TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Radibratović, Milica
AU  - Papadimitriou, Vassiliki
AU  - Nedić, Olgica
AU  - Sotiroudis, Theodore G.
AU  - Nikolić, Milan
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S1386142521000597
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4486
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
T2  - Spectrochimica Acta Part A: Molecular and Biomolecular SpectroscopySpectrochimica 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 L. 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, Spectrochimica Acta Part A: Molecular and Biomolecular SpectroscopySpectrochimica 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. L., 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 SL, 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 L., 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  - DATA
AU  - Minić, Simeon L.
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Radibratović, Milica
AU  - Sotiroudis, Theodore G.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3403
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Supplementary data for article: Minic, S. L.; Milcic, M.; Stanic-Vucinic, D.; Radibratovic, M.; Sotiroudis, T. G.; Nikolic, M. R.; Velickovic, T. C. Phycocyanobilin, a Bioactive Tetrapyrrolic Compound of Blue-Green Alga Spirulina, Binds with High Affinity and Competes with Bilirubin for Binding on Human Serum Albumin. RSC Advances 2015, 5 (76), 61787–61798. https://doi.org/10.1039/c5ra05534b
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3403
ER  - 

@misc{
author = "Minić, Simeon L. and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Radibratović, Milica and Sotiroudis, Theodore G. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2015",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Supplementary data for article: Minic, S. L.; Milcic, M.; Stanic-Vucinic, D.; Radibratovic, M.; Sotiroudis, T. G.; Nikolic, M. R.; Velickovic, T. C. Phycocyanobilin, a Bioactive Tetrapyrrolic Compound of Blue-Green Alga Spirulina, Binds with High Affinity and Competes with Bilirubin for Binding on Human Serum Albumin. RSC Advances 2015, 5 (76), 61787–61798. https://doi.org/10.1039/c5ra05534b",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3403"
}

Minić, S. L., Milčić, M. K., Stanić-Vučinić, D., Radibratović, M., Sotiroudis, T. G., Nikolić, M.,& Ćirković-Veličković, T.. (2015). Supplementary data for article: Minic, S. L.; Milcic, M.; Stanic-Vucinic, D.; Radibratovic, M.; Sotiroudis, T. G.; Nikolic, M. R.; Velickovic, T. C. Phycocyanobilin, a Bioactive Tetrapyrrolic Compound of Blue-Green Alga Spirulina, Binds with High Affinity and Competes with Bilirubin for Binding on Human Serum Albumin. RSC Advances 2015, 5 (76), 61787–61798. https://doi.org/10.1039/c5ra05534b. in RSC Advances
Royal Soc Chemistry, Cambridge..
https://hdl.handle.net/21.15107/rcub_cherry_3403

Minić SL, Milčić MK, Stanić-Vučinić D, Radibratović M, Sotiroudis TG, Nikolić M, Ćirković-Veličković T. Supplementary data for article: Minic, S. L.; Milcic, M.; Stanic-Vucinic, D.; Radibratovic, M.; Sotiroudis, T. G.; Nikolic, M. R.; Velickovic, T. C. Phycocyanobilin, a Bioactive Tetrapyrrolic Compound of Blue-Green Alga Spirulina, Binds with High Affinity and Competes with Bilirubin for Binding on Human Serum Albumin. RSC Advances 2015, 5 (76), 61787–61798. https://doi.org/10.1039/c5ra05534b. in RSC Advances. 2015;.
https://hdl.handle.net/21.15107/rcub_cherry_3403 .

Minić, Simeon L., Milčić, Miloš K., Stanić-Vučinić, Dragana, Radibratović, Milica, Sotiroudis, Theodore G., Nikolić, Milan, Ćirković-Veličković, Tanja, "Supplementary data for article: Minic, S. L.; Milcic, M.; Stanic-Vucinic, D.; Radibratovic, M.; Sotiroudis, T. G.; Nikolic, M. R.; Velickovic, T. C. Phycocyanobilin, a Bioactive Tetrapyrrolic Compound of Blue-Green Alga Spirulina, Binds with High Affinity and Competes with Bilirubin for Binding on Human Serum Albumin. RSC Advances 2015, 5 (76), 61787–61798. https://doi.org/10.1039/c5ra05534b" in RSC Advances (2015),
https://hdl.handle.net/21.15107/rcub_cherry_3403 .

