, Nikolić, Milan, Srdić, Tatjana, Minić, Simeon, "Exploring if Porphyra sp. extract functions as serum substitute in HT29 cell culture" in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia (2023):82-82,
https://hdl.handle.net/21.15107/rcub_cer_6671 .

TY  - CONF
AU  - Radomirović, Mirjana
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Nikolić, Milan
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković Veličković, Tanja
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6945
AB  - Phycocyanobilin (PCB) is an open-chain tetrapyrrole chromophore of phycocyanin (PC), chromoprotein derived from the cyanobacterium Arthrospira platensis. Our group has previously demonstrated the potential of PCB to covalently modify free cysteine residue of proteins using food protein β-lactoglobulin as a model protein. Relying on the proven ability of PCB to be attached to sulfhydryl groups of proteins, we propose a new method for covalent attachment of PCB to potentially any protein. We used Traut’s reagent (TR, 2-iminothiolane) to introduce free sulfhydryl groups in the model protein, bovine serum albumin (BSA), by modifying its lysine residues. All tested molar ratios of TR per mole of protein successfully modified BSA. A higher degree of modification by TR induced more profound alterations of BSA structure, as evidenced by near-UV and far-UV circular dichroism spectroscopy. At the same time, minor changes in BSA oligomerization and aggregation profile occurred with increasing TR molar ratio. PCB was covalently attached to introduced sulfhydryl groups at pH 9 at 20–fold molar ratio of PCB per mole of protein. An increase in the molar ratio of TR per mole of BSA leads to amplification of fluorescent signal of PCB-modified BSA, most significantly observed starting from 50-fold and higher TR ratios. Using BSA as a model protein, a 50-fold molar excess of TR seems to be the optimal choice for balancing a satisfactory signal amplification level and the negative effect on protein structure. BSA covalently modified with PCB has higher antioxidative activity than free BSA. The proposed method thus serves as a proof of concept for labeling virtually any protein with PCB as means of either functionalization through covalent attachment of bioactive PCB or obtaining fluorescent probes for application in fluorescence-based techniques.
PB  - Wiley
PB  - Federation of European Biochemical Societies
C3  - The Biochemistry Global Summit, 9th-14th July, 2022. In: FEBS Open Bio
T1  - Covalent modification of bovine serum albumin with phycocyanobilin using Traut's reagent
VL  - 12
IS  - Suppl. 1
SP  - 302
EP  - 303
UR  - https://hdl.handle.net/21.15107/rcub_cer_6945
ER  - 

@conference{
author = "Radomirović, Mirjana and Gligorijević, Nikola and Minić, Simeon and Nikolić, Milan and Stanić-Vučinić, Dragana and Ćirković Veličković, Tanja",
year = "2022",
abstract = "Phycocyanobilin (PCB) is an open-chain tetrapyrrole chromophore of phycocyanin (PC), chromoprotein derived from the cyanobacterium Arthrospira platensis. Our group has previously demonstrated the potential of PCB to covalently modify free cysteine residue of proteins using food protein β-lactoglobulin as a model protein. Relying on the proven ability of PCB to be attached to sulfhydryl groups of proteins, we propose a new method for covalent attachment of PCB to potentially any protein. We used Traut’s reagent (TR, 2-iminothiolane) to introduce free sulfhydryl groups in the model protein, bovine serum albumin (BSA), by modifying its lysine residues. All tested molar ratios of TR per mole of protein successfully modified BSA. A higher degree of modification by TR induced more profound alterations of BSA structure, as evidenced by near-UV and far-UV circular dichroism spectroscopy. At the same time, minor changes in BSA oligomerization and aggregation profile occurred with increasing TR molar ratio. PCB was covalently attached to introduced sulfhydryl groups at pH 9 at 20–fold molar ratio of PCB per mole of protein. An increase in the molar ratio of TR per mole of BSA leads to amplification of fluorescent signal of PCB-modified BSA, most significantly observed starting from 50-fold and higher TR ratios. Using BSA as a model protein, a 50-fold molar excess of TR seems to be the optimal choice for balancing a satisfactory signal amplification level and the negative effect on protein structure. BSA covalently modified with PCB has higher antioxidative activity than free BSA. The proposed method thus serves as a proof of concept for labeling virtually any protein with PCB as means of either functionalization through covalent attachment of bioactive PCB or obtaining fluorescent probes for application in fluorescence-based techniques.",
publisher = "Wiley, Federation of European Biochemical Societies",
journal = "The Biochemistry Global Summit, 9th-14th July, 2022. In: FEBS Open Bio",
title = "Covalent modification of bovine serum albumin with phycocyanobilin using Traut's reagent",
volume = "12",
number = "Suppl. 1",
pages = "302-303",
url = "https://hdl.handle.net/21.15107/rcub_cer_6945"
}

Radomirović, M., Gligorijević, N., Minić, S., Nikolić, M., Stanić-Vučinić, D.,& Ćirković Veličković, T.. (2022). Covalent modification of bovine serum albumin with phycocyanobilin using Traut's reagent. in The Biochemistry Global Summit, 9th-14th July, 2022. In: FEBS Open Bio
Wiley., 12(Suppl. 1), 302-303.
https://hdl.handle.net/21.15107/rcub_cer_6945

Radomirović M, Gligorijević N, Minić S, Nikolić M, Stanić-Vučinić D, Ćirković Veličković T. Covalent modification of bovine serum albumin with phycocyanobilin using Traut's reagent. in The Biochemistry Global Summit, 9th-14th July, 2022. In: FEBS Open Bio. 2022;12(Suppl. 1):302-303.
https://hdl.handle.net/21.15107/rcub_cer_6945 .

Radomirović, Mirjana, Gligorijević, Nikola, Minić, Simeon, Nikolić, Milan, Stanić-Vučinić, Dragana, Ćirković Veličković, Tanja, "Covalent modification of bovine serum albumin with phycocyanobilin using Traut's reagent" in The Biochemistry Global Summit, 9th-14th July, 2022. In: FEBS Open Bio, 12, no. Suppl. 1 (2022):302-303,
https://hdl.handle.net/21.15107/rcub_cer_6945 .

TY  - CHAP
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6486
AB  - Bilirubin is a tetrapyrrole, yellow pigment, and it is a degradation product
created in heme metabolism. This molecule is predominantly present in
its unconjugated form in circulation, and it is mainly bound to human
serum albumin. The presence of small amounts of free, unconjugated
bilirubin enables its interactions with other circulation components. In
conditions like Gilbert syndrome or diabetes, the concentration of
unconjugated bilirubin increases in the blood, making other interacting
partners from circulation more important for its metabolism. In the liver,
bilirubin is converted to conjugated form, which is then excreted from
the organism. While the significant increase of bilirubin is toxic, research
suggests that small increases may be beneficial since bilirubin has
antioxidative and anticancer potential. In this chapter, interactions of
bilirubin with several proteins will be described together with the effects
of these interactions on the protein’s structure and function.
PB  - New York: Nova Science Publishers, Inc.
T2  - Advances in Biology
T1  - Bilirubin Interactions with Different Proteins and Implications of These Interactions
VL  - 1
SP  - 85
EP  - 122
UR  - https://hdl.handle.net/21.15107/rcub_cer_6486
ER  - 

@inbook{
author = "Gligorijević, Nikola and Minić, Simeon",
year = "2022",
abstract = "Bilirubin is a tetrapyrrole, yellow pigment, and it is a degradation product
created in heme metabolism. This molecule is predominantly present in
its unconjugated form in circulation, and it is mainly bound to human
serum albumin. The presence of small amounts of free, unconjugated
bilirubin enables its interactions with other circulation components. In
conditions like Gilbert syndrome or diabetes, the concentration of
unconjugated bilirubin increases in the blood, making other interacting
partners from circulation more important for its metabolism. In the liver,
bilirubin is converted to conjugated form, which is then excreted from
the organism. While the significant increase of bilirubin is toxic, research
suggests that small increases may be beneficial since bilirubin has
antioxidative and anticancer potential. In this chapter, interactions of
bilirubin with several proteins will be described together with the effects
of these interactions on the protein’s structure and function.",
publisher = "New York: Nova Science Publishers, Inc.",
journal = "Advances in Biology",
booktitle = "Bilirubin Interactions with Different Proteins and Implications of These Interactions",
volume = "1",
pages = "85-122",
url = "https://hdl.handle.net/21.15107/rcub_cer_6486"
}

Gligorijević, N.,& Minić, S.. (2022). Bilirubin Interactions with Different Proteins and Implications of These Interactions. in Advances in Biology
New York: Nova Science Publishers, Inc.., 1, 85-122.
https://hdl.handle.net/21.15107/rcub_cer_6486

Gligorijević N, Minić S. Bilirubin Interactions with Different Proteins and Implications of These Interactions. in Advances in Biology. 2022;1:85-122.
https://hdl.handle.net/21.15107/rcub_cer_6486 .

Gligorijević, Nikola, Minić, Simeon, "Bilirubin Interactions with Different Proteins and Implications of These Interactions" in Advances in Biology, 1 (2022):85-122,
https://hdl.handle.net/21.15107/rcub_cer_6486 .

TY  - CONF
AU  - Nedić, Olgica
AU  - Gligorijević, Nikola
AU  - Penezić, Ana
AU  - Minić, Simeon
AU  - Radomirović, Mirjana
AU  - Nikolić, Milan
AU  - Ćirković Veličković, Tanja
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6728
AB  - Our research work was focused on interactions between resveratrol (R) and tibnnogen (I), (dihydro)alpha-lipoic acid (ALA) and fibrinogen or albumin, and phycocyanobilin (PCB) and catalase. Resveratrol is found in grapes and berries, leafy greens are a source of ALA and alga Spirulina is a source of PCB. L-P interactions were investigated by following-up structural changes of proteins and/or ligands using spectrometric methods (spectrofluorimetry, CD, FTIR) and by examining the primary role of individual proteins upon ligand binding.
PB  - Belgrade : University of Belgrade - Faculty of Agriculture
C3  - Book of abstracts - 1st European Symposium on Phytochemicals in Medicine and Food (1EuSPMF), 7-9 September 2022, Belgrade, Serbia
T1  - Food antioxidants and their interaction with human proteins
SP  - 13
EP  - 13
UR  - https://hdl.handle.net/21.15107/rcub_cer_6728
ER  - 

