TY  - CONF
AU  - Krstić-Ristivojević, Maja
AU  - Vasović, Tamara
AU  - Smiljanić, Katarina
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5951
AB  - rom over 10 kg in 1960 to over 20 kg in 2014, the yearly per capita consumption of
marine products has increased significantly during the past 50 years. In many nations,
especially those with poor overall protein intake, seafood protein is a crucial component of
the diet1. However, as defined by the European Community shellfish protein tropomyosin
(TPM) is one of the major allergens and major causes of anaphylaxis 2. Although TPM
originating from vertebrates is not considered as an allergen there is evidence that several
fish tropomyosin can be allergenic3. TPM protein is organized of two parallel alpha-helical
molecules which are wound around each other forming a coiled -coil structure2. Although
the degree of similarity between TPM molecules is high, their allergenic potency is
different. Scientists putting a lot of effort into iden tifying and sequencing tropomyosin
isoforms since this information probably explains the intriguing nature of the TPM
molecule. This is a very challenging task given that the differences in mass and pI values
between TPM isoforms are discrete.
TPM was isolated from mussels (Mytilus galloprovincialis), and clams (Venerupis
philippinarum) according to the protocol developed within/and for purposes of the
IMPTOX research project. The obtained “in-house” TPM proteins were resolved using
two-dimensional polyacrylamide gel electrophoresis (2D-PAGE). Isoelectric focusing was
performed on rehydrated Immobiline strips IPG 3-5.6NL 13 cm in Ettan IPGPhor 3 device.
The second dimension was carried out on 12% PAA gels. Upon protein bands excision to
prevent TPM interchain disulfide cross-linking reduction and alkylation of cysteine was
performed. The samples were digested with proteomics-grade trypsin in a 1:50 enzyme-to-
substrate ratio overnight at 37 °C. The obtained peptides were chromatographically
separated using the EASY-nLC II system and analyzed using Orbitrap Exploris 240 mass
spectrometer.
2D-PAGE resolved two isoforms of mussel TPM and up to eight isoforms of clam TPM.
The determined pI value of the dominant isoform of mussel TPM was 4.7 while the
discrete band arising from the second TPM isoform was slightly shifted toward acidic pI
and smaller molecular mass. The determined pI value of the three most dominant clam
TPM isoforms was 4.8, the fourth isoform was slightly shifted toward a more basic pI
value and lower protein molecular weight. The rest of the isoforms were slightly shifted
toward more acidic pI and at a similar molecular weight as the three dominant isoforms.
PB  - Kragujevac : Univerzitet, Prirodno-matematički fakultet
C3  - Zbornik apstrakata, VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike”, 2. jun 2023. godine, Kragujevac
T1  - Identification of isoforms of shelfish tropomyosin
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5951
ER  - 

@conference{
author = "Krstić-Ristivojević, Maja and Vasović, Tamara and Smiljanić, Katarina and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "rom over 10 kg in 1960 to over 20 kg in 2014, the yearly per capita consumption of
marine products has increased significantly during the past 50 years. In many nations,
especially those with poor overall protein intake, seafood protein is a crucial component of
the diet1. However, as defined by the European Community shellfish protein tropomyosin
(TPM) is one of the major allergens and major causes of anaphylaxis 2. Although TPM
originating from vertebrates is not considered as an allergen there is evidence that several
fish tropomyosin can be allergenic3. TPM protein is organized of two parallel alpha-helical
molecules which are wound around each other forming a coiled -coil structure2. Although
the degree of similarity between TPM molecules is high, their allergenic potency is
different. Scientists putting a lot of effort into iden tifying and sequencing tropomyosin
isoforms since this information probably explains the intriguing nature of the TPM
molecule. This is a very challenging task given that the differences in mass and pI values
between TPM isoforms are discrete.
TPM was isolated from mussels (Mytilus galloprovincialis), and clams (Venerupis
philippinarum) according to the protocol developed within/and for purposes of the
IMPTOX research project. The obtained “in-house” TPM proteins were resolved using
two-dimensional polyacrylamide gel electrophoresis (2D-PAGE). Isoelectric focusing was
performed on rehydrated Immobiline strips IPG 3-5.6NL 13 cm in Ettan IPGPhor 3 device.
The second dimension was carried out on 12% PAA gels. Upon protein bands excision to
prevent TPM interchain disulfide cross-linking reduction and alkylation of cysteine was
performed. The samples were digested with proteomics-grade trypsin in a 1:50 enzyme-to-
substrate ratio overnight at 37 °C. The obtained peptides were chromatographically
separated using the EASY-nLC II system and analyzed using Orbitrap Exploris 240 mass
spectrometer.
2D-PAGE resolved two isoforms of mussel TPM and up to eight isoforms of clam TPM.
The determined pI value of the dominant isoform of mussel TPM was 4.7 while the
discrete band arising from the second TPM isoform was slightly shifted toward acidic pI
and smaller molecular mass. The determined pI value of the three most dominant clam
TPM isoforms was 4.8, the fourth isoform was slightly shifted toward a more basic pI
value and lower protein molