TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Radomirović, Mirjana Ž.
AU  - Simović, Ana
AU  - Radibratović, Milica
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5555
AB  - Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.
PB  - Bentham Science
T2  - Current Analytical Chemistry
T1  - Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk
VL  - 18
IS  - 3
SP  - 341
EP  - 359
DO  - 10.2174/1573411017666210108092338
ER  - 

@article{
author = "Radosavljević, Jelena and Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Radomirović, Mirjana Ž. and Simović, Ana and Radibratović, Milica and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.",
publisher = "Bentham Science",
journal = "Current Analytical Chemistry",
title = "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk",
volume = "18",
number = "3",
pages = "341-359",
doi = "10.2174/1573411017666210108092338"
}

Radosavljević, J., Stanić-Vučinić, D., Stojadinović, M. M., Radomirović, M. Ž., Simović, A., Radibratović, M.,& Ćirković-Veličković, T.. (2022). Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry
Bentham Science., 18(3), 341-359.
https://doi.org/10.2174/1573411017666210108092338

Radosavljević J, Stanić-Vučinić D, Stojadinović MM, Radomirović MŽ, Simović A, Radibratović M, Ćirković-Veličković T. Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry. 2022;18(3):341-359.
doi:10.2174/1573411017666210108092338 .

Radosavljević, Jelena, Stanić-Vučinić, Dragana, Stojadinović, Marija M., Radomirović, Mirjana Ž., Simović, Ana, Radibratović, Milica, Ćirković-Veličković, Tanja, "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk" in Current Analytical Chemistry, 18, no. 3 (2022):341-359,
https://doi.org/10.2174/1573411017666210108092338 . .

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Radomirović, Mirjana Ž.
AU  - Simović, Ana
AU  - Radibratović, Milica
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5556
AB  - Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.
PB  - Bentham Science
T2  - Current Analytical Chemistry
T1  - Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk
VL  - 18
IS  - 3
SP  - 341
EP  - 359
DO  - 10.2174/1573411017666210108092338
ER  - 

@article{
author = "Radosavljević, Jelena and Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Radomirović, Mirjana Ž. and Simović, Ana and Radibratović, Milica and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.",
publisher = "Bentham Science",
journal = "Current Analytical Chemistry",
title = "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk",
volume = "18",
number = "3",
pages = "341-359",
doi = "10.2174/1573411017666210108092338"
}

Radosavljević, J., Stanić-Vučinić, D., Stojadinović, M. M., Radomirović, M. Ž., Simović, A., Radibratović, M.,& Ćirković-Veličković, T.. (2022). Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry
Bentham Science., 18(3), 341-359.
https://doi.org/10.2174/1573411017666210108092338

Radosavljević J, Stanić-Vučinić D, Stojadinović MM, Radomirović MŽ, Simović A, Radibratović M, Ćirković-Veličković T. Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry. 2022;18(3):341-359.
doi:10.2174/1573411017666210108092338 .

Radosavljević, Jelena, Stanić-Vučinić, Dragana, Stojadinović, Marija M., Radomirović, Mirjana Ž., Simović, Ana, Radibratović, Milica, Ćirković-Veličković, Tanja, "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk" in Current Analytical Chemistry, 18, no. 3 (2022):341-359,
https://doi.org/10.2174/1573411017666210108092338 . .

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Radomirović, Mirjana
AU  - Lević, Steva M.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
AU  - Nedić, Olgica
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7288
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
SP  - 24
EP  - 31
DO  - 10.5281/zenodo.5512285
ER  - 

@article{
author = "Gligorijević, Nikola and Minić, Simeon and Radomirović, Mirjana 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",
pages = "24-31",
doi = "10.5281/zenodo.5512285"
}

Gligorijević, N., Minić, S., Radomirović, M., 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), 24-31.
https://doi.org/10.5281/zenodo.5512285

Gligorijević N, Minić S, Radomirović M, Lević SM, Nikolić M, Ćirković-Veličković T, Nedić O. Ligand binding to fibrinogen influences its structure and function. in Biologia Serbica. 2021;43(1):24-31.
doi:10.5281/zenodo.5512285 .

Gligorijević, Nikola, Minić, Simeon, Radomirović, Mirjana, 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):24-31,
https://doi.org/10.5281/zenodo.5512285 . .

