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  - 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 .