TY  - JOUR
AU  - Nedić, Olgica
AU  - Penezić, Ana
AU  - Minić, Simeon
AU  - Radomirović, Mirjana Ž.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
AU  - Gligorijević, Nikola
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6028
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  - 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 Ž. 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 = "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. Ž., Nikolić, M., Ćirković-Veličković, T.,& Gligorijević, N.. (2023). Food Antioxidants and Their Interaction with Human Proteins. in Antioxidants
MDPI., 12(4), 815.
https://doi.org/10.3390/antiox12040815

Nedić O, Penezić A, Minić S, Radomirović MŽ, 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 Ž., 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  - Combet, Sophie
AU  - Nikolić, Milan
AU  - Minić, Simeon
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6451
AB  - C-phycocyanin (C-PC), a blue, light-harvesting protein from Arthrospira platensis, is known for industrial application as a food colourant. However, thermal treatment has detrimental effects on C-PC colour due to sensitivity to high temperatures; therefore, its application in the food industry is limited. Hence, stabilisation of the C-PC structure by adding small, food-derived molecules (e.g. sugars) or applying an alternative approach to thermal treatment, such as high-pressure (HP), may allow broader use of this protein. We aimed to study HP and thermal stability of C-PC in the presence of selected sugars (glucose, fructose and sucrose). Ex-situ absorption spectroscopy showed that 18% of glucose, sucrose and fructose solutions, upon incubation at 65℃, exhibit higher colour preservation (91.4, 52.9 and 52.5%, respectively) in comparison to the control (46.9%). HP treatment of C-PC at 450 MPa in 18% solutions of glucose, sucrose and fructose showed 90.1, 93.2 and 74.2% of residual absorbance, respectively, while the HP treatment of control gives 82.3% of residual absorbance. In situ thermal fluorescence measurements revealed that free C-PC has a melting point (Tm) of 55.4°C. In comparison, glucose and sucrose increase Tm of C-PC to 64.4 and 61.4°C, respectively, while fructose does not significantly influence C-PC melting point. In situ HP fluorescence study confirms the stabilisation effects of sugars: the transition pressure (P1/2) of C-PC (230 MPa) is substantially increased in the presence of glucose (277 MPa), sucrose (304 MPa) and fructose (273 MPa). These results showed that HP treatment has significantly less detrimental effects on C-PC colour stability than thermal treatment, and the overall stability of C-PC is substantially increased in the presence of sugars. In contrast, the sugar type determines the stabilisation effect's extent. Consequently, HP treatment of C-PC-containing food could provide an alternative to thermal processing to avoid losing its vivid blue colour.
PB  - FEBS Press
C3  - The 47th FEBS Congress, 8-12 July, Tours, France
T1  - Effects of sugars on thermal and high-pressure stability of C-phycocyanin from Arthrospira platensis
SP  - 232
EP  - 233
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6451
ER  - 

@conference{
author = "Veličković, Luka and Combet, Sophie and Nikolić, Milan and Minić, Simeon",
year = "2023",
abstract = "C-phycocyanin (C-PC), a blue, light-harvesting protein from Arthrospira platensis, is known for industrial application as a food colourant. However, thermal treatment has detrimental effects on C-PC colour due to sensitivity to high temperatures; therefore, its application in the food industry is limited. Hence, stabilisation of the C-PC structure by adding small, food-derived molecules (e.g. sugars) or applying an alternative approach to thermal treatment, such as high-pressure (HP), may allow broader use of this protein. We aimed to study HP and thermal stability of C-PC in the presence of selected sugars (glucose, fructose and sucrose). Ex-situ absorption spectroscopy showed that 18% of glucose, sucrose and fructose solutions, upon incubation at 65℃, exhibit higher colour preservation (91.4, 52.9 and 52.5%, respectively) in comparison to the control (46.9%). HP treatment of C-PC at 450 MPa in 18% solutions of glucose, sucrose and fructose showed 90.1, 93.2 and 74.2% of residual absorbance, respectively, while the HP treatment of control gives 82.3% of residual absorbance. In situ thermal fluorescence measurements revealed that free C-PC has a melting point (Tm) of 55.4°C. In comparison, glucose and sucrose increase Tm of C-PC to 64.4 and 61.4°C, respectively, while fructose does not significantly influence C-PC melting point. In situ HP fluorescence study confirms the stabilisation effects of sugars: the transition pressure (P1/2) of C-PC (230 MPa) is substantially increased in the presence of glucose (277 MPa), sucrose (304 MPa) and fructose (273 MPa). These results showed that HP treatment has significantly less detrimental effects on C-PC colour stability than thermal treatment, and the overall stability of C-PC is substantially increased in the presence of sugars. In contrast, the sugar type determines the stabilisation effect's extent. Consequently, HP treatment of C-PC-containing food could provide an alternative to thermal processing to avoid losing its vivid blue colour.",
publisher = "FEBS Press",
journal = "The 47th FEBS Congress, 8-12 July, Tours, France",
title = "Effects of sugars on thermal and high-pressure stability of C-phycocyanin from Arthrospira platensis",
pages = "232-233",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6451"
}

Veličković, L., Combet, S., Nikolić, M.,& Minić, S.. (2023). Effects of sugars on thermal and high-pressure stability of C-phycocyanin from Arthrospira platensis. in The 47th FEBS Congress, 8-12 July, Tours, France
FEBS Press., 232-233.
https://hdl.handle.net/21.15107/rcub_cherry_6451

Veličković L, Combet S, Nikolić M, Minić S. Effects of sugars on thermal and high-pressure stability of C-phycocyanin from Arthrospira platensis. in The 47th FEBS Congress, 8-12 July, Tours, France. 2023;:232-233.
https://hdl.handle.net/21.15107/rcub_cherry_6451 .

Veličković, Luka, Combet, Sophie, Nikolić, Milan, Minić, Simeon, "Effects of sugars on thermal and high-pressure stability of C-phycocyanin from Arthrospira platensis" in The 47th FEBS Congress, 8-12 July, Tours, France (2023):232-233,
https://hdl.handle.net/21.15107/rcub_cherry_6451 .

TY  - CONF
AU  - Nedić, Olgica
AU  - Gligorijević, Nikola
AU  - Penezić, Ana
AU  - Minić, Simeon
AU  - Radomirović, Mirjana Ž.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6031
AB  - Our research work was focused on interactions between resveratrol (R) and fibrinogen (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 : Faculty of Agriculture
C3  - 1st European Symposium on Phytochemicals in Medicine and Food, 7th-9th September, 2022. In: Book of Abstracts
T1  - Food antioxidants and their interaction with human proteins
SP  - 13
EP  - 13
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6031
ER  - 

@conference{
author = "Nedić, Olgica and Gligorijević, Nikola and Penezić, Ana and Minić, Simeon and Radomirović, Mirjana Ž. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Our research work was focused on interactions between resveratrol (R) and fibrinogen (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 : Faculty of Agriculture",
journal = "1st European Symposium on Phytochemicals in Medicine and Food, 7th-9th September, 2022. In: Book of Abstracts",
title = "Food antioxidants and their interaction with human proteins",
pages = "13-13",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6031"
}

Nedić, O., Gligorijević, N., Penezić, A., Minić, S., Radomirović, M. Ž., Nikolić, M.,& Ćirković-Veličković, T.. (2022). Food antioxidants and their interaction with human proteins. in 1st European Symposium on Phytochemicals in Medicine and Food, 7th-9th September, 2022. In: Book of Abstracts
Belgrade : Faculty of Agriculture., 13-13.
https://hdl.handle.net/21.15107/rcub_cherry_6031

Nedić O, Gligorijević N, Penezić A, Minić S, Radomirović MŽ, Nikolić M, Ćirković-Veličković T. Food antioxidants and their interaction with human proteins. in 1st European Symposium on Phytochemicals in Medicine and Food, 7th-9th September, 2022. In: Book of Abstracts. 2022;:13-13.
https://hdl.handle.net/21.15107/rcub_cherry_6031 .

Nedić, Olgica, Gligorijević, Nikola, Penezić, Ana, Minić, Simeon, Radomirović, Mirjana Ž., Nikolić, Milan, Ćirković-Veličković, Tanja, "Food antioxidants and their interaction with human proteins" in 1st European Symposium on Phytochemicals in Medicine and Food, 7th-9th September, 2022. In: Book of Abstracts (2022):13-13,
https://hdl.handle.net/21.15107/rcub_cherry_6031 .