TY  - CONF
AU  - Radomirović, Mirjana
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Rajković, Andreja
AU  - Ćirković Veličković, Tanja
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7280
AB  - Food allergies affect up to 10% of the general population and represent an important health problem in the field of
food safety in industrialized countries. Hence, developing reliable, specific, and sensitive methods for detecting and
quantifying allergens in food products is of high importance. Shellfish have been recognized as one of the eight
most common sources of allergens, with tropomyosin (TPM) being considered a major heat-stable allergen, having
a highly conserved amino acid sequence among different shellfish species. Allergenicity of TPM may change during
food processing, such as cooking. The objective of this study was to develop an enzyme-linked immunosorbent
assay (ELISA) for the detection and quantification of shellfish tropomyosin in food samples.
Two different extraction buffers - phosphate-buffered saline (PBS) and PBS containing 1 M sodium-chloride
(PBSN), were compared for their ability to recover proteins from pre-cooked frozen Mediterranean mussel (Mytilus
galloprovincialis) and fresh frozen razor mud shrimp (Solenocera melantho). The samples were additionally cooked
according to the manufacturer's instruction and analyzed as such. The protein content was quantified using Bradford
protein assay, and the protein components of soluble extracts were profiled using SDS-PAGE. TPM presence was
confirmed using Western blot. Sandwich ELISA was developed using a monoclonal anti-TPM antibody as a capture
antibody, while polyclonal anti-TPM antibody served as a detection antibody and was coupled to the biotinylated
secondary antibody and streptavidin-alkaline phosphatase conjugate. Tropomyosin was quantified using highly
purified natural shrimp tropomyosin as standard.
The profile of extracted proteins was changed when using PBSN instead of PBS. A higher concentration of proteins
was recovered from raw shrimp using PBSN instead of PBS. At the same time, the type of extraction buffer did not
affect protein recovery either from heated shrimp or pre-cooked/heated mussels. Significantly fewer proteins were
extracted from cooked shrimp sample compared to the raw shrimp, while cooking showed no effect on the extraction
of proteins from mussels. Cooking did not affect TPM recognition in Western blot. TPM was quantified in shrimp
samples in sandwich ELISA. However, developed ELISA could not quantify mussel's TPM, indicating that this
approach may distinguish mussels and shrimp TPM.
PB  - Sociedade Portuguesa de Química
C3  - Book of Abstracts - XXI EuroFoodChem conference, 22nd-24th November, 2021, Virtual Congress
T1  - Extraction and quantification of tropomyosin in selected samples of shellfish
SP  - 118
EP  - 118
UR  - https://hdl.handle.net/21.15107/rcub_cer_7280
ER  - 

@conference{
author = "Radomirović, Mirjana and Gligorijević, Nikola and Stanić-Vučinić, Dragana and Rajković, Andreja and Ćirković Veličković, Tanja",
year = "2021",
abstract = "Food allergies affect up to 10% of the general population and represent an important health problem in the field of
food safety in industrialized countries. Hence, developing reliable, specific, and sensitive methods for detecting and
quantifying allergens in food products is of high importance. Shellfish have been recognized as one of the eight
most common sources of allergens, with tropomyosin (TPM) being considered a major heat-stable allergen, having
a highly conserved amino acid sequence among different shellfish species. Allergenicity of TPM may change during
food processing, such as cooking. The objective of this study was to develop an enzyme-linked immunosorbent
assay (ELISA) for the detection and quantification of shellfish tropomyosin in food samples.
Two different extraction buffers - phosphate-buffered saline (PBS) and PBS containing 1 M sodium-chloride
(PBSN), were compared for their ability to recover proteins from pre-cooked frozen Mediterranean mussel (Mytilus
galloprovincialis) and fresh frozen razor mud shrimp (Solenocera melantho). The samples were additionally cooked
according to the manufacturer's instruction and analyzed as such. The protein content was quantified using Bradford
protein assay, and the protein components of soluble extracts were profiled using SDS-PAGE. TPM presence was
confirmed using Western blot. Sandwich ELISA was developed using a monoclonal anti-TPM antibody as a capture
antibody, while polyclonal anti-TPM antibody served as a detection antibody and was coupled to the biotinylated
secondary antibody and streptavidin-alkaline phosphatase conjugate. Tropomyosin was quantified using highly
purified natural shrimp tropomyosin as standard.
The profile of extracted proteins was changed when using PBSN instead of PBS. A higher concentration of proteins
was recovered from raw shrimp using PBSN instead of PBS. At the same time, the type of extraction buffer did not
affect protein recovery either from heated shrimp or pre-cooked/heated mussels. Significantly fewer proteins were
extracted from cooked shrimp sample compared to the raw shrimp, while cooking showed no effect on the extraction
of proteins from mussels. Cooking did not affect TPM recognition in Western blot. TPM was quantified in shrimp
samples in sandwich ELISA. However, developed ELISA could not quantify mussel's TPM, indicating that this
approach may distinguish mussels and shrimp TPM.",
publisher = "Sociedade Portuguesa de Química",
journal = "Book of Abstracts - XXI EuroFoodChem conference, 22nd-24th November, 2021, Virtual Congress",
title = "Extraction and quantification of tropomyosin in selected samples of shellfish",
pages = "118-118",
url = "https://hdl.handle.net/21.15107/rcub_cer_7280"
}