@conference{
author = "Nedić, Olgica and Gligorijević, Nikola and Penezić, Ana and Minić, Simeon and Radomirović, Mirjana and Nikolić, Milan and Ćirković Veličković, Tanja",
year = "2022",
abstract = "Our research work was focused on interactions between resveratrol (R) and tibnnogen (I), (dihydro)alpha-lipoic acid (ALA) and fibrinogen or albumin, and phycocyanobilin (PCB) and catalase. Resveratrol is found in grapes and berries, leafy greens are a source of ALA and alga Spirulina is a source of PCB. L-P interactions were investigated by following-up structural changes of proteins and/or ligands using spectrometric methods (spectrofluorimetry, CD, FTIR) and by examining the primary role of individual proteins upon ligand binding.",
publisher = "Belgrade : University of Belgrade - Faculty of Agriculture",
journal = "Book of abstracts - 1st European Symposium on Phytochemicals in Medicine and Food (1EuSPMF), 7-9 September 2022, Belgrade, Serbia",
title = "Food antioxidants and their interaction with human proteins",
pages = "13-13",
url = "https://hdl.handle.net/21.15107/rcub_cer_6728"
}

Nedić, O., Gligorijević, N., Penezić, A., Minić, S., Radomirović, M., Nikolić, M.,& Ćirković Veličković, T.. (2022). Food antioxidants and their interaction with human proteins. in Book of abstracts - 1st European Symposium on Phytochemicals in Medicine and Food (1EuSPMF), 7-9 September 2022, Belgrade, Serbia
Belgrade : University of Belgrade - Faculty of Agriculture., 13-13.
https://hdl.handle.net/21.15107/rcub_cer_6728

Nedić O, Gligorijević N, Penezić A, Minić S, Radomirović M, Nikolić M, Ćirković Veličković T. Food antioxidants and their interaction with human proteins. in Book of abstracts - 1st European Symposium on Phytochemicals in Medicine and Food (1EuSPMF), 7-9 September 2022, Belgrade, Serbia. 2022;:13-13.
https://hdl.handle.net/21.15107/rcub_cer_6728 .

Nedić, Olgica, Gligorijević, Nikola, Penezić, Ana, Minić, Simeon, Radomirović, Mirjana, Nikolić, Milan, Ćirković Veličković, Tanja, "Food antioxidants and their interaction with human proteins" in Book of abstracts - 1st European Symposium on Phytochemicals in Medicine and Food (1EuSPMF), 7-9 September 2022, Belgrade, Serbia (2022):13-13,
https://hdl.handle.net/21.15107/rcub_cer_6728 .

TY  - CONF
AU  - Vasović, Tamara
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Nikolić, Milan
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6821
AB  - Oxidative stress undoubtedly accompanies mental disorders, and
the pleiotropic effects of atypical antipsychotics, recommended
drugs in the treatment of psychosis, are not clarified at the
molecular level. Catalase is one of the key enzymes of the primary
antioxidant protection system. This work studied the binding
of second-generation antipsychotic drug Clozapine to
commercial bovine liver catalase. Using various spectroscopic
methods under simulated physiological conditions, we found
moderate binding affinity of clozapine for catalase (Ka ~ 2x105
M-1), the binding influenced the secondary and tertiary structure
of protein (according to UV-VIS and CD spectroscopy) and it
managed to slightly increase its thermal stability. In AAPH
induced oxidation experiments, we found that clozapine efficiently
protects catalase from free-radicals oxidation and preserves
its activity. Clozapine affects catalase activity in dose
dependant manner, having no significant effect at lower concentrations
but significantly inhibiting enzyme at saturating concentrations.
In conclusion, our results indicate that the effect of
direct binding of clozapine to catalase can be both beneficial and
harmful and that this effect is dose dependent.
PB  - Wiley
C3  - FEBS Open Bio
T1  - Antipsychotic clozapine binds catalase and preserves its activity in oxidative environment
VL  - 12
IS  - Supplement 1
SP  - 264
EP  - 264
DO  - 10.1002/2211-5463.13440
ER  - 

@conference{
author = "Vasović, Tamara and Gligorijević, Nikola and Minić, Simeon and Nikolić, Milan",
year = "2022",
abstract = "Oxidative stress undoubtedly accompanies mental disorders, and
the pleiotropic effects of atypical antipsychotics, recommended
drugs in the treatment of psychosis, are not clarified at the
molecular level. Catalase is one of the key enzymes of the primary
antioxidant protection system. This work studied the binding
of second-generation antipsychotic drug Clozapine to
commercial bovine liver catalase. Using various spectroscopic
methods under simulated physiological conditions, we found
moderate binding affinity of clozapine for catalase (Ka ~ 2x105
M-1), the binding influenced the secondary and tertiary structure
of protein (according to UV-VIS and CD spectroscopy) and it
managed to slightly increase its thermal stability. In AAPH
induced oxidation experiments, we found that clozapine efficiently
protects catalase from free-radicals oxidation and preserves
its activity. Clozapine affects catalase activity in dose
dependant manner, having no significant effect at lower concentrations
but significantly inhibiting enzyme at saturating concentrations.
In conclusion, our results indicate that the effect of
direct binding of clozapine to catalase can be both beneficial and
harmful and that this effect is dose dependent.",
publisher = "Wiley",
journal = "FEBS Open Bio",
title = "Antipsychotic clozapine binds catalase and preserves its activity in oxidative environment",
volume = "12",
number = "Supplement 1",
pages = "264-264",
doi = "10.1002/2211-5463.13440"
}

Vasović, T., Gligorijević, N., Minić, S.,& Nikolić, M.. (2022). Antipsychotic clozapine binds catalase and preserves its activity in oxidative environment. in FEBS Open Bio
Wiley., 12(Supplement 1), 264-264.
https://doi.org/10.1002/2211-5463.13440

Vasović T, Gligorijević N, Minić S, Nikolić M. Antipsychotic clozapine binds catalase and preserves its activity in oxidative environment. in FEBS Open Bio. 2022;12(Supplement 1):264-264.
doi:10.1002/2211-5463.13440 .

Vasović, Tamara, Gligorijević, Nikola, Minić, Simeon, Nikolić, Milan, "Antipsychotic clozapine binds catalase and preserves its activity in oxidative environment" in FEBS Open Bio, 12, no. Supplement 1 (2022):264-264,
https://doi.org/10.1002/2211-5463.13440 . .

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  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Radibratović, Milica
AU  - Papadimitriou, Vassiliki
AU  - Nedić, Olgica
AU  - Sotiroudis, Theodore G.
AU  - Nikolić, Milan
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4226
AB  - Phycocyanobilin is a dark blue linear tetrapyrrole chromophore covalently attached to protein subunits of phycobiliproteins present in the light-harvesting complexes of the cyanobacteria Arthrospira platensis (Spirulina “superfood”). It shows exceptional health-promoting properties and emerging use in various fields of bioscience and industry. This study aims to examine the mutual impact of phycocyanobilin interactions with catalase, a life-essential antioxidant enzyme. Fluorescence quenching experiments demonstrated moderate binding (Ka of 3.9 × 104 M−1 at 25 °C; n = 0.89) (static type), while van't Hoff plot points to an enthalpically driven ligand binding (ΔG = −28.2 kJ mol−1; ΔH = −41.9 kJ mol−1). No significant changes in protein secondary structures (α-helix content ~22%) and thermal protein stability in terms of enzyme tetramer subunits (Tm ~ 64 °C) were detected upon ligand binding. Alterations in the tertiary catalase structure were found without adverse effects on enzyme activity (~2 × 106 IU/mL). The docking study results indicated that the ligand most likely binds to amino acid residues (Asn141, Arg 362, Tyr369 and Asn384) near the cavity between the enzyme homotetramer subunits not related to the active site. Finally, complex formation protects the pigment from free-radical induced oxidation (bleaching), suggesting possible prolongation of its half-life and bioactivity in vivo if bound to catalase.
PB  - Elsevier
T2  - Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
T1  - Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity
VL  - 251
SP  - 119483
DO  - 10.1016/j.saa.2021.119483
ER  - 

@article{
author = "Gligorijević, Nikola and Minić, Simeon and Radibratović, Milica and Papadimitriou, Vassiliki and Nedić, Olgica and Sotiroudis, Theodore G. and Nikolić, Milan",
year = "2021",
abstract = "Phycocyanobilin is a dark blue linear tetrapyrrole chromophore covalently attached to protein subunits of phycobiliproteins present in the light-harvesting complexes of the cyanobacteria Arthrospira platensis (Spirulina “superfood”). It shows exceptional health-promoting properties and emerging use in various fields of bioscience and industry. This study aims to examine the mutual impact of phycocyanobilin interactions with catalase, a life-essential antioxidant enzyme. Fluorescence quenching experiments demonstrated moderate binding (Ka of 3.9 × 104 M−1 at 25 °C; n = 0.89) (static type), while van't Hoff plot points to an enthalpically driven ligand binding (ΔG = −28.2 kJ mol−1; ΔH = −41.9 kJ mol−1). No significant changes in protein secondary structures (α-helix content ~22%) and thermal protein stability in terms of enzyme tetramer subunits (Tm ~ 64 °C) were detected upon ligand binding. Alterations in the tertiary catalase structure were found without adverse effects on enzyme activity (~2 × 106 IU/mL). The docking study results indicated that the ligand most likely binds to amino acid residues (Asn141, Arg 362, Tyr369 and Asn384) near the cavity between the enzyme homotetramer subunits not related to the active site. Finally, complex formation protects the pigment from free-radical induced oxidation (bleaching), suggesting possible prolongation of its half-life and bioactivity in vivo if bound to catalase.",
publisher = "Elsevier",
journal = "Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy",
title = "Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity",
volume = "251",
pages = "119483",
doi = "10.1016/j.saa.2021.119483"
}

Gligorijević, N., Minić, S., Radibratović, M., Papadimitriou, V., Nedić, O., Sotiroudis, T. G.,& Nikolić, M.. (2021). Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity. in Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
Elsevier., 251, 119483.
https://doi.org/10.1016/j.saa.2021.119483

Gligorijević N, Minić S, Radibratović M, Papadimitriou V, Nedić O, Sotiroudis TG, Nikolić M. Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity. in Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy. 2021;251:119483.
doi:10.1016/j.saa.2021.119483 .