TY  - CONF
AU  - Simović, Ana
AU  - Radomirović, Mirjana Ž.
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Minić, Simeon L.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5520
AB  - The emergence of the coronavirus SARS-CoV-2 has attracted attention of the whole scientific community. The SARS-CoV-2 spike (S) protein plays the most important role in viral attachment to host receptor angiotensin-converting enzyme 2 (ACE2), via the receptor-binding domain (RBD), fusion and entry into the host, and it serves as a target for the development of antibodies, entry inhibitors and vaccines. It has been demonstrated that phycocyanobilin (PCB), a bioactive open-chain tetrapyrrole chromophore of phycocyanin (PC), chromoprotein derived from the cyanobacterium Arthrospira platensis, can bind a plethora of different proteins, both in a noncovalent and covalent manner. This study aimed to investigate interactions of PCB with S protein and RBD respectively. Electrophoretic techniques, fluorescence spectroscopy, and inhibition of S–PCB and RBD–PCB covalent adduct formation using iodoacetamide and N-ethylmaleimide, were employed to examine interactions of PCB with S protein and RBD, while the effects of PCB binding on RBD structure were studied by CD spectroscopy. SDS-PAGE with Zn2+ staining has revealed that PCB covalently binds to both S protein and RBD, via free cysteine residues. Binding constants determined by the fluorescence quenching method were: 2.1×107 M–1 for PCB and S protein and 8.4×104 M–1 for PCB and RBD. Far-UV circular dichroism spectra showed that the binding of PCB influences RBD structure by decreasing the disordered structure content. Due to moderately strong noncovalent interactions of PCB with S protein and RBD, as well as covalent adducts formation, it may exert one of its many bioactive effects via impact on S protein binding to ACE2 receptor.
PB  - Faculty of Chemistry, Serbian Biochemical Society
C3  - Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia
T1  - Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain
SP  - 130
EP  - 131
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5520
ER  - 

@conference{
author = "Simović, Ana and Radomirović, Mirjana Ž. and Gligorijević, Nikola and Stanić-Vučinić, Dragana and Minić, Simeon L. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "The emergence of the coronavirus SARS-CoV-2 has attracted attention of the whole scientific community. The SARS-CoV-2 spike (S) protein plays the most important role in viral attachment to host receptor angiotensin-converting enzyme 2 (ACE2), via the receptor-binding domain (RBD), fusion and entry into the host, and it serves as a target for the development of antibodies, entry inhibitors and vaccines. It has been demonstrated that phycocyanobilin (PCB), a bioactive open-chain tetrapyrrole chromophore of phycocyanin (PC), chromoprotein derived from the cyanobacterium Arthrospira platensis, can bind a plethora of different proteins, both in a noncovalent and covalent manner. This study aimed to investigate interactions of PCB with S protein and RBD respectively. Electrophoretic techniques, fluorescence spectroscopy, and inhibition of S–PCB and RBD–PCB covalent adduct formation using iodoacetamide and N-ethylmaleimide, were employed to examine interactions of PCB with S protein and RBD, while the effects of PCB binding on RBD structure were studied by CD spectroscopy. SDS-PAGE with Zn2+ staining has revealed that PCB covalently binds to both S protein and RBD, via free cysteine residues. Binding constants determined by the fluorescence quenching method were: 2.1×107 M–1 for PCB and S protein and 8.4×104 M–1 for PCB and RBD. Far-UV circular dichroism spectra showed that the binding of PCB influences RBD structure by decreasing the disordered structure content. Due to moderately strong noncovalent interactions of PCB with S protein and RBD, as well as covalent adducts formation, it may exert one of its many bioactive effects via impact on S protein binding to ACE2 receptor.",
publisher = "Faculty of Chemistry, Serbian Biochemical Society",
journal = "Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia",
title = "Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain",
pages = "130-131",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5520"
}

Simović, A., Radomirović, M. Ž., Gligorijević, N., Stanić-Vučinić, D., Minić, S. L., Nikolić, M.,& Ćirković-Veličković, T.. (2022). Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain. in Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia
Faculty of Chemistry, Serbian Biochemical Society., 130-131.
https://hdl.handle.net/21.15107/rcub_cherry_5520

Simović A, Radomirović MŽ, Gligorijević N, Stanić-Vučinić D, Minić SL, Nikolić M, Ćirković-Veličković T. Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain. in Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia. 2022;:130-131.
https://hdl.handle.net/21.15107/rcub_cherry_5520 .

Simović, Ana, Radomirović, Mirjana Ž., Gligorijević, Nikola, Stanić-Vučinić, Dragana, Minić, Simeon L., Nikolić, Milan, Ćirković-Veličković, Tanja, "Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain" in Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia (2022):130-131,
https://hdl.handle.net/21.15107/rcub_cherry_5520 .

TY  - CONF
AU  - Jovanović, Zorana
AU  - Veličković, Luka
AU  - Gligorijević, Nikola
AU  - Šunderić, Miloš
AU  - Zoumpanioti, Maria
AU  - Minić, Simeon L.
AU  - Nikolić, Milan
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5785
AB  - To minimize the impact of artificial food colouring (e.g., in drinks) on health, chemical dyes are increasingly replaced by natural 
ones. C-phycocyanin (C-PC), hexameric light-harvesting phycobiliprotein from cyanobacteria Artrhorspira platensis, has been 
proposed as an alternative. The intensive blue colour of C-PC arises from phycocyanobilin (PCB), the covalently attached 
tetrapyrrole chromophores. The presence of PCB chromophores gives C-PC a broad range of bioactive effects (antioxidant, 
anticancer, and immunomodulatory ones), substantially increasing their potential for applications in the food industry. However, 
C-PC issensitive to temperature, and its colour significantly diminishes by thermal treatment, limiting its use in the food industry. 
Hence, improving C-PC stability is the major challenge for successful application in food and beverage colouring. It is well 
known that binding small, high-affinity ligands significantly improve protein stability. Therefore, selecting food-derived ligands 
(such as vitamins, polyphenols, sugars, etc.) with the ability to bind C-PC firmly could be a promising strategy to increase the
C-PC stability and preserve its colour, which should increase its application potential in the food industry.
The main aim of this study is to characterize the binding of selected food-derived ligands (including quercetin, coenzyme Q10, 
gallic acid, vanillic acid, vanillin, resveratrol, glucose, fructose, sucrose, vitamin K, menthol, and dihydrolipoic acid) to C-PC 
by standard spectroscopic methods (UV/VIS absorption spectroscopy, spectrofluorimetry, and CD spectroscopy). Quercetin has
the strongest binding affinity to C-PC (Ka~3.7x105 M-1
), and its effects on C-PC structure and stability have been further 
investigated. CD spectroscopy revealed that quercetin induces stabilization of the protein secondary structure under simulated 
physiological conditions, while the conformation of the PCB chromophore is altered upon quercetin binding. Furthermore, 
quercetin binding increases the thermal stability of C-PC. 
Overall, our study revealed the ability of high-affinity, food-derived ligands to increase the stability of C-PC, which may enhance 
its application potential in the food industry.
PB  - Belgrade : Faculty of Chemistry
C3  - Serbian Biochemical Society, Eleventh Conference, Scientific meeting of an international character: "Amazing Biochemistry"; 2022 Sep 22-23; Novi Sad, Serbia
T1  - C-Phycocyanin from cyanobacteria Artrhorspira platensis: Binding of selected  food-derived ligands
SP  - 165
EP  - 165
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5785
ER  - 

@conference{
author = "Jovanović, Zorana and Veličković, Luka and Gligorijević, Nikola and Šunderić, Miloš and Zoumpanioti, Maria and Minić, Simeon L. and Nikolić, Milan",
year = "2022",
abstract = "To minimize the impact of artificial food colouring (e.g., in drinks) on health, chemical dyes are increasingly replaced by natural 
ones. C-phycocyanin (C-PC), hexameric light-harvesting phycobiliprotein from cyanobacteria Artrhorspira platensis, has been 
proposed as an alternative. The intensive blue colour of C-PC arises from phycocyanobilin (PCB), the covalently attached 
tetrapyrrole chromophores. The presence of PCB chromophores gives C-PC a broad range of bioactive effects (antioxidant, 
anticancer, and immunomodulatory ones), substantially increasing their potential for applications in the food industry. However, 
C-PC issensitive to temperature, and its colour significantly diminishes by thermal treatment, limiting its use in the food industry. 
Hence, improving C-PC stability is the major challenge for successful application in food and beverage colouring. It is well 
known that binding small, high-affinity ligands significantly improve protein stability. Therefore, selecting food-derived ligands 
(such as vitamins, polyphenols, sugars, etc.) with the ability to bind C-PC firmly could be a promising strategy to increase the
C-PC stability and preserve its colour, which should increase its application potential in the food industry.
The main aim of this study is to characterize the binding of selected food-derived ligands (including quercetin, coenzyme Q10, 
gallic acid, vanillic acid, vanillin, resveratrol, glucose, fructose, sucrose, vitamin K, menthol, and dihydrolipoic acid) to C-PC 
by standard spectroscopic methods (UV/VIS absorption spectroscopy, spectrofluorimetry, and CD spectroscopy). Quercetin has
the strongest binding affinity to C-PC (Ka~3.7x105 M-1
), and its effects on C-PC structure and stability have been further 
investigated. CD spectroscopy revealed that quercetin induces stabilization of the protein secondary structure under simulated 
physiological conditions, while the conformation of the PCB chromophore is altered upon quercetin binding. Furthermore, 
quercetin binding increases the thermal stability of C-PC. 
Overall, our study revealed the ability of high-affinity, food-derived ligands to increase the stability of C-PC, which may enhance 
its application potential in the food industry.",
publisher = "Belgrade : Faculty of Chemistry",
journal = "Serbian Biochemical Society, Eleventh Conference, Scientific meeting of an international character: "Amazing Biochemistry"; 2022 Sep 22-23; Novi Sad, Serbia",
title = "C-Phycocyanin from cyanobacteria Artrhorspira platensis: Binding of selected  food-derived ligands",
pages = "165-165",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5785"
}

Jovanović, Z., Veličković, L., Gligorijević, N., Šunderić, M., Zoumpanioti, M., Minić, S. L.,& Nikolić, M.. (2022). C-Phycocyanin from cyanobacteria Artrhorspira platensis: Binding of selected  food-derived ligands. in Serbian Biochemical Society, Eleventh Conference, Scientific meeting of an international character: "Amazing Biochemistry"; 2022 Sep 22-23; Novi Sad, Serbia
Belgrade : Faculty of Chemistry., 165-165.
https://hdl.handle.net/21.15107/rcub_cherry_5785

Jovanović Z, Veličković L, Gligorijević N, Šunderić M, Zoumpanioti M, Minić SL, Nikolić M. C-Phycocyanin from cyanobacteria Artrhorspira platensis: Binding of selected  food-derived ligands. in Serbian Biochemical Society, Eleventh Conference, Scientific meeting of an international character: "Amazing Biochemistry"; 2022 Sep 22-23; Novi Sad, Serbia. 2022;:165-165.
https://hdl.handle.net/21.15107/rcub_cherry_5785 .