Radomirović, M., Gligorijević, N., Stanić-Vučinić, D., Rajković, A.,& Ćirković Veličković, T.. (2021). Extraction and quantification of tropomyosin in selected samples of shellfish. in Book of Abstracts - XXI EuroFoodChem conference, 22nd-24th November, 2021, Virtual Congress
Sociedade Portuguesa de Química., 118-118.
https://hdl.handle.net/21.15107/rcub_cer_7280

Radomirović M, Gligorijević N, Stanić-Vučinić D, Rajković A, Ćirković Veličković T. Extraction and quantification of tropomyosin in selected samples of shellfish. in Book of Abstracts - XXI EuroFoodChem conference, 22nd-24th November, 2021, Virtual Congress. 2021;:118-118.
https://hdl.handle.net/21.15107/rcub_cer_7280 .

Radomirović, Mirjana, Gligorijević, Nikola, Stanić-Vučinić, Dragana, Rajković, Andreja, Ćirković Veličković, Tanja, "Extraction and quantification of tropomyosin in selected samples of shellfish" in Book of Abstracts - XXI EuroFoodChem conference, 22nd-24th November, 2021, Virtual Congress (2021):118-118,
https://hdl.handle.net/21.15107/rcub_cer_7280 .

TY  - CONF
AU  - Mutić, Tamara
AU  - Gligorijević, Nikola
AU  - Ćirković Veličković, Tanja
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7281
AB  - Microplastics are plastic fibers, particles or films with diameters smaller than 5 mm and they have shown different
effects on proteins [1]. Microplastics (MPs) are small in size, have low densities, can exist in the atmosphere for a
long time and can easily be spread by wind [2]. The objective of this study was to investigate adsorption affinity of
different types of MPs (polyethylene terephthalate (PET), polystyrene (PS) and polyvinyl chloride (PVC)) with
ovalbumin. In this study ovalbumin, isolated from chicken egg white, was used. Plastics were mixed with ovalbumin
for 1,2,4 and 19 h and then the absorbance of the remaining protein in the solution was measured at 280nm. In
addition, Langmuir isotherm mathematical model to calculate the adsorption affinity of ovalbumin for MPs was used.
We determined affinity constants by using Langmuir isotherm models for different particle size (PS 120 μm and PS
500 μm), different types of plastics (PET, PS and PVC) and pH values (3 and 7,2). Adsorption experiment results
showed that adsorption depends on type of plastics. Our results showed that PVC did not adsorb ovalbumin,
however, PET and PS have interacted with protein. Adsorption capacities of all analysed MPs increase with pH of
solution. Under different pH values, MPs and protein have different charges that may affect adsorption
characteristics. With increase of pH from 3 to 7, the affinity for protein adsorption increased 1.4 times for PS (smaller
in size) while for PS (bigger size) and PET protein affinity was two times higher at pH 3.
PB  - Sociedade Portuguesa de Química
C3  - Book of Abstracts - XXI EuroFoodChem conference, 22nd-24th November, 2021, Virtual Congress
T1  - Binding affinity ovalbumin on different type of microplastics using Langmuir isotherm
SP  - 178
EP  - 178
UR  - https://hdl.handle.net/21.15107/rcub_cer_7281
ER  - 

@conference{
author = "Mutić, Tamara and Gligorijević, Nikola and Ćirković Veličković, Tanja",
year = "2021",
abstract = "Microplastics are plastic fibers, particles or films with diameters smaller than 5 mm and they have shown different
effects on proteins [1]. Microplastics (MPs) are small in size, have low densities, can exist in the atmosphere for a
long time and can easily be spread by wind [2]. The objective of this study was to investigate adsorption affinity of
different types of MPs (polyethylene terephthalate (PET), polystyrene (PS) and polyvinyl chloride (PVC)) with
ovalbumin. In this study ovalbumin, isolated from chicken egg white, was used. Plastics were mixed with ovalbumin
for 1,2,4 and 19 h and then the absorbance of the remaining protein in the solution was measured at 280nm. In
addition, Langmuir isotherm mathematical model to calculate the adsorption affinity of ovalbumin for MPs was used.
We determined affinity constants by using Langmuir isotherm models for different particle size (PS 120 μm and PS
500 μm), different types of plastics (PET, PS and PVC) and pH values (3 and 7,2). Adsorption experiment results
showed that adsorption depends on type of plastics. Our results showed that PVC did not adsorb ovalbumin,
however, PET and PS have interacted with protein. Adsorption capacities of all analysed MPs increase with pH of
solution. Under different pH values, MPs and protein have different charges that may affect adsorption
characteristics. With increase of pH from 3 to 7, the affinity for protein adsorption increased 1.4 times for PS (smaller
in size) while for PS (bigger size) and PET protein affinity was two times higher at pH 3.",
publisher = "Sociedade Portuguesa de Química",
journal = "Book of Abstracts - XXI EuroFoodChem conference, 22nd-24th November, 2021, Virtual Congress",
title = "Binding affinity ovalbumin on different type of microplastics using Langmuir isotherm",
pages = "178-178",
url = "https://hdl.handle.net/21.15107/rcub_cer_7281"
}

Mutić, T., Gligorijević, N.,& Ćirković Veličković, T.. (2021). Binding affinity ovalbumin on different type of microplastics using Langmuir isotherm. in Book of Abstracts - XXI EuroFoodChem conference, 22nd-24th November, 2021, Virtual Congress
Sociedade Portuguesa de Química., 178-178.
https://hdl.handle.net/21.15107/rcub_cer_7281

Mutić T, Gligorijević N, Ćirković Veličković T. Binding affinity ovalbumin on different type of microplastics using Langmuir isotherm. in Book of Abstracts - XXI EuroFoodChem conference, 22nd-24th November, 2021, Virtual Congress. 2021;:178-178.
https://hdl.handle.net/21.15107/rcub_cer_7281 .

Mutić, Tamara, Gligorijević, Nikola, Ćirković Veličković, Tanja, "Binding affinity ovalbumin on different type of microplastics using Langmuir isotherm" in Book of Abstracts - XXI EuroFoodChem conference, 22nd-24th November, 2021, Virtual Congress (2021):178-178,
https://hdl.handle.net/21.15107/rcub_cer_7281 .

TY  - CONF
AU  - Mutić, Tamara
AU  - Gligorijević, Nikola
AU  - Ćirković Veličković, Tanja
PY  - 2021
UR  - https://ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e5deeb546e&appId=PPGMS
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7283
AB  - Microplastics (MPs) are small in size, have low densities, can exist in the atmosphere for a
long time and can easily be spread by wind. Microplastics are plastic fibers, particles or films
with diameters smaller than 5 mm and they have shown different effects on proteins. The
objective of this study was to investigate adsorption affinity of different types of MPs
(polyethylene terephthalate (PET), polystyrene (PS) and polyvinyl chloride (PVC)) with
ovalbumin. Ovalbumin, isolated from chicken egg white, was used in this study. Plastics were
mixed with ovalbumin for 1,2,4 and 19 h and then the absorbance of the remaining protein in
the solution was measured at 280nm. In addition, isotherm mathematical model to calculate
the adsorption affinity of ovalbumin for MPs was used. We determined affinity constants by
using Langmuir isotherm models for different particle size (PS 120 m and PS 500 m),
different type of plastics (PET, PS and PVC) and pH values (3 and 7,2). Adsorption
experiment results showed that adsorption depends on type of plastics. Our results showed
that PVC did not adsorb protein, however, PET and PS have interacted with protein.
Adsorption capacities of all analysed MPs increase with pH of solution. Under different pH
values, MPs and protein have different charges that may affect adsorption characteristics.
With increase of pH from 3 to 7, the level of protein adsorption on MPs increased 14 times
for PS (smaller in size) and 5 times for PS (bigger size) and PET.
PB  - University of Belgrade - Faculty of Chemistry
C3  - FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Book of Abstracts, 16th-18th June, 2021, Belgrade, Serbia
T1  - Ovalbumin adsorption on different types of microplastic
SP  - 43
EP  - 43
UR  - https://hdl.handle.net/21.15107/rcub_cer_7283
ER  - 