Gligorijević, Nikola, Minić, Simeon, Radibratović, Milica, Papadimitriou, Vassiliki, Nedić, Olgica, Sotiroudis, Theodore G., Nikolić, Milan, "Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity" in Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy, 251 (2021):119483,
https://doi.org/10.1016/j.saa.2021.119483 . .

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Šukalović, Vladimir
AU  - Minić, Simeon
AU  - Miljuš, Goran
AU  - Nedić, Olgica
AU  - Penezić, Ana
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4763
AB  - The binding of a popular food supplement and well-known antioxidant, dihydro-alpha-lipoic acid (DHLA) to human serum albumin (HSA) was characterised. The binding was monitored by several spectroscopic methods together with the molecular docking approach. HSA was able to bind DHLA with moderate affinity, 1.00±0.05×104 M-1. Spectroscopic data demonstrated that the preferential binding site for DHLA on HSA is IIA (Sudlow I). Both experimental and molecular docking analysis identified electrostatic (salt bridges) and hydrogen bonds as the key interactions involved in DHLA binding to HSA. Molecular docking confirmed that the Sudlow I site could accommodate DHLA and that the ligand is bound to the protein in a specific conformation. The molecular dynamic simulation showed that the formed complex is stable. Binding of DHLA does not affect the structure of the protein, but it thermally stabilises HSA. Bound DHLA had no effect on the susceptibility of HSA to trypsin digestion. Since DHLA is a commonly used food supplement, knowledge of its pharmacokinetics and pharmacodynamic properties in an organism is very important. This study further expands it by providing a detailed analysis of its interaction with HSA, the primary drug transporter in the circulation.
AB  - У раду су описане карктеристике везивања дихидро-липоинске киселине (DHLA), познатог суплемента у исхрани и антиоксиданса, за албумин из серума људи (HSA). Процес везивања је праћен применом већег броја спектроскопских метода и молекул-
ским моделовањем. HSA везује DHLA умереним афинитетом, 1,00±0,05×104 M-1. Спектроскопски резултати су показали да је везујуће место IIA (Sudlow I) главно место везивања DHLA за HSA. Експериментални, као и резултати молекулског моделовања, су идентификовали електростатичке (сони мостови) и водоничне везе као главне типове
интеракција. Резултати молекулског моделовања су потврдили да и место Sudlow I може везати DHLA, која је у том случају у специфичној конформацији. Симулација молекулске динамике је показала да је формирани комплекс стабилан. Везивање DHLA не
утиче на структуру протеина, али повећава његову термалну стабилност. Везани DHLA не утиче на подложност HSA трипсинској дигестији. Како је DHLA уобичајен суплемент у исхрани, знање о његовим фармакоконетичким и фармакодинамичким особинама је веома важно. Ово испитивање допуњује досадашња знања детаљном анализом интеракције DHLA са HSA, примарним транспортним протеином лекова у циркулацији.
PB  - Belgrade : Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - Physicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approaches
T1  - Физичко-хемијска карактеризација интеракције дихидро-липоинске киселине и албумина из серума људи применом мулти-спектроскопских метода и молекулског моделовања
VL  - 86
IS  - 9
SP  - 795
EP  - 807
DO  - 10.2298/JSC210420041G
ER  - 

@article{
author = "Gligorijević, Nikola and Šukalović, Vladimir and Minić, Simeon and Miljuš, Goran and Nedić, Olgica and Penezić, Ana",
year = "2021",
abstract = "The binding of a popular food supplement and well-known antioxidant, dihydro-alpha-lipoic acid (DHLA) to human serum albumin (HSA) was characterised. The binding was monitored by several spectroscopic methods together with the molecular docking approach. HSA was able to bind DHLA with moderate affinity, 1.00±0.05×104 M-1. Spectroscopic data demonstrated that the preferential binding site for DHLA on HSA is IIA (Sudlow I). Both experimental and molecular docking analysis identified electrostatic (salt bridges) and hydrogen bonds as the key interactions involved in DHLA binding to HSA. Molecular docking confirmed that the Sudlow I site could accommodate DHLA and that the ligand is bound to the protein in a specific conformation. The molecular dynamic simulation showed that the formed complex is stable. Binding of DHLA does not affect the structure of the protein, but it thermally stabilises HSA. Bound DHLA had no effect on the susceptibility of HSA to trypsin digestion. Since DHLA is a commonly used food supplement, knowledge of its pharmacokinetics and pharmacodynamic properties in an organism is very important. This study further expands it by providing a detailed analysis of its interaction with HSA, the primary drug transporter in the circulation., У раду су описане карктеристике везивања дихидро-липоинске киселине (DHLA), познатог суплемента у исхрани и антиоксиданса, за албумин из серума људи (HSA). Процес везивања је праћен применом већег броја спектроскопских метода и молекул-
ским моделовањем. HSA везује DHLA умереним афинитетом, 1,00±0,05×104 M-1. Спектроскопски резултати су показали да је везујуће место IIA (Sudlow I) главно место везивања DHLA за HSA. Експериментални, као и резултати молекулског моделовања, су идентификовали електростатичке (сони мостови) и водоничне везе као главне типове
интеракција. Резултати молекулског моделовања су потврдили да и место Sudlow I може везати DHLA, која је у том случају у специфичној конформацији. Симулација молекулске динамике је показала да је формирани комплекс стабилан. Везивање DHLA не
утиче на структуру протеина, али повећава његову термалну стабилност. Везани DHLA не утиче на подложност HSA трипсинској дигестији. Како је DHLA уобичајен суплемент у исхрани, знање о његовим фармакоконетичким и фармакодинамичким особинама је веома важно. Ово испитивање допуњује досадашња знања детаљном анализом интеракције DHLA са HSA, примарним транспортним протеином лекова у циркулацији.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Physicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approaches, Физичко-хемијска карактеризација интеракције дихидро-липоинске киселине и албумина из серума људи применом мулти-спектроскопских метода и молекулског моделовања",
volume = "86",
number = "9",
pages = "795-807",
doi = "10.2298/JSC210420041G"
}