Jovanović, Zorana, Veličković, Luka, Gligorijević, Nikola, Šunderić, Miloš, Zoumpanioti, Maria, Minić, Simeon L., Nikolić, Milan, "C-Phycocyanin from cyanobacteria Artrhorspira platensis: Binding of selected  food-derived ligands" in Serbian Biochemical Society, Eleventh Conference, Scientific meeting of an international character: "Amazing Biochemistry"; 2022 Sep 22-23; Novi Sad, Serbia (2022):165-165,
https://hdl.handle.net/21.15107/rcub_cherry_5785 .

TY  - CONF
AU  - Minić, Simeon L.
AU  - Jovanović, Zorana
AU  - Veličlović, Luka
AU  - Gligorijević, Nikola
AU  - Zoumpanioti, Maria
AU  - Nikolić, Milan
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5786
AB  - Stabilization of the vivid colors of phycobiliproteins of micro/macroalgae is a prerequisite
for their greater use in the food industry. Phycocyanin (C-PC) was purified from
cyanobacteria Spirulina (Arthrospira) Pacifica raw extract by ammonium sulfate protein
precipitation and anion ion-exchange chromatography. Purity was confirmed
electrophoretically (SDS-PAGE). The binding of ten selected bioactive polyphenols to CPC (including quercetin, coenzyme Q10, gallic acid, vanillic acid, and resveratrol) was
examined by standard spectroscopic methods. Quercetin is shown to have the strongest
binding (Ka~3x105
 M-1), with stabilization of the secondary protein structure under
physiological conditions.
AB  - Stabilizacija živopisnih boja fikobilinskih proteina mikro/makroalgi preduslov je za
njihovo veće korišćenje u industriji hrane. Fikocijanin (C-PC) je prečišćen iz sirovog
ekstrakta cijanobakterije Spirulina (Arthrospira) Pacifica, taloženjem proteina amonijumsulfatom i anjonskom jonoizmenjivačkom hromatografijom. Čistoća je potvrđena
elektroforetski (SDS-PAGE). Vezivanje deset odabranih bioaktivnih polifenola za C-PC
(uključujući kvarcetin, koenzim Q10, galnu kiselinu, vanilinsku kiselinu i resveratrol)
ispitano je standardnim spektroskopskim metodama. Kvarcetin je pokazao najjače
vezivanje (Ka~3x105
 M-1), uz stabilizaciju sekundarne strukture proteina pod fiziološkim
uslovima.
PB  - Belgrade : Serbian Chemical Society
C3  - 58th Meeting of the Serbian Chemical Society, Belgrade, Serbia, 9th-10th June, 2022. In: Book of Abstracts and Proceedings
T1  - Phycocyanin from microalgae Spirulina: purification and binding of selected (poly)phenols
SP  - 62
EP  - 62
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5786
ER  - 

@conference{
author = "Minić, Simeon L. and Jovanović, Zorana and Veličlović, Luka and Gligorijević, Nikola and Zoumpanioti, Maria and Nikolić, Milan",
year = "2022",
abstract = "Stabilization of the vivid colors of phycobiliproteins of micro/macroalgae is a prerequisite
for their greater use in the food industry. Phycocyanin (C-PC) was purified from
cyanobacteria Spirulina (Arthrospira) Pacifica raw extract by ammonium sulfate protein
precipitation and anion ion-exchange chromatography. Purity was confirmed
electrophoretically (SDS-PAGE). The binding of ten selected bioactive polyphenols to CPC (including quercetin, coenzyme Q10, gallic acid, vanillic acid, and resveratrol) was
examined by standard spectroscopic methods. Quercetin is shown to have the strongest
binding (Ka~3x105
 M-1), with stabilization of the secondary protein structure under
physiological conditions., Stabilizacija živopisnih boja fikobilinskih proteina mikro/makroalgi preduslov je za
njihovo veće korišćenje u industriji hrane. Fikocijanin (C-PC) je prečišćen iz sirovog
ekstrakta cijanobakterije Spirulina (Arthrospira) Pacifica, taloženjem proteina amonijumsulfatom i anjonskom jonoizmenjivačkom hromatografijom. Čistoća je potvrđena
elektroforetski (SDS-PAGE). Vezivanje deset odabranih bioaktivnih polifenola za C-PC
(uključujući kvarcetin, koenzim Q10, galnu kiselinu, vanilinsku kiselinu i resveratrol)
ispitano je standardnim spektroskopskim metodama. Kvarcetin je pokazao najjače
vezivanje (Ka~3x105
 M-1), uz stabilizaciju sekundarne strukture proteina pod fiziološkim
uslovima.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "58th Meeting of the Serbian Chemical Society, Belgrade, Serbia, 9th-10th June, 2022. In: Book of Abstracts and Proceedings",
title = "Phycocyanin from microalgae Spirulina: purification and binding of selected (poly)phenols",
pages = "62-62",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5786"
}

Minić, S. L., Jovanović, Z., Veličlović, L., Gligorijević, N., Zoumpanioti, M.,& Nikolić, M.. (2022). Phycocyanin from microalgae Spirulina: purification and binding of selected (poly)phenols. in 58th Meeting of the Serbian Chemical Society, Belgrade, Serbia, 9th-10th June, 2022. In: Book of Abstracts and Proceedings
Belgrade : Serbian Chemical Society., 62-62.
https://hdl.handle.net/21.15107/rcub_cherry_5786

Minić SL, Jovanović Z, Veličlović L, Gligorijević N, Zoumpanioti M, Nikolić M. Phycocyanin from microalgae Spirulina: purification and binding of selected (poly)phenols. in 58th Meeting of the Serbian Chemical Society, Belgrade, Serbia, 9th-10th June, 2022. In: Book of Abstracts and Proceedings. 2022;:62-62.
https://hdl.handle.net/21.15107/rcub_cherry_5786 .

Minić, Simeon L., Jovanović, Zorana, Veličlović, Luka, Gligorijević, Nikola, Zoumpanioti, Maria, Nikolić, Milan, "Phycocyanin from microalgae Spirulina: purification and binding of selected (poly)phenols" in 58th Meeting of the Serbian Chemical Society, Belgrade, Serbia, 9th-10th June, 2022. In: Book of Abstracts and Proceedings (2022):62-62,
https://hdl.handle.net/21.15107/rcub_cherry_5786 .

TY  - CHAP
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5985
AB  - Bilirubin is a tetrapyrrole, yellow pigment, and it is a degradation productcreated in heme metabolism. This molecule is predominantly present inits unconjugated form in circulation, and it is mainly bound to humanserum albumin. The presence of small amounts of free, unconjugatedbilirubin enables its interactions with other circulation components. Inconditions like Gilbert syndrome or diabetes, the concentration ofunconjugated bilirubin increases in the blood, making other interactingpartners from circulation more important for its metabolism. In the liver,bilirubin is converted to conjugated form, which is then excreted fromthe organism. While the significant increase of bilirubin is toxic, researchsuggests that small increases may be beneficial since bilirubin hasantioxidative and anticancer potential. In this chapter, interactions ofbilirubin with several proteins will be described together with the effectsof 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 productcreated in heme metabolism. This molecule is predominantly present inits unconjugated form in circulation, and it is mainly bound to humanserum albumin. The presence of small amounts of free, unconjugatedbilirubin enables its interactions with other circulation components. Inconditions like Gilbert syndrome or diabetes, the concentration ofunconjugated bilirubin increases in the blood, making other interactingpartners from circulation more important for its metabolism. In the liver,bilirubin is converted to conjugated form, which is then excreted fromthe organism. While the significant increase of bilirubin is toxic, researchsuggests that small increases may be beneficial since bilirubin hasantioxidative and anticancer potential. In this chapter, interactions ofbilirubin with several proteins will be described together with the effectsof 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  - Radomirović, Mirjana Ž.
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Nikolić, Milan
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6029
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  - Federation of European Biochemical Societies
PB  - Wiley
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_cherry_6029
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. 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 = "Federation of European Biochemical Societies, Wiley",
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_cherry_6029"
}

Radomirović, M. Ž., 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
Federation of European Biochemical Societies., 12(Suppl. 1), 302-303.
https://hdl.handle.net/21.15107/rcub_cherry_6029

Radomirović MŽ, 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_cherry_6029 .

Radomirović, Mirjana Ž., 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_cherry_6029 .

TY  - CONF
AU  - Veličković, Luka
AU  - Nikolić, Milan
AU  - Minić, Simeon L.
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5780
AB  - C-phycocyanin (C-PC), the major protein of cyanobacteria Arthrospira platensis, is a blue
pigment that primarily transfers energy during photosynthesis.It has diverse
biotechnological applications since it can be used in nutraceutical, cosmetics,
pharmaceutical industries, and biomedical research.Its intensive blue colour and strong
antioxidant activity give C-PC significant potential to replace synthetic colourants in the
food industry. However, thermal treatment of food has detrimental effects on C-PC colour
due to sensitivity to higher temperatures; therefore,the application of this natural colourant
in food and other products is limited. Hence, improving C-PC stability is the major
challenge for successful application in food and beverages colouring. In the light of this,we
aim to investigate the thermal stability of C-PC in the presence of selected sugars (glucose,
fructose and sucrose), commonly used in the food industry. Ex-situabsorption
spectrophotometryshowed that 18% solution (w/v) of glucose, sucrose and fructose at pH
7,upon incubation at 65℃, exhibit 91.4, 52.9 and 52.5% of colour preservation,
respectively.In situ fluorescence measurements revealed that free C-PC has a melting point
of 55.4°C, while the presence of glucose and sucrose increases the melting point of C-PC
to 64.4 and 61.4°C, respectively. On the other hand, fructose does not significantly
influence the C-PC melting point. These results show that the thermal stability ofthe CPCsolution is substantially increased in the presence of sugars, while the type of sugar
significantly determines the extent of the stabilisation effect. Overall, our study provides
the strategy for enhancing the application potential of C-PC as natural food colourant,
providing a food product with vivid blue colour and substantial antioxidant activities.
PB  - Belgrade : Serbian Biochemical Society
C3  - Serbian Biochemical Society, The XI Conference "Amazing Biochemistry"  Novi Sad, Faculty of Sciences, 22nd and 23rd of September, 2022
T1  - Sugar-mediated thermal stabilisation of C-phycocyanin from Arthrospira platensis
SP  - 165
EP  - 165
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5780
ER  - 

@conference{
author = "Veličković, Luka and Nikolić, Milan and Minić, Simeon L.",
year = "2022",
abstract = "C-phycocyanin (C-PC), the major protein of cyanobacteria Arthrospira platensis, is a blue
pigment that primarily transfers energy during photosynthesis.It has diverse
biotechnological applications since it can be used in nutraceutical, cosmetics,
pharmaceutical industries, and biomedical research.Its intensive blue colour and strong
antioxidant activity give C-PC significant potential to replace synthetic colourants in the
food industry. However, thermal treatment of food has detrimental effects on C-PC colour
due to sensitivity to higher temperatures; therefore,the application of this natural colourant
in food and other products is limited. Hence, improving C-PC stability is the major
challenge for successful application in food and beverages colouring. In the light of this,we
aim to investigate the thermal stability of C-PC in the presence of selected sugars (glucose,
fructose and sucrose), commonly used in the food industry. Ex-situabsorption
spectrophotometryshowed that 18% solution (w/v) of glucose, sucrose and fructose at pH
7,upon incubation at 65℃, exhibit 91.4, 52.9 and 52.5% of colour preservation,
respectively.In situ fluorescence measurements revealed that free C-PC has a melting point
of 55.4°C, while the presence of glucose and sucrose increases the melting point of C-PC
to 64.4 and 61.4°C, respectively. On the other hand, fructose does not significantly
influence the C-PC melting point. These results show that the thermal stability ofthe CPCsolution is substantially increased in the presence of sugars, while the type of sugar
significantly determines the extent of the stabilisation effect. Overall, our study provides
the strategy for enhancing the application potential of C-PC as natural food colourant,
providing a food product with vivid blue colour and substantial antioxidant activities.",
publisher = "Belgrade : Serbian Biochemical Society",
journal = "Serbian Biochemical Society, The XI Conference "Amazing Biochemistry"  Novi Sad, Faculty of Sciences, 22nd and 23rd of September, 2022",
title = "Sugar-mediated thermal stabilisation of C-phycocyanin from Arthrospira platensis",
pages = "165-165",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5780"
}

Veličković, L., Nikolić, M.,& Minić, S. L.. (2022). Sugar-mediated thermal stabilisation of C-phycocyanin from Arthrospira platensis. in Serbian Biochemical Society, The XI Conference "Amazing Biochemistry"  Novi Sad, Faculty of Sciences, 22nd and 23rd of September, 2022
Belgrade : Serbian Biochemical Society., 165-165.
https://hdl.handle.net/21.15107/rcub_cherry_5780

Veličković L, Nikolić M, Minić SL. Sugar-mediated thermal stabilisation of C-phycocyanin from Arthrospira platensis. in Serbian Biochemical Society, The XI Conference "Amazing Biochemistry"  Novi Sad, Faculty of Sciences, 22nd and 23rd of September, 2022. 2022;:165-165.
https://hdl.handle.net/21.15107/rcub_cherry_5780 .

Veličković, Luka, Nikolić, Milan, Minić, Simeon L., "Sugar-mediated thermal stabilisation of C-phycocyanin from Arthrospira platensis" in Serbian Biochemical Society, The XI Conference "Amazing Biochemistry"  Novi Sad, Faculty of Sciences, 22nd and 23rd of September, 2022 (2022):165-165,
https://hdl.handle.net/21.15107/rcub_cherry_5780 .

TY  - JOUR
AU  - Simović, Ana
AU  - Combet, Sophie
AU  - Ćirković-Veličković, Tanja
AU  - Nikolic, Milan
AU  - Minić, Simeon L.
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5002
AB  - This study aimed to characterise the stability of R-phycoerythrin (R-PE), a vivid natural colourant with emerging
potential for application in the food industry. High-quality (A560/A280 ≥ 5), native (α-helix content 75%) R-PE
was purified from commercial dried Nori (Porphyra sp.) flakes. Thermal unfolding revealed two transitions (at 56
and 72 ◦C), ascribed to different protein subunits. Contrary to elevated temperature, high-pressure (HP) treatment showed significant advantages: The R-PE unfolding was partly reversible and the colour bleaching was
minimal. Binding of Cu2+ (6.3 × 105 M− 1
) and Zn2+ (1.7 × 103 M− 1
) influenced conformational changes in the
protein tetrapyrrole chromophore without affecting R-PE structure and stability (colour). The results give new
insights into the stability of R-PE suggesting its usefulness for the replacement of toxic synthetic dyes. Preservation of the red colour of R-PE could be considered in fortified food and beverages by HP processing. R-PE may
act as a biosensor for Cu2+ in aquatic systems.
PB  - Elsevier
T2  - Food Chemistry
T1  - Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes
VL  - 374
IS  - 131780
DO  - 10.1016/j.foodchem.2021.131780
ER  - 

@article{
author = "Simović, Ana and Combet, Sophie and Ćirković-Veličković, Tanja and Nikolic, Milan and Minić, Simeon L.",
year = "2022",
abstract = "This study aimed to characterise the stability of R-phycoerythrin (R-PE), a vivid natural colourant with emerging
potential for application in the food industry. High-quality (A560/A280 ≥ 5), native (α-helix content 75%) R-PE
was purified from commercial dried Nori (Porphyra sp.) flakes. Thermal unfolding revealed two transitions (at 56
and 72 ◦C), ascribed to different protein subunits. Contrary to elevated temperature, high-pressure (HP) treatment showed significant advantages: The R-PE unfolding was partly reversible and the colour bleaching was
minimal. Binding of Cu2+ (6.3 × 105 M− 1
) and Zn2+ (1.7 × 103 M− 1
) influenced conformational changes in the
protein tetrapyrrole chromophore without affecting R-PE structure and stability (colour). The results give new
insights into the stability of R-PE suggesting its usefulness for the replacement of toxic synthetic dyes. Preservation of the red colour of R-PE could be considered in fortified food and beverages by HP processing. R-PE may
act as a biosensor for Cu2+ in aquatic systems.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes",
volume = "374",
number = "131780",
doi = "10.1016/j.foodchem.2021.131780"
}

Simović, A., Combet, S., Ćirković-Veličković, T., Nikolic, M.,& Minić, S. L.. (2022). Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes. in Food Chemistry
Elsevier., 374(131780).
https://doi.org/10.1016/j.foodchem.2021.131780

Simović A, Combet S, Ćirković-Veličković T, Nikolic M, Minić SL. Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes. in Food Chemistry. 2022;374(131780).
doi:10.1016/j.foodchem.2021.131780 .

Simović, Ana, Combet, Sophie, Ćirković-Veličković, Tanja, Nikolic, Milan, Minić, Simeon L., "Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes" in Food Chemistry, 374, no. 131780 (2022),
https://doi.org/10.1016/j.foodchem.2021.131780 . .

TY  - DATA
AU  - Simović, Ana
AU  - Combet, Sophie
AU  - Ćirković-Veličković, Tanja
AU  - Nikolic, Milan
AU  - Minić, Simeon L.
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5003
PB  - Elsevier
T2  - Food Chemistry
T1  - Supplementary data for the article: Simović, A.; Combet, S.; Ćirković-Veličković, T.; Nikolic, M.; Minić, S. L. Probing the Stability of the Food Colourant R-Phycoerythrin from Dried Nori Flakes. Food Chemistry 2022, 374 (131780). https://doi.org/10.1016/j.foodchem.2021.131780.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5003
ER  - 

@misc{
author = "Simović, Ana and Combet, Sophie and Ćirković-Veličković, Tanja and Nikolic, Milan and Minić, Simeon L.",
year = "2022",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Supplementary data for the article: Simović, A.; Combet, S.; Ćirković-Veličković, T.; Nikolic, M.; Minić, S. L. Probing the Stability of the Food Colourant R-Phycoerythrin from Dried Nori Flakes. Food Chemistry 2022, 374 (131780). https://doi.org/10.1016/j.foodchem.2021.131780.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5003"
}

Simović, A., Combet, S., Ćirković-Veličković, T., Nikolic, M.,& Minić, S. L.. (2022). Supplementary data for the article: Simović, A.; Combet, S.; Ćirković-Veličković, T.; Nikolic, M.; Minić, S. L. Probing the Stability of the Food Colourant R-Phycoerythrin from Dried Nori Flakes. Food Chemistry 2022, 374 (131780). https://doi.org/10.1016/j.foodchem.2021.131780.. in Food Chemistry
Elsevier..
https://hdl.handle.net/21.15107/rcub_cherry_5003

Simović A, Combet S, Ćirković-Veličković T, Nikolic M, Minić SL. Supplementary data for the article: Simović, A.; Combet, S.; Ćirković-Veličković, T.; Nikolic, M.; Minić, S. L. Probing the Stability of the Food Colourant R-Phycoerythrin from Dried Nori Flakes. Food Chemistry 2022, 374 (131780). https://doi.org/10.1016/j.foodchem.2021.131780.. in Food Chemistry. 2022;.
https://hdl.handle.net/21.15107/rcub_cherry_5003 .