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Radibratović, Milica
AU  - Sotiroudis, Theodore G.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1741
AB  - Human serum albumin (HSA) is an important regulator of the pharmacokinetic properties of bioactive compounds. Phycocyanobilin is a blue tetrapyrrole chromophore of C-phycocyanin with proven health-promoting activities. Despite its structural similarity to bilirubin, the conformation it adopts in aqueous solution is different and the pigment is more soluble than bilirubin. The aim of our study was to examine binding of phycocyanobilin for HSA and to investigate its competition with bilirubin. Based on a computational approach, we demonstrated two putative high-affinity binding pockets on HSA of virtually identical energies for the neutral and anion forms of bilirubin, but with slightly favorable predictions for anion forms of phycocyanobilin. Computational prediction of phycocyanobilin pK(a) values suggested a monoanion form to be the most stable form at physiological conditions. The computationally predicted binding sites for phycocyanobilin were identical to the two previously identified binding sites for bilirubin (subdomains IB and IIA). Results obtained by protein and pigment fluorescence measurements, circular dichroism, and competition experiments confirmed high affinity (binding constant of 2.2 x 10(6) M-1 at 25 degrees C), stereo-selective binding of phycocyanobilin M-conformer to HSA and its competition with bilirubin, warfarin and hemin. Our experimental data confirm that phycocyanobilin binds to IB and IIA binding site of HSA with an affinity similar to bilirubin. In conditions characterized by an increased bilirubin plasma concentration, or intake of drugs binding to IB or IIA binding site, pharmacokinetics of phycocyanobilin may also be changed.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin
VL  - 5
IS  - 76
SP  - 61787
EP  - 61798
DO  - 10.1039/c5ra05534b
ER  - 

@article{
author = "Minić, Simeon L. and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Radibratović, Milica and Sotiroudis, Theodore G. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2015",
abstract = "Human serum albumin (HSA) is an important regulator of the pharmacokinetic properties of bioactive compounds. Phycocyanobilin is a blue tetrapyrrole chromophore of C-phycocyanin with proven health-promoting activities. Despite its structural similarity to bilirubin, the conformation it adopts in aqueous solution is different and the pigment is more soluble than bilirubin. The aim of our study was to examine binding of phycocyanobilin for HSA and to investigate its competition with bilirubin. Based on a computational approach, we demonstrated two putative high-affinity binding pockets on HSA of virtually identical energies for the neutral and anion forms of bilirubin, but with slightly favorable predictions for anion forms of phycocyanobilin. Computational prediction of phycocyanobilin pK(a) values suggested a monoanion form to be the most stable form at physiological conditions. The computationally predicted binding sites for phycocyanobilin were identical to the two previously identified binding sites for bilirubin (subdomains IB and IIA). Results obtained by protein and pigment fluorescence measurements, circular dichroism, and competition experiments confirmed high affinity (binding constant of 2.2 x 10(6) M-1 at 25 degrees C), stereo-selective binding of phycocyanobilin M-conformer to HSA and its competition with bilirubin, warfarin and hemin. Our experimental data confirm that phycocyanobilin binds to IB and IIA binding site of HSA with an affinity similar to bilirubin. In conditions characterized by an increased bilirubin plasma concentration, or intake of drugs binding to IB or IIA binding site, pharmacokinetics of phycocyanobilin may also be changed.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin",
volume = "5",
number = "76",
pages = "61787-61798",
doi = "10.1039/c5ra05534b"
}

Minić, S. L., Milčić, M. K., Stanić-Vučinić, D., Radibratović, M., Sotiroudis, T. G., Nikolić, M.,& Ćirković-Veličković, T.. (2015). Phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin. in RSC Advances
Royal Soc Chemistry, Cambridge., 5(76), 61787-61798.
https://doi.org/10.1039/c5ra05534b

Minić SL, Milčić MK, Stanić-Vučinić D, Radibratović M, Sotiroudis TG, Nikolić M, Ćirković-Veličković T. Phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin. in RSC Advances. 2015;5(76):61787-61798.
doi:10.1039/c5ra05534b .

Minić, Simeon L., Milčić, Miloš K., Stanić-Vučinić, Dragana, Radibratović, Milica, Sotiroudis, Theodore G., Nikolić, Milan, Ćirković-Veličković, Tanja, "Phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin" in RSC Advances, 5, no. 76 (2015):61787-61798,
https://doi.org/10.1039/c5ra05534b . .