Gligorijević, N., Šukalović, V., Minić, S., Miljuš, G., Nedić, O.,& Penezić, A.. (2021). Physicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approaches. in Journal of the Serbian Chemical Society
Belgrade : Serbian Chemical Society., 86(9), 795-807.
https://doi.org/10.2298/JSC210420041G

Gligorijević N, Šukalović V, Minić S, Miljuš G, Nedić O, Penezić A. Physicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approaches. in Journal of the Serbian Chemical Society. 2021;86(9):795-807.
doi:10.2298/JSC210420041G .

Gligorijević, Nikola, Šukalović, Vladimir, Minić, Simeon, Miljuš, Goran, Nedić, Olgica, Penezić, Ana, "Physicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approaches" in Journal of the Serbian Chemical Society, 86, no. 9 (2021):795-807,
https://doi.org/10.2298/JSC210420041G . .

TY  - CONF
AU  - Radomirović, Mirjana
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Nikolić, Milan
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e5deeb546e&appId=PPGMS
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7282
AB  - Phycobiliproteins (PBP) have been employed in numerous fluorescence-based techniques owing
to highly fluorescent, covalently bound tetrapyrrole chromophores. So far, only entire PBPs have
been utilized as fluorescent probes. A new method for covalent attachment of phycocyanin’s
chromophore, phycocyanobilin (PCB), to potentially any protein, is proposed, relying on the
ability of PCB to be attached to sulfhydryl groups of proteins. Traut’s reagent (TR, 2-
iminothiolane) was exploited for introduction of sulfhydryl groups in the model protein, bovine
serum albumin (BSA), by modifying its primary amines. Introduced sulfhydryl groups were then
targeted for modification by PCB. All tested molar ratios of TR per mole of protein were
successful in modification of BSA. Near-UV and far-UV circular dichroism spectroscopy
revealed that a higher degree of modification by TR induces more profound alterations of BSA
structure, leading at the same time to minor changes in BSA oligomerization and aggregation
profile. PCB was covalently attached to introduced sulfhydryl groups at pH 9 at 20–fold ratio of
TR. An increase in the molar ratio of TR per mole of BSA leads to amplification of fluorescent
signal of PCB-modified BSA, most significantly observed starting from 50-fold and higher TR
ratios. Using BSA as a model protein, a 50-fold molar excess of TR seems to be the optimal ratio
for balancing between the effect on protein structure and the degree of labeling and thus
fluorescent signal obtained. The proposed method could be used for labeling of virtually any
protein, as means of either obtaining fluorescent probes for application in fluorescent techniques
or functionalization of, for example, food proteins through covalent attachment of bioactive
PCB.
PB  - University of Belgrade - Faculty of Chemistry
C3  - FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Book of Abstracts, 16th-18th June, 2021, Belgrade, Serbia
T1  - Traut’s reagent application in fluorescent labeling of bovine serum albumin with phycocyanobilin
SP  - 37
EP  - 37
UR  - https://hdl.handle.net/21.15107/rcub_cer_7282
ER  - 

@conference{
author = "Radomirović, Mirjana and Gligorijević, Nikola and Minić, Simeon and Nikolić, Milan and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Phycobiliproteins (PBP) have been employed in numerous fluorescence-based techniques owing
to highly fluorescent, covalently bound tetrapyrrole chromophores. So far, only entire PBPs have
been utilized as fluorescent probes. A new method for covalent attachment of phycocyanin’s
chromophore, phycocyanobilin (PCB), to potentially any protein, is proposed, relying on the
ability of PCB to be attached to sulfhydryl groups of proteins. Traut’s reagent (TR, 2-
iminothiolane) was exploited for introduction of sulfhydryl groups in the model protein, bovine
serum albumin (BSA), by modifying its primary amines. Introduced sulfhydryl groups were then
targeted for modification by PCB. All tested molar ratios of TR per mole of protein were
successful in modification of BSA. Near-UV and far-UV circular dichroism spectroscopy
revealed that a higher degree of modification by TR induces more profound alterations of BSA
structure, leading at the same time to minor changes in BSA oligomerization and aggregation
profile. PCB was covalently attached to introduced sulfhydryl groups at pH 9 at 20–fold ratio of
TR. An increase in the molar ratio of TR per mole of BSA leads to amplification of fluorescent
signal of PCB-modified BSA, most significantly observed starting from 50-fold and higher TR
ratios. Using BSA as a model protein, a 50-fold molar excess of TR seems to be the optimal ratio
for balancing between the effect on protein structure and the degree of labeling and thus
fluorescent signal obtained. The proposed method could be used for labeling of virtually any
protein, as means of either obtaining fluorescent probes for application in fluorescent techniques
or functionalization of, for example, food proteins through covalent attachment of bioactive
PCB.",
publisher = "University of Belgrade - Faculty of Chemistry",
journal = "FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Book of Abstracts, 16th-18th June, 2021, Belgrade, Serbia",
title = "Traut’s reagent application in fluorescent labeling of bovine serum albumin with phycocyanobilin",
pages = "37-37",
url = "https://hdl.handle.net/21.15107/rcub_cer_7282"
}