Simović, Ana, Combet, Sophie, Ćirković-Veličković, Tanja, Nikolic, Milan, Minić, Simeon L., "Supplementary data for the article: Simović, A.; Combet, S.; Ćirković-Veličković, T.; Nikolic, M.; Minić, S. L. Probing the Stability of the Food Colourant R-Phycoerythrin from Dried Nori Flakes. Food Chemistry 2022, 374 (131780). https://doi.org/10.1016/j.foodchem.2021.131780." in Food Chemistry (2022),
https://hdl.handle.net/21.15107/rcub_cherry_5003 .

TY  - CONF
AU  - Obradović, Milica
AU  - Nikolić, Milan
AU  - Minić, Simeon L.
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5787
AB  - Phycobiliproteins are major photosynthetic accessory pigments in cyanobacteria and red
algae. Their vivid colours arise from covalently attached tetrapyrrole chromophores. The
exciting characteristic of tetrapyrrole chromophores is the ability to bind metal ions. Heavy
metals are among the most abundant and most dangerous environmental pollutants, and
their removal from the environment is a crucial challenge. Therefore, utilizing PBPs-metal
binding properties could be helpful in heavy metal detection and/or removal. The main aim
of this study is to characterize the binding of selected heavy metal ions (Hg2+, Pb2+, Cd2+)
to R-phycocyanin (R-PC) isolated and purified from red algae Porphyra spp.The protein
fluorescence quenching approach revealed the strong binding affinity of R-PC to Hg2+
(Kd~0.1 μM), while protein binding to Pb2+ and Cd2+ is lower (Kd~3 μM) but still in the
high to moderate range. Circular dichroism spectroscopy demonstrated the ability of Hg2+,
Pb2+ and Cd2+ to slightly -helical content) in
R-PC. Our results indicatethat R-PC could beexploited as a potential biosensor for heavy
metal ions detection (especially Hg2+) in aquatic systems as well as in their removal from
the environment (e.g. waste-water management).
PB  - Belgrade : Faculty of Chemistry
C3  - Serbian Biochemical Society, Eleventh Conference, Scientific meeting of an international character: "Amazing Biochemistry"; 2022 Sep 22-23; Novi Sad, Serbia
T1  - R-Phycocyanin from red algae Porphyra spp: Binding of selected heavy metal ions
SP  - 113
EP  - 113
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5787
ER  - 

@conference{
author = "Obradović, Milica and Nikolić, Milan and Minić, Simeon L.",
year = "2022",
abstract = "Phycobiliproteins are major photosynthetic accessory pigments in cyanobacteria and red
algae. Their vivid colours arise from covalently attached tetrapyrrole chromophores. The
exciting characteristic of tetrapyrrole chromophores is the ability to bind metal ions. Heavy
metals are among the most abundant and most dangerous environmental pollutants, and
their removal from the environment is a crucial challenge. Therefore, utilizing PBPs-metal
binding properties could be helpful in heavy metal detection and/or removal. The main aim
of this study is to characterize the binding of selected heavy metal ions (Hg2+, Pb2+, Cd2+)
to R-phycocyanin (R-PC) isolated and purified from red algae Porphyra spp.The protein
fluorescence quenching approach revealed the strong binding affinity of R-PC to Hg2+
(Kd~0.1 μM), while protein binding to Pb2+ and Cd2+ is lower (Kd~3 μM) but still in the
high to moderate range. Circular dichroism spectroscopy demonstrated the ability of Hg2+,
Pb2+ and Cd2+ to slightly -helical content) in
R-PC. Our results indicatethat R-PC could beexploited as a potential biosensor for heavy
metal ions detection (especially Hg2+) in aquatic systems as well as in their removal from
the environment (e.g. waste-water management).",
publisher = "Belgrade : Faculty of Chemistry",
journal = "Serbian Biochemical Society, Eleventh Conference, Scientific meeting of an international character: "Amazing Biochemistry"; 2022 Sep 22-23; Novi Sad, Serbia",
title = "R-Phycocyanin from red algae Porphyra spp: Binding of selected heavy metal ions",
pages = "113-113",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5787"
}

Obradović, M., Nikolić, M.,& Minić, S. L.. (2022). R-Phycocyanin from red algae Porphyra spp: Binding of selected heavy metal ions. in Serbian Biochemical Society, Eleventh Conference, Scientific meeting of an international character: "Amazing Biochemistry"; 2022 Sep 22-23; Novi Sad, Serbia
Belgrade : Faculty of Chemistry., 113-113.
https://hdl.handle.net/21.15107/rcub_cherry_5787

Obradović M, Nikolić M, Minić SL. R-Phycocyanin from red algae Porphyra spp: Binding of selected heavy metal ions. in Serbian Biochemical Society, Eleventh Conference, Scientific meeting of an international character: "Amazing Biochemistry"; 2022 Sep 22-23; Novi Sad, Serbia. 2022;:113-113.
https://hdl.handle.net/21.15107/rcub_cherry_5787 .

Obradović, Milica, Nikolić, Milan, Minić, Simeon L., "R-Phycocyanin from red algae Porphyra spp: Binding of selected heavy metal ions" in Serbian Biochemical Society, Eleventh Conference, Scientific meeting of an international character: "Amazing Biochemistry"; 2022 Sep 22-23; Novi Sad, Serbia (2022):113-113,
https://hdl.handle.net/21.15107/rcub_cherry_5787 .

TY  - JOUR
AU  - Radomirović, Mirjana Ž.
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Van Haute, Sam
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4863
AB  - β-lactoglobulin (BLG) is a major whey protein with numerous techno-functional properties desirable for the food industry. Phycocyanobilin (PCB), a bioactive pigment of Arthrospira platensis with health-promoting effects, covalently binds to BLG at physiological pH. This study investigated the effects of this covalent modification on BLG functional properties. The BLG–PCB adduct possesses enhanced antioxidant properties, and bound PCB protects BLG against free radical-induced oxidation. Despite the similar thermal stabilities of BLG and BLG–PCB, BLG–PCB is less susceptible to covalent and noncovalent aggregation under moderate heat treatment (63 °C, 30 min). Blocked thiol group and reduced hydrophobicity due to hindering of hydrophobic residues by bound PCB, as well as the heat-induced transition of β-sheet to α-helix, contributed to the low susceptibility of BLG–PCB to aggregation. BLG–PCB has a higher resistance to pepsin and pancreatin digestion than BLG and unaltered IgE-binding properties. The improved functional properties of BLG–PCB make it a useful ingredient in the food industry.
PB  - Elsevier
T2  - Food Hydrocolloids
T1  - Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating
VL  - 123
SP  - 107169
DO  - 10.1016/j.foodhyd.2021.107169
ER  - 

@article{
author = "Radomirović, Mirjana Ž. and Minić, Simeon L. and Stanić-Vučinić, Dragana and Nikolić, Milan and Van Haute, Sam and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "β-lactoglobulin (BLG) is a major whey protein with numerous techno-functional properties desirable for the food industry. Phycocyanobilin (PCB), a bioactive pigment of Arthrospira platensis with health-promoting effects, covalently binds to BLG at physiological pH. This study investigated the effects of this covalent modification on BLG functional properties. The BLG–PCB adduct possesses enhanced antioxidant properties, and bound PCB protects BLG against free radical-induced oxidation. Despite the similar thermal stabilities of BLG and BLG–PCB, BLG–PCB is less susceptible to covalent and noncovalent aggregation under moderate heat treatment (63 °C, 30 min). Blocked thiol group and reduced hydrophobicity due to hindering of hydrophobic residues by bound PCB, as well as the heat-induced transition of β-sheet to α-helix, contributed to the low susceptibility of BLG–PCB to aggregation. BLG–PCB has a higher resistance to pepsin and pancreatin digestion than BLG and unaltered IgE-binding properties. The improved functional properties of BLG–PCB make it a useful ingredient in the food industry.",
publisher = "Elsevier",
journal = "Food Hydrocolloids",
title = "Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating",
volume = "123",
pages = "107169",
doi = "10.1016/j.foodhyd.2021.107169"
}

Radomirović, M. Ž., Minić, S. L., Stanić-Vučinić, D., Nikolić, M., Van Haute, S., Rajković, A.,& Ćirković-Veličković, T.. (2022). Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating. in Food Hydrocolloids
Elsevier., 123, 107169.
https://doi.org/10.1016/j.foodhyd.2021.107169

Radomirović MŽ, Minić SL, Stanić-Vučinić D, Nikolić M, Van Haute S, Rajković A, Ćirković-Veličković T. Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating. in Food Hydrocolloids. 2022;123:107169.
doi:10.1016/j.foodhyd.2021.107169 .

Radomirović, Mirjana Ž., Minić, Simeon L., Stanić-Vučinić, Dragana, Nikolić, Milan, Van Haute, Sam, Rajković, Andreja, Ćirković-Veličković, Tanja, "Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating" in Food Hydrocolloids, 123 (2022):107169,
https://doi.org/10.1016/j.foodhyd.2021.107169 . .

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Annighofer, Burkhard
AU  - Helary, Arnaud
AU  - Sago, Laıla
AU  - Cornu, David
AU  - Brulet, Annie
AU  - Combet, Sophie
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5690
AB  - High pressure (HP) is a particularly powerful tool to study protein folding/unfolding, revealing subtle structural rearrangements.
Bovine b-lactoglobulin (BLG), a protein of interest in food science, exhibits a strong propensity to bind various
bioactive molecules. We probed the effects of the binding of biliverdin (BV), a tetrapyrrole linear chromophore, on the stability
of BLG under pressure, by combining in situ HP small-angle neutron scattering (SANS) and HP-UV absorption spectroscopy.
Although BV induces a slight destabilization of BLG during HP-induced unfolding, a ligand excess strongly prevents BLG oligomerization.
Moreover, at SANS resolution, an excess of BV induces the complete recovery of the protein ‘‘native’’ 3D structure
after HP removal, despite the presence of the BV covalently bound adduct. Mass spectrometry highlights the crucial role of
cysteine residues in the competitive and protective effects of BV during pressure denaturation of BLG through SH/S-S
exchange.
PB  - Biophysical Society
T2  - Biophysical Journal
T1  - Structure of proteins under pressure: Covalent binding effects of biliverdin on b-lactoglobulin
VL  - 121
SP  - 1
EP  - 12
DO  - 10.1016/j.bpj.2022.06.003
ER  - 

@article{
author = "Minić, Simeon L. and Annighofer, Burkhard and Helary, Arnaud and Sago, Laıla and Cornu, David and Brulet, Annie and Combet, Sophie",
year = "2022",
abstract = "High pressure (HP) is a particularly powerful tool to study protein folding/unfolding, revealing subtle structural rearrangements.
Bovine b-lactoglobulin (BLG), a protein of interest in food science, exhibits a strong propensity to bind various
bioactive molecules. We probed the effects of the binding of biliverdin (BV), a tetrapyrrole linear chromophore, on the stability
of BLG under pressure, by combining in situ HP small-angle neutron scattering (SANS) and HP-UV absorption spectroscopy.
Although BV induces a slight destabilization of BLG during HP-induced unfolding, a ligand excess strongly prevents BLG oligomerization.
Moreover, at SANS resolution, an excess of BV induces the complete recovery of the protein ‘‘native’’ 3D structure
after HP removal, despite the presence of the BV covalently bound adduct. Mass spectrometry highlights the crucial role of
cysteine residues in the competitive and protective effects of BV during pressure denaturation of BLG through SH/S-S
exchange.",
publisher = "Biophysical Society",
journal = "Biophysical Journal",
title = "Structure of proteins under pressure: Covalent binding effects of biliverdin on b-lactoglobulin",
volume = "121",
pages = "1-12",
doi = "10.1016/j.bpj.2022.06.003"
}

Minić, S. L., Annighofer, B., Helary, A., Sago, L., Cornu, D., Brulet, A.,& Combet, S.. (2022). Structure of proteins under pressure: Covalent binding effects of biliverdin on b-lactoglobulin. in Biophysical Journal
Biophysical Society., 121, 1-12.
https://doi.org/10.1016/j.bpj.2022.06.003

Minić SL, Annighofer B, Helary A, Sago L, Cornu D, Brulet A, Combet S. Structure of proteins under pressure: Covalent binding effects of biliverdin on b-lactoglobulin. in Biophysical Journal. 2022;121:1-12.
doi:10.1016/j.bpj.2022.06.003 .

Minić, Simeon L., Annighofer, Burkhard, Helary, Arnaud, Sago, Laıla, Cornu, David, Brulet, Annie, Combet, Sophie, "Structure of proteins under pressure: Covalent binding effects of biliverdin on b-lactoglobulin" in Biophysical Journal, 121 (2022):1-12,
https://doi.org/10.1016/j.bpj.2022.06.003 . .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Nikolić, Milan
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6032
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  - Belgrade : Faculty of Chemistry
C3  - FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts
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_cherry_6032
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. 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 = "Belgrade : Faculty of Chemistry",
journal = "FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts",
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_cherry_6032"
}

Radomirović, M. Ž., 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”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts
Belgrade : Faculty of Chemistry., 37-37.
https://hdl.handle.net/21.15107/rcub_cherry_6032

Radomirović MŽ, 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”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts. 2021;:37-37.
https://hdl.handle.net/21.15107/rcub_cherry_6032 .

Radomirović, Mirjana Ž., 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”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts (2021):37-37,
https://hdl.handle.net/21.15107/rcub_cherry_6032 .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Minić, Simeon
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6035
AB  - Background: β-lactoglobulin (BLG) is the major whey protein with many techno-functional properties desirable for the food industry. Phycocyanobilin (PCB), the bioactive pigment of Arthrospira platensis, is able to covalently bind to BLG via free cysteine residue under physiologically relevant conditions, resulting in subtle changes in BLG’s tertiary structure. This work sought to investigate the effects of BLG covalent modification by PCB on protein’s pepsin and pancreatin in vitro digestibility and IgE binding capacity, the properties that could significantly affect its usage in the food industry.
Methods: BLG-PCB covalent adduct was obtained at pH 7.2 and 37 ˚C. Pepsin and pancreatin digestibility of BLG-PCB was assessed using in vitro digestion models and compared to unmodified protein. Protein digestion was monitored by SDS-PAGE. IgE binding properties of BLG and BLG-PCB were investigated using Western blot and inhibitory Enzyme-Linked Immunosorbent Assay.
Results: Covalent BLG-PCB adduct is more resistant to digestion by both pepsin and pancreatin. Covalent modification prolongs BLG’s gastric and intestinal half-life, without increasing its IgE-binding capacity.
Conclusion: Higher resistance to pepsin and pancreatin digestion without increased IgE-binding capacity makes phycocyanobilin-modified β-lactoglobulin a promising ingredient in the food industry that could serve as a vehicle for prolonged delivery of bioactive PCB.
PB  - COST Infogest
C3  - Virtual International Conference on Food Digestion, On-line event, 6th-7th May, 2021. In: Book of Abstracts
T1  - Phycocyanobilin-modified β-lactoglobulin is more resistant to pepsin and pancreatin digestion
SP  - 14
EP  - 14
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6035
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Minić, Simeon and Stanić-Vučinić, Dragana and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Background: β-lactoglobulin (BLG) is the major whey protein with many techno-functional properties desirable for the food industry. Phycocyanobilin (PCB), the bioactive pigment of Arthrospira platensis, is able to covalently bind to BLG via free cysteine residue under physiologically relevant conditions, resulting in subtle changes in BLG’s tertiary structure. This work sought to investigate the effects of BLG covalent modification by PCB on protein’s pepsin and pancreatin in vitro digestibility and IgE binding capacity, the properties that could significantly affect its usage in the food industry.
Methods: BLG-PCB covalent adduct was obtained at pH 7.2 and 37 ˚C. Pepsin and pancreatin digestibility of BLG-PCB was assessed using in vitro digestion models and compared to unmodified protein. Protein digestion was monitored by SDS-PAGE. IgE binding properties of BLG and BLG-PCB were investigated using Western blot and inhibitory Enzyme-Linked Immunosorbent Assay.
Results: Covalent BLG-PCB adduct is more resistant to digestion by both pepsin and pancreatin. Covalent modification prolongs BLG’s gastric and intestinal half-life, without increasing its IgE-binding capacity.
Conclusion: Higher resistance to pepsin and pancreatin digestion without increased IgE-binding capacity makes phycocyanobilin-modified β-lactoglobulin a promising ingredient in the food industry that could serve as a vehicle for prolonged delivery of bioactive PCB.",
publisher = "COST Infogest",
journal = "Virtual International Conference on Food Digestion, On-line event, 6th-7th May, 2021. In: Book of Abstracts",
title = "Phycocyanobilin-modified β-lactoglobulin is more resistant to pepsin and pancreatin digestion",
pages = "14-14",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6035"
}

Radomirović, M. Ž., Minić, S., Stanić-Vučinić, D., Nikolić, M.,& Ćirković-Veličković, T.. (2021). Phycocyanobilin-modified β-lactoglobulin is more resistant to pepsin and pancreatin digestion. in Virtual International Conference on Food Digestion, On-line event, 6th-7th May, 2021. In: Book of Abstracts
COST Infogest., 14-14.
https://hdl.handle.net/21.15107/rcub_cherry_6035

Radomirović MŽ, Minić S, Stanić-Vučinić D, Nikolić M, Ćirković-Veličković T. Phycocyanobilin-modified β-lactoglobulin is more resistant to pepsin and pancreatin digestion. in Virtual International Conference on Food Digestion, On-line event, 6th-7th May, 2021. In: Book of Abstracts. 2021;:14-14.
https://hdl.handle.net/21.15107/rcub_cherry_6035 .

Radomirović, Mirjana Ž., Minić, Simeon, Stanić-Vučinić, Dragana, Nikolić, Milan, Ćirković-Veličković, Tanja, "Phycocyanobilin-modified β-lactoglobulin is more resistant to pepsin and pancreatin digestion" in Virtual International Conference on Food Digestion, On-line event, 6th-7th May, 2021. In: Book of Abstracts (2021):14-14,
https://hdl.handle.net/21.15107/rcub_cherry_6035 .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Nikolić, Milan
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6039
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  - Beograd : Srpsko hemijsko društvo
C3  - 57th Meeting of the Serbian Chemical Society, Kragujevac, Serbia, 18th-19th June, 2021. In: Book of Abstracts and Proceedings
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_cherry_6039
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. 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 = "Beograd : Srpsko hemijsko društvo",
journal = "57th Meeting of the Serbian Chemical Society, Kragujevac, Serbia, 18th-19th June, 2021. In: Book of Abstracts and Proceedings",
title = "Fluorescent labeling of bovine serum albumin with phycocyanobilin using Traut’s reagent",
pages = "71-71",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6039"
}

Radomirović, M. Ž., 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 57th Meeting of the Serbian Chemical Society, Kragujevac, Serbia, 18th-19th June, 2021. In: Book of Abstracts and Proceedings
Beograd : Srpsko hemijsko društvo., 71-71.
https://hdl.handle.net/21.15107/rcub_cherry_6039

Radomirović MŽ, 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 57th Meeting of the Serbian Chemical Society, Kragujevac, Serbia, 18th-19th June, 2021. In: Book of Abstracts and Proceedings. 2021;:71-71.
https://hdl.handle.net/21.15107/rcub_cherry_6039 .