@conference{
author = "Mutić, Tamara and Gligorijević, Nikola and Ćirković Veličković, Tanja",
year = "2021",
abstract = "Microplastics (MPs) are small in size, have low densities, can exist in the atmosphere for a
long time and can easily be spread by wind. Microplastics are plastic fibers, particles or films
with diameters smaller than 5 mm and they have shown different effects on proteins. The
objective of this study was to investigate adsorption affinity of different types of MPs
(polyethylene terephthalate (PET), polystyrene (PS) and polyvinyl chloride (PVC)) with
ovalbumin. Ovalbumin, isolated from chicken egg white, was used in this study. Plastics were
mixed with ovalbumin for 1,2,4 and 19 h and then the absorbance of the remaining protein in
the solution was measured at 280nm. In addition, isotherm mathematical model to calculate
the adsorption affinity of ovalbumin for MPs was used. We determined affinity constants by
using Langmuir isotherm models for different particle size (PS 120 m and PS 500 m),
different type of plastics (PET, PS and PVC) and pH values (3 and 7,2). Adsorption
experiment results showed that adsorption depends on type of plastics. Our results showed
that PVC did not adsorb protein, however, PET and PS have interacted with protein.
Adsorption capacities of all analysed MPs increase with pH of solution. Under different pH
values, MPs and protein have different charges that may affect adsorption characteristics.
With increase of pH from 3 to 7, the level of protein adsorption on MPs increased 14 times
for PS (smaller in size) and 5 times for PS (bigger size) and PET.",
publisher = "University of Belgrade - Faculty of Chemistry",
journal = "FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Book of Abstracts, 16th-18th June, 2021, Belgrade, Serbia",
title = "Ovalbumin adsorption on different types of microplastic",
pages = "43-43",
url = "https://hdl.handle.net/21.15107/rcub_cer_7283"
}

Mutić, T., Gligorijević, N.,& Ćirković Veličković, T.. (2021). Ovalbumin adsorption on different types of microplastic. in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Book of Abstracts, 16th-18th June, 2021, Belgrade, Serbia
University of Belgrade - Faculty of Chemistry., 43-43.
https://hdl.handle.net/21.15107/rcub_cer_7283

Mutić T, Gligorijević N, Ćirković Veličković T. Ovalbumin adsorption on different types of microplastic. in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Book of Abstracts, 16th-18th June, 2021, Belgrade, Serbia. 2021;:43-43.
https://hdl.handle.net/21.15107/rcub_cer_7283 .

Mutić, Tamara, Gligorijević, Nikola, Ćirković Veličković, Tanja, "Ovalbumin adsorption on different types of microplastic" in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Book of Abstracts, 16th-18th June, 2021, Belgrade, Serbia (2021):43-43,
https://hdl.handle.net/21.15107/rcub_cer_7283 .

TY  - CONF
AU  - Gligorijević, Nikola
AU  - Radomirović, Mirjana
AU  - Rajković, Andreja
AU  - Nedić, Olgica
AU  - Ćirković Veličković, Tanja
PY  - 2021
UR  - https://ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e5deeb546e&appId=PPGMS
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7284
AB  - The French paradox describes a lower incidence of cardiovascular problems despite a high intake of
saturated fats. This phenomenon was associated with higher consumption of red wine, only to be later discovered that the presence of several antioxidants, including resveratrol, are responsible for it. We investigated if resveratrol has a more direct role in protection from harmful oxidation and development of thrombosis, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetric analysis demonstrated binding of resveratrol to fibrinogen, the main protein in the coagulation process, which also has an important application as a food additive in making of fibrin gels. Various spectroscopic methods have demonstrated that binding of
resveratrol does not unfold or destabilize fibrinogen since both near and far-UV CD spectra as well as its melting temperature remained unchanged. A mutuallyprotective effect against the free radical-
induced oxidation of resveratrol and fibrinogen was found. The presence of fibrinogen caused a very
small masking effect of the antioxidative potential of resveratrol, measured by a reduction of
hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing potential bioavailability and activity of resveratrol in circulation. By direct interaction and protection of fibrinogen, resveratrol may serve as an important antioxidant for prevention of
thrombosis. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.
PB  - University of Belgrade - Faculty of Chemistry
C3  - FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Book of Abstracts, 16th-18th June, 2021, Belgrade, Serbia
T1  - Resveratrol and fibrinogen interactions
SP  - 15
EP  - 15
UR  - https://hdl.handle.net/21.15107/rcub_cer_7284
ER  - 

@conference{
author = "Gligorijević, Nikola and Radomirović, Mirjana and Rajković, Andreja and Nedić, Olgica and Ćirković Veličković, Tanja",
year = "2021",
abstract = "The French paradox describes a lower incidence of cardiovascular problems despite a high intake of
saturated fats. This phenomenon was associated with higher consumption of red wine, only to be later discovered that the presence of several antioxidants, including resveratrol, are responsible for it. We investigated if resveratrol has a more direct role in protection from harmful oxidation and development of thrombosis, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetric analysis demonstrated binding of resveratrol to fibrinogen, the main protein in the coagulation process, which also has an important application as a food additive in making of fibrin gels. Various spectroscopic methods have demonstrated that binding of
resveratrol does not unfold or destabilize fibrinogen since both near and far-UV CD spectra as well as its melting temperature remained unchanged. A mutuallyprotective effect against the free radical-
induced oxidation of resveratrol and fibrinogen was found. The presence of fibrinogen caused a very
small masking effect of the antioxidative potential of resveratrol, measured by a reduction of
hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing potential bioavailability and activity of resveratrol in circulation. By direct interaction and protection of fibrinogen, resveratrol may serve as an important antioxidant for prevention of
thrombosis. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.",
publisher = "University of Belgrade - Faculty of Chemistry",
journal = "FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Book of Abstracts, 16th-18th June, 2021, Belgrade, Serbia",
title = "Resveratrol and fibrinogen interactions",
pages = "15-15",
url = "https://hdl.handle.net/21.15107/rcub_cer_7284"
}

Gligorijević, N., Radomirović, M., Rajković, A., Nedić, O.,& Ćirković Veličković, T.. (2021). Resveratrol and fibrinogen interactions. in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Book of Abstracts, 16th-18th June, 2021, Belgrade, Serbia
University of Belgrade - Faculty of Chemistry., 15-15.
https://hdl.handle.net/21.15107/rcub_cer_7284

Gligorijević N, Radomirović M, Rajković A, Nedić O, Ćirković Veličković T. Resveratrol and fibrinogen interactions. in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Book of Abstracts, 16th-18th June, 2021, Belgrade, Serbia. 2021;:15-15.
https://hdl.handle.net/21.15107/rcub_cer_7284 .

Gligorijević, Nikola, Radomirović, Mirjana, Rajković, Andreja, Nedić, Olgica, Ćirković Veličković, Tanja, "Resveratrol and fibrinogen interactions" in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Book of Abstracts, 16th-18th June, 2021, Belgrade, Serbia (2021):15-15,
https://hdl.handle.net/21.15107/rcub_cer_7284 .

TY  - JOUR
AU  - Radibratović, Milica
AU  - Al-Hanish, Ayah
AU  - Minić, Simeon
AU  - Radomirović, Mirjana
AU  - Milčić, Miloš
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković Veličković, Tanja
PY  - 2019
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3212
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 epigallocatechin-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 α-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 and Radomirović, Mirjana and Milčić, Miloš 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 epigallocatechin-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 α-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., Radomirović, M., Milčić, M., Stanić-Vučinić, D.,& Ćirković Veličković, T.. (2019). Stabilization of apo α-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 S, Radomirović M, Milčić M, Stanić-Vučinić D, Ćirković Veličković T. Stabilization of apo α-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, Radomirović, Mirjana, Milčić, Miloš, Stanić-Vučinić, Dragana, Ćirković Veličković, Tanja, "Stabilization of apo α-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  - Uzelac, Tamara N.
AU  - Nikolić-Kokić, Aleksandra
AU  - Spasić, Snežana
AU  - Mačvanin, Mirjana T.
AU  - Nikolić, Milan
AU  - Mandić, Ljuba M.
AU  - Jovanović, Vesna B.
PY  - 2019
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3432
AB  - Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of itsreactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.
PB  - Elsevier
T2  - Chemico-Biological Interactions
T1  - Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content
VL  - 311
SP  - 108787
DO  - 10.1016/j.cbi.2019.108787
ER  - 

@article{
author = "Uzelac, Tamara N. and Nikolić-Kokić, Aleksandra and Spasić, Snežana and Mačvanin, Mirjana T. and Nikolić, Milan and Mandić, Ljuba M. and Jovanović, Vesna B.",
year = "2019",
abstract = "Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of itsreactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.",
publisher = "Elsevier",
journal = "Chemico-Biological Interactions",
title = "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content",
volume = "311",
pages = "108787",
doi = "10.1016/j.cbi.2019.108787"
}

Uzelac, T. N., Nikolić-Kokić, A., Spasić, S., Mačvanin, M. T., Nikolić, M., Mandić, L. M.,& Jovanović, V. B.. (2019). Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions
Elsevier., 311, 108787.
https://doi.org/10.1016/j.cbi.2019.108787

Uzelac TN, Nikolić-Kokić A, Spasić S, Mačvanin MT, Nikolić M, Mandić LM, Jovanović VB. Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions. 2019;311:108787.
doi:10.1016/j.cbi.2019.108787 .

Uzelac, Tamara N., Nikolić-Kokić, Aleksandra, Spasić, Snežana, Mačvanin, Mirjana T., Nikolić, Milan, Mandić, Ljuba M., Jovanović, Vesna B., "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content" in Chemico-Biological Interactions, 311 (2019):108787,
https://doi.org/10.1016/j.cbi.2019.108787 . .

TY  - JOUR
AU  - Uzelac, Tamara N.
AU  - Nikolić-Kokić, Aleksandra
AU  - Spasić, Snežana
AU  - Mačvanin, Mirjana T.
AU  - Nikolić, Milan
AU  - Mandić, Ljuba M.
AU  - Jovanović, Vesna B.
PY  - 2019
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3053
AB  - Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of its
reactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.
PB  - Elsevier
T2  - Chemico-Biological Interactions
T1  - Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content
VL  - 311
SP  - 108787
DO  - 10.1016/j.cbi.2019.108787
ER  - 

@article{
author = "Uzelac, Tamara N. and Nikolić-Kokić, Aleksandra and Spasić, Snežana and Mačvanin, Mirjana T. and Nikolić, Milan and Mandić, Ljuba M. and Jovanović, Vesna B.",
year = "2019",
abstract = "Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of its
reactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.",
publisher = "Elsevier",
journal = "Chemico-Biological Interactions",
title = "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content",
volume = "311",
pages = "108787",
doi = "10.1016/j.cbi.2019.108787"
}

Uzelac, T. N., Nikolić-Kokić, A., Spasić, S., Mačvanin, M. T., Nikolić, M., Mandić, L. M.,& Jovanović, V. B.. (2019). Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions
Elsevier., 311, 108787.
https://doi.org/10.1016/j.cbi.2019.108787

Uzelac TN, Nikolić-Kokić A, Spasić S, Mačvanin MT, Nikolić M, Mandić LM, Jovanović VB. Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions. 2019;311:108787.
doi:10.1016/j.cbi.2019.108787 .

Uzelac, Tamara N., Nikolić-Kokić, Aleksandra, Spasić, Snežana, Mačvanin, Mirjana T., Nikolić, Milan, Mandić, Ljuba M., Jovanović, Vesna B., "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content" in Chemico-Biological Interactions, 311 (2019):108787,
https://doi.org/10.1016/j.cbi.2019.108787 . .