Radomirović, M., Gligorijević, N., Minić, S., Nikolić, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Traut’s reagent application in fluorescent labeling of bovine serum albumin with phycocyanobilin. in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Book of Abstracts, 16th-18th June, 2021, Belgrade, Serbia
University of Belgrade - Faculty of Chemistry., 37-37.
https://hdl.handle.net/21.15107/rcub_cer_7282

Radomirović M, Gligorijević N, Minić S, Nikolić M, Stanić-Vučinić D, Ćirković-Veličković T. Traut’s reagent application in fluorescent labeling of bovine serum albumin with phycocyanobilin. in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Book of Abstracts, 16th-18th June, 2021, Belgrade, Serbia. 2021;:37-37.
https://hdl.handle.net/21.15107/rcub_cer_7282 .

Radomirović, Mirjana, Gligorijević, Nikola, Minić, Simeon, Nikolić, Milan, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Traut’s reagent application in fluorescent labeling of bovine serum albumin with phycocyanobilin" in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Book of Abstracts, 16th-18th June, 2021, Belgrade, Serbia (2021):37-37,
https://hdl.handle.net/21.15107/rcub_cer_7282 .

TY  - CONF
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Radomirović, Mirjana
AU  - Lević, Steva
AU  - Ćirković Veličković, Tanja
AU  - Nikolić, Milan
AU  - Nedić, Olgica
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7287
AB  - Fibrinogen is a plasma protein most susceptible to oxidation. Through this chemical
modification, fibrinogen acquires thrombogenic characteristics in different
pathophysiological conditions. Increased carbonyl content and reduced porosity impair the
degradation of formed fibrin mediated by plasmin. Fibrinogen is capable of interacting
with many proteins, ions, and small molecules. These interactions can modify the
functions of this protein. The discovery of new binding partners that may protect
fibrinogen from harmful oxidation and, thus, preserve its normal function is essential.
Some of the newly detected interactions between fibrinogen and small, natural bioactive
molecules, together with the influence of these interactions on the structure and function of
fibrinogen, will be presented in this text.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Tenth Conference with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia
T1  - Ligand binding to fibrinogen influences its structure and function
SP  - 31
EP  - 31
UR  - https://hdl.handle.net/21.15107/rcub_cer_7287
ER  - 

@conference{
author = "Gligorijević, Nikola and Minić, Simeon and Radomirović, Mirjana and Lević, Steva and Ćirković Veličković, Tanja and Nikolić, Milan and Nedić, Olgica",
year = "2021",
abstract = "Fibrinogen is a plasma protein most susceptible to oxidation. Through this chemical
modification, fibrinogen acquires thrombogenic characteristics in different
pathophysiological conditions. Increased carbonyl content and reduced porosity impair the
degradation of formed fibrin mediated by plasmin. Fibrinogen is capable of interacting
with many proteins, ions, and small molecules. These interactions can modify the
functions of this protein. The discovery of new binding partners that may protect
fibrinogen from harmful oxidation and, thus, preserve its normal function is essential.
Some of the newly detected interactions between fibrinogen and small, natural bioactive
molecules, together with the influence of these interactions on the structure and function of
fibrinogen, will be presented in this text.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Tenth Conference with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia",
title = "Ligand binding to fibrinogen influences its structure and function",
pages = "31-31",
url = "https://hdl.handle.net/21.15107/rcub_cer_7287"
}

Gligorijević, N., Minić, S., Radomirović, M., Lević, S., Ćirković Veličković, T., Nikolić, M.,& Nedić, O.. (2021). Ligand binding to fibrinogen influences its structure and function. in Serbian Biochemical Society Tenth Conference with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia
Serbian Biochemical Society., 31-31.
https://hdl.handle.net/21.15107/rcub_cer_7287

Gligorijević N, Minić S, Radomirović M, Lević S, Ćirković Veličković T, Nikolić M, Nedić O. Ligand binding to fibrinogen influences its structure and function. in Serbian Biochemical Society Tenth Conference with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia. 2021;:31-31.
https://hdl.handle.net/21.15107/rcub_cer_7287 .

Gligorijević, Nikola, Minić, Simeon, Radomirović, Mirjana, Lević, Steva, Ćirković Veličković, Tanja, Nikolić, Milan, Nedić, Olgica, "Ligand binding to fibrinogen influences its structure and function" in Serbian Biochemical Society Tenth Conference with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia (2021):31-31,
https://hdl.handle.net/21.15107/rcub_cer_7287 .