Radomirović, Mirjana Ž., 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 57th Meeting of the Serbian Chemical Society, Kragujevac, Serbia, 18th-19th June, 2021. In: Book of Abstracts and Proceedings (2021):71-71,
https://hdl.handle.net/21.15107/rcub_cherry_6039 .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Minić, Simeon
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6030
AB  - β-lactoglobulin (BLG) is the major milk allergen with many techno-functional properties desirable for the food industry. Our previous study demonstrated that phycocyanobilin (PCB), the bioactive pigment of Spirulina platensis with many health-promoting effects, covalently binds to BLG at physiological pH via free cysteine residue. To help produce hypoallergenic food, this study explored the possibility of reducing the allergenicity, while at the same time improving the techno-functional properties of BLG. Antioxidant properties, heat-induced changes, pepsin and pancreatin digestibility and IgE binding properties of BLG-PCB covalent adduct were investigated and compared to unmodified protein. BLG-PCB possesses enhanced antioxidative properties, while also being protected by PCB against free-radical induced oxidation. Although thermally as stable as unmodified protein, BLG-PCB is less susceptible to heat-induced oligomerization and aggregation under moderate heat treatment (63 ˚C, 30 min). The surface hydrophobicity of BLG-PCB is lower than that of BLG and, contrary to unmodified BLG, it does not change upon heating.
The heating of BLG-PCB decreases its β-sheet content, making it less prone to the formation of amyloid-like structures. Covalently modified protein is more resistant to pepsin and pancreatin digestion in comparison to unmodified protein. Enzyme-linked immunosorbent assay indicated that covalent modification by PCB is effective in reducing the IgE-binding capacity of BLG. Taken together, these results indicate that BLG covalent modification by PCB improves BLG’s techno-functional properties, without increasing its IgE binding abilities, thus making it a useful ingredient in the food industry.
C3  - The 45th FEBS Congress, Virtual Congress, 3rd-8th July, 2021. In: FEBS Open Bio
T1  - β-lactoglobulin covalent modification by phycocyanobilin: Effect on protein’s techno-functional and IgE binding properties
VL  - 11
IS  - Suppl. 1
SP  - 196
EP  - 197
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6030
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Minić, Simeon and Stanić-Vučinić, Dragana and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "β-lactoglobulin (BLG) is the major milk allergen with many techno-functional properties desirable for the food industry. Our previous study demonstrated that phycocyanobilin (PCB), the bioactive pigment of Spirulina platensis with many health-promoting effects, covalently binds to BLG at physiological pH via free cysteine residue. To help produce hypoallergenic food, this study explored the possibility of reducing the allergenicity, while at the same time improving the techno-functional properties of BLG. Antioxidant properties, heat-induced changes, pepsin and pancreatin digestibility and IgE binding properties of BLG-PCB covalent adduct were investigated and compared to unmodified protein. BLG-PCB possesses enhanced antioxidative properties, while also being protected by PCB against free-radical induced oxidation. Although thermally as stable as unmodified protein, BLG-PCB is less susceptible to heat-induced oligomerization and aggregation under moderate heat treatment (63 ˚C, 30 min). The surface hydrophobicity of BLG-PCB is lower than that of BLG and, contrary to unmodified BLG, it does not change upon heating.
The heating of BLG-PCB decreases its β-sheet content, making it less prone to the formation of amyloid-like structures. Covalently modified protein is more resistant to pepsin and pancreatin digestion in comparison to unmodified protein. Enzyme-linked immunosorbent assay indicated that covalent modification by PCB is effective in reducing the IgE-binding capacity of BLG. Taken together, these results indicate that BLG covalent modification by PCB improves BLG’s techno-functional properties, without increasing its IgE binding abilities, thus making it a useful ingredient in the food industry.",
journal = "The 45th FEBS Congress, Virtual Congress, 3rd-8th July, 2021. In: FEBS Open Bio",
title = "β-lactoglobulin covalent modification by phycocyanobilin: Effect on protein’s techno-functional and IgE binding properties",
volume = "11",
number = "Suppl. 1",
pages = "196-197",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6030"
}

Radomirović, M. Ž., Minić, S., Stanić-Vučinić, D., Nikolić, M.,& Ćirković-Veličković, T.. (2021). β-lactoglobulin covalent modification by phycocyanobilin: Effect on protein’s techno-functional and IgE binding properties. in The 45th FEBS Congress, Virtual Congress, 3rd-8th July, 2021. In: FEBS Open Bio, 11(Suppl. 1), 196-197.
https://hdl.handle.net/21.15107/rcub_cherry_6030

Radomirović MŽ, Minić S, Stanić-Vučinić D, Nikolić M, Ćirković-Veličković T. β-lactoglobulin covalent modification by phycocyanobilin: Effect on protein’s techno-functional and IgE binding properties. in The 45th FEBS Congress, Virtual Congress, 3rd-8th July, 2021. In: FEBS Open Bio. 2021;11(Suppl. 1):196-197.
https://hdl.handle.net/21.15107/rcub_cherry_6030 .

Radomirović, Mirjana Ž., Minić, Simeon, Stanić-Vučinić, Dragana, Nikolić, Milan, Ćirković-Veličković, Tanja, "β-lactoglobulin covalent modification by phycocyanobilin: Effect on protein’s techno-functional and IgE binding properties" in The 45th FEBS Congress, Virtual Congress, 3rd-8th July, 2021. In: FEBS Open Bio, 11, no. Suppl. 1 (2021):196-197,
https://hdl.handle.net/21.15107/rcub_cherry_6030 .

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  - JOUR
AU  - Gligorijević, Nikola
AU  - Šukalović, Vladimir
AU  - Minić, Simeon L.
AU  - Miljuš, Goran
AU  - Nedić, Olgica
AU  - Penezić, Ana Z.
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4667
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.
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
VL  - 86
IS  - 9
SP  - 795
EP  - 807
DO  - 10.2298/JSC210420041G
ER  - 

@article{
author = "Gligorijević, Nikola and Šukalović, Vladimir and Minić, Simeon L. and Miljuš, Goran and Nedić, Olgica and Penezić, Ana Z.",
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.",
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",
volume = "86",
number = "9",
pages = "795-807",
doi = "10.2298/JSC210420041G"
}

Gligorijević, N., Šukalović, V., Minić, S. L., Miljuš, G., Nedić, O.,& Penezić, A. Z.. (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 SL, Miljuš G, Nedić O, Penezić AZ. 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 L., Miljuš, Goran, Nedić, Olgica, Penezić, Ana Z., "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  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Lević, Steva M.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
AU  - Nedić, Olgica
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4862
AB  - Fibrinogen is a plasma protein that is highly susceptible to oxidation. Because of this chemical modification, fibrinogen acquires thrombogenic characteristics under 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  - University of Novi Sad - Faculty of Sciences, Department of Biology
T2  - Biologia Serbica
T1  - Ligand binding to fibrinogen influences its structure and function
VL  - 43
IS  - 1
DO  - 10.5281/zenodo.5512285
ER  - 

@article{
author = "Gligorijević, Nikola and Minić, Simeon L. and Radomirović, Mirjana Ž. and Lević, Steva M. and Nikolić, Milan and Ćirković-Veličković, Tanja and Nedić, Olgica",
year = "2021",
abstract = "Fibrinogen is a plasma protein that is highly susceptible to oxidation. Because of this chemical modification, fibrinogen acquires thrombogenic characteristics under 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 = "University of Novi Sad - Faculty of Sciences, Department of Biology",
journal = "Biologia Serbica",
title = "Ligand binding to fibrinogen influences its structure and function",
volume = "43",
number = "1",
doi = "10.5281/zenodo.5512285"
}

Gligorijević, N., Minić, S. L., Radomirović, M. Ž., Lević, S. M., Nikolić, M., Ćirković-Veličković, T.,& Nedić, O.. (2021). Ligand binding to fibrinogen influences its structure and function. in Biologia Serbica
University of Novi Sad - Faculty of Sciences, Department of Biology., 43(1).
https://doi.org/10.5281/zenodo.5512285

Gligorijević N, Minić SL, Radomirović MŽ, Lević SM, Nikolić M, Ćirković-Veličković T, Nedić O. Ligand binding to fibrinogen influences its structure and function. in Biologia Serbica. 2021;43(1).
doi:10.5281/zenodo.5512285 .

Gligorijević, Nikola, Minić, Simeon L., Radomirović, Mirjana Ž., Lević, Steva M., Nikolić, Milan, Ćirković-Veličković, Tanja, Nedić, Olgica, "Ligand binding to fibrinogen influences its structure and function" in Biologia Serbica, 43, no. 1 (2021),
https://doi.org/10.5281/zenodo.5512285 . .