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  - Radomirović, Mirjana
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Nikolić, Milan
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković Veličković, Tanja
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7290
AB  - Phycobiliproteins (PBP) are extensively used as fluorescent probes due to highly fluorescent,
covalently bound, tetrapyrrole chromophores. A new method for covalent attachment of
phycocyanin’s chromophore, phycocyanobilin (PCB), is proposed. We exploited Traut’s reagent
(TR) to introduce sulfhydryl groups in the bovine serum albumin (BSA), by modifying its lysine
residues. TR successfully modified BSA under all tested molar ratios of reagent per mole of BSA.
The higher degree of modification by TR induces more profound alterations of BSA structure. PCB
was covalently attached to introduced sulfhydryl groups at pH 9 at 20–fold ratio. An increase in the
molar ratio of TR per mole of BSA leads to amplification of fluorescent signal of PCB-modified
BSA. Using BSA as a model protein, a 50-fold molar excess of TR seems to be the optimal choice
for balancing between a satisfactory level of signal amplification and the adverse effect on protein
structure. The method could be used for labeling virtually any protein.
PB  - Belgrade : Serbian Chemical Society
C3  - Kratki izvodi radova, Knjiga radova 57. Savetovanje Srpskog hemijskog društva, 18. i 19. juni 2021, Kragujevac / Book of abstracts, Proceedings - 57th Meeting of the Serbian Chemical Society, June 18-19, 2021, Kragujevac, Serbia
T1  - Fluorescent labeling of bovine serum albumin with phycocyanobilin using Traut’s reagent
SP  - 71
EP  - 71
UR  - https://hdl.handle.net/21.15107/rcub_cer_7290
ER  - 

@conference{
author = "Radomirović, Mirjana and Gligorijević, Nikola and Minić, Simeon and Nikolić, Milan and Stanić-Vučinić, Dragana and Ćirković Veličković, Tanja",
year = "2021",
abstract = "Phycobiliproteins (PBP) are extensively used as fluorescent probes due to highly fluorescent,
covalently bound, tetrapyrrole chromophores. A new method for covalent attachment of
phycocyanin’s chromophore, phycocyanobilin (PCB), is proposed. We exploited Traut’s reagent
(TR) to introduce sulfhydryl groups in the bovine serum albumin (BSA), by modifying its lysine
residues. TR successfully modified BSA under all tested molar ratios of reagent per mole of BSA.
The higher degree of modification by TR induces more profound alterations of BSA structure. PCB
was covalently attached to introduced sulfhydryl groups at pH 9 at 20–fold ratio. An increase in the
molar ratio of TR per mole of BSA leads to amplification of fluorescent signal of PCB-modified
BSA. Using BSA as a model protein, a 50-fold molar excess of TR seems to be the optimal choice
for balancing between a satisfactory level of signal amplification and the adverse effect on protein
structure. The method could be used for labeling virtually any protein.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Kratki izvodi radova, Knjiga radova 57. Savetovanje Srpskog hemijskog društva, 18. i 19. juni 2021, Kragujevac / Book of abstracts, Proceedings - 57th Meeting of the Serbian Chemical Society, June 18-19, 2021, Kragujevac, Serbia",
title = "Fluorescent labeling of bovine serum albumin with phycocyanobilin using Traut’s reagent",
pages = "71-71",
url = "https://hdl.handle.net/21.15107/rcub_cer_7290"
}

Radomirović, M., Gligorijević, N., Minić, S., Nikolić, M., Stanić-Vučinić, D.,& Ćirković Veličković, T.. (2021). Fluorescent labeling of bovine serum albumin with phycocyanobilin using Traut’s reagent. in Kratki izvodi radova, Knjiga radova 57. Savetovanje Srpskog hemijskog društva, 18. i 19. juni 2021, Kragujevac / Book of abstracts, Proceedings - 57th Meeting of the Serbian Chemical Society, June 18-19, 2021, Kragujevac, Serbia
Belgrade : Serbian Chemical Society., 71-71.
https://hdl.handle.net/21.15107/rcub_cer_7290

Radomirović M, Gligorijević N, Minić S, Nikolić M, Stanić-Vučinić D, Ćirković Veličković T. Fluorescent labeling of bovine serum albumin with phycocyanobilin using Traut’s reagent. in Kratki izvodi radova, Knjiga radova 57. Savetovanje Srpskog hemijskog društva, 18. i 19. juni 2021, Kragujevac / Book of abstracts, Proceedings - 57th Meeting of the Serbian Chemical Society, June 18-19, 2021, Kragujevac, Serbia. 2021;:71-71.
https://hdl.handle.net/21.15107/rcub_cer_7290 .

Radomirović, Mirjana, Gligorijević, Nikola, Minić, Simeon, Nikolić, Milan, Stanić-Vučinić, Dragana, Ćirković Veličković, Tanja, "Fluorescent labeling of bovine serum albumin with phycocyanobilin using Traut’s reagent" in Kratki izvodi radova, Knjiga radova 57. Savetovanje Srpskog hemijskog društva, 18. i 19. juni 2021, Kragujevac / Book of abstracts, Proceedings - 57th Meeting of the Serbian Chemical Society, June 18-19, 2021, Kragujevac, Serbia (2021):71-71,
https://hdl.handle.net/21.15107/rcub_cer_7290 .