TY  - CHAP
AU  - Nikolić, Milan
AU  - Minić, Simeon L.
AU  - Mačvanin, Mirjana T.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
AU  - Jacob-Lopes, Eduardo
AU  - Queiroz, Maria Isabel
AU  - Zepka, Leila Queiroz
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4893
AB  - The aim of this chapter is to review and discuss methodology and protocols in the analysis of phycobiliproteins (phycocyanins, allophycocyanins, and phycoerythrins) and their chromophores. Due to the presence of multiple covalently bound open-chain tetrapyrrole chromophores, phycobiliproteins are colored and strongly fluorescent molecules, with high absorption coefficients (105 to 106) and excellent fluorescent quantum yield (0.51 up to 0.98). Therefore, a vast number of methods for phycobiliproteins analysis is based on these spectral characteristics, whereas assessment of their bioactivity is related to their exceptional redox and metal-chelating properties. This chapter is dedicated to methods used for isolation and purification, structure analysis, physicochemical properties and stability characterization, quantification, as well as in vitro and in vivo biological activities evaluation. In addition, emerging approaches related to phycobiliproteins analysis are also reviewed including interactions with other biomolecules and ions and identification of phycobiliprotein (chromo)peptides by mass spectrometry.
PB  - Springer International Publishing
T2  - Pigments from Microalgae Handbook
T1  - Analytical Protocols in Phycobiliproteins Analysis
SP  - 179
EP  - 201
DO  - 10.1007/978-3-030-50971-2_8
ER  - 

@inbook{
author = "Nikolić, Milan and Minić, Simeon L. and Mačvanin, Mirjana T. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja and Jacob-Lopes, Eduardo and Queiroz, Maria Isabel and Zepka, Leila Queiroz",
year = "2020",
abstract = "The aim of this chapter is to review and discuss methodology and protocols in the analysis of phycobiliproteins (phycocyanins, allophycocyanins, and phycoerythrins) and their chromophores. Due to the presence of multiple covalently bound open-chain tetrapyrrole chromophores, phycobiliproteins are colored and strongly fluorescent molecules, with high absorption coefficients (105 to 106) and excellent fluorescent quantum yield (0.51 up to 0.98). Therefore, a vast number of methods for phycobiliproteins analysis is based on these spectral characteristics, whereas assessment of their bioactivity is related to their exceptional redox and metal-chelating properties. This chapter is dedicated to methods used for isolation and purification, structure analysis, physicochemical properties and stability characterization, quantification, as well as in vitro and in vivo biological activities evaluation. In addition, emerging approaches related to phycobiliproteins analysis are also reviewed including interactions with other biomolecules and ions and identification of phycobiliprotein (chromo)peptides by mass spectrometry.",
publisher = "Springer International Publishing",
journal = "Pigments from Microalgae Handbook",
booktitle = "Analytical Protocols in Phycobiliproteins Analysis",
pages = "179-201",
doi = "10.1007/978-3-030-50971-2_8"
}

Nikolić, M., Minić, S. L., Mačvanin, M. T., Stanić-Vučinić, D., Ćirković-Veličković, T., Jacob-Lopes, E., Queiroz, M. I.,& Zepka, L. Q.. (2020). Analytical Protocols in Phycobiliproteins Analysis. in Pigments from Microalgae Handbook
Springer International Publishing., 179-201.
https://doi.org/10.1007/978-3-030-50971-2_8

Nikolić M, Minić SL, Mačvanin MT, Stanić-Vučinić D, Ćirković-Veličković T, Jacob-Lopes E, Queiroz MI, Zepka LQ. Analytical Protocols in Phycobiliproteins Analysis. in Pigments from Microalgae Handbook. 2020;:179-201.
doi:10.1007/978-3-030-50971-2_8 .

Nikolić, Milan, Minić, Simeon L., Mačvanin, Mirjana T., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, Jacob-Lopes, Eduardo, Queiroz, Maria Isabel, Zepka, Leila Queiroz, "Analytical Protocols in Phycobiliproteins Analysis" in Pigments from Microalgae Handbook (2020):179-201,
https://doi.org/10.1007/978-3-030-50971-2_8 . .

TY  - CHAP
AU  - Nikolić, Milan
AU  - Minić, Simeon L.
AU  - Mačvanin, Mirjana T.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
AU  - Jacob-Lopes, Eduardo
AU  - Queiroz, Maria Isabel
AU  - Zepka, Leila Queiroz
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4892
AB  - The aim of this chapter is to review and discuss methodology and protocols in the analysis of phycobiliproteins (phycocyanins, allophycocyanins, and phycoerythrins) and their chromophores. Due to the presence of multiple covalently bound open-chain tetrapyrrole chromophores, phycobiliproteins are colored and strongly fluorescent molecules, with high absorption coefficients (105 to 106) and excellent fluorescent quantum yield (0.51 up to 0.98). Therefore, a vast number of methods for phycobiliproteins analysis is based on these spectral characteristics, whereas assessment of their bioactivity is related to their exceptional redox and metal-chelating properties. This chapter is dedicated to methods used for isolation and purification, structure analysis, physicochemical properties and stability characterization, quantification, as well as in vitro and in vivo biological activities evaluation. In addition, emerging approaches related to phycobiliproteins analysis are also reviewed including interactions with other biomolecules and ions and identification of phycobiliprotein (chromo)peptides by mass spectrometry.
PB  - Springer International Publishing
T2  - Pigments from Microalgae Handbook
T1  - Analytical Protocols in Phycobiliproteins Analysis
SP  - 179
EP  - 201
DO  - 10.1007/978-3-030-50971-2_8
ER  - 

@inbook{
author = "Nikolić, Milan and Minić, Simeon L. and Mačvanin, Mirjana T. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja and Jacob-Lopes, Eduardo and Queiroz, Maria Isabel and Zepka, Leila Queiroz",
year = "2020",
abstract = "The aim of this chapter is to review and discuss methodology and protocols in the analysis of phycobiliproteins (phycocyanins, allophycocyanins, and phycoerythrins) and their chromophores. Due to the presence of multiple covalently bound open-chain tetrapyrrole chromophores, phycobiliproteins are colored and strongly fluorescent molecules, with high absorption coefficients (105 to 106) and excellent fluorescent quantum yield (0.51 up to 0.98). Therefore, a vast number of methods for phycobiliproteins analysis is based on these spectral characteristics, whereas assessment of their bioactivity is related to their exceptional redox and metal-chelating properties. This chapter is dedicated to methods used for isolation and purification, structure analysis, physicochemical properties and stability characterization, quantification, as well as in vitro and in vivo biological activities evaluation. In addition, emerging approaches related to phycobiliproteins analysis are also reviewed including interactions with other biomolecules and ions and identification of phycobiliprotein (chromo)peptides by mass spectrometry.",
publisher = "Springer International Publishing",
journal = "Pigments from Microalgae Handbook",
booktitle = "Analytical Protocols in Phycobiliproteins Analysis",
pages = "179-201",
doi = "10.1007/978-3-030-50971-2_8"
}

Nikolić, M., Minić, S. L., Mačvanin, M. T., Stanić-Vučinić, D., Ćirković-Veličković, T., Jacob-Lopes, E., Queiroz, M. I.,& Zepka, L. Q.. (2020). Analytical Protocols in Phycobiliproteins Analysis. in Pigments from Microalgae Handbook
Springer International Publishing., 179-201.
https://doi.org/10.1007/978-3-030-50971-2_8

Nikolić M, Minić SL, Mačvanin MT, Stanić-Vučinić D, Ćirković-Veličković T, Jacob-Lopes E, Queiroz MI, Zepka LQ. Analytical Protocols in Phycobiliproteins Analysis. in Pigments from Microalgae Handbook. 2020;:179-201.
doi:10.1007/978-3-030-50971-2_8 .

Nikolić, Milan, Minić, Simeon L., Mačvanin, Mirjana T., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, Jacob-Lopes, Eduardo, Queiroz, Maria Isabel, Zepka, Leila Queiroz, "Analytical Protocols in Phycobiliproteins Analysis" in Pigments from Microalgae Handbook (2020):179-201,
https://doi.org/10.1007/978-3-030-50971-2_8 . .

TY  - JOUR
AU  - Radibratović, Milica
AU  - Al-Hanish, Ayah
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3733
AB  - α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. 

EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.
PB  - Elsevier
T2  - Food Chemistry
T1  - Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study
VL  - 278
SP  - 388
EP  - 395
DO  - 10.1016/j.foodchem.2018.11.038
ER  - 

@article{
author = "Radibratović, Milica and Al-Hanish, Ayah and Minić, Simeon L. and Radomirović, Mirjana Ž. and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. 

EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study",
volume = "278",
pages = "388-395",
doi = "10.1016/j.foodchem.2018.11.038"
}

Radibratović, M., Al-Hanish, A., Minić, S. L., Radomirović, M. Ž., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2019). Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. in Food Chemistry
Elsevier., 278, 388-395.
https://doi.org/10.1016/j.foodchem.2018.11.038

Radibratović M, Al-Hanish A, Minić SL, Radomirović MŽ, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. in Food Chemistry. 2019;278:388-395.
doi:10.1016/j.foodchem.2018.11.038 .

Radibratović, Milica, Al-Hanish, Ayah, Minić, Simeon L., Radomirović, Mirjana Ž., Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study" in Food Chemistry, 278 (2019):388-395,
https://doi.org/10.1016/j.foodchem.2018.11.038 . .

TY  - JOUR
AU  - Radibratović, Milica
AU  - Al-Hanish, Ayah
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4848
AB  - α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.
PB  - Elsevier
T2  - Food Chemistry
T1  - Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study
VL  - 278
SP  - 388
EP  - 395
DO  - 10.1016/j.foodchem.2018.11.038
ER  - 

@article{
author = "Radibratović, Milica and Al-Hanish, Ayah and Minić, Simeon L. and Radomirović, Mirjana Ž. and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study",
volume = "278",
pages = "388-395",
doi = "10.1016/j.foodchem.2018.11.038"
}

Radibratović, M., Al-Hanish, A., Minić, S. L., Radomirović, M. Ž., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2019). Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. in Food Chemistry
Elsevier., 278, 388-395.
https://doi.org/10.1016/j.foodchem.2018.11.038

Radibratović M, Al-Hanish A, Minić SL, Radomirović MŽ, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. in Food Chemistry. 2019;278:388-395.
doi:10.1016/j.foodchem.2018.11.038 .

Radibratović, Milica, Al-Hanish, Ayah, Minić, Simeon L., Radomirović, Mirjana Ž., Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study" in Food Chemistry, 278 (2019):388-395,
https://doi.org/10.1016/j.foodchem.2018.11.038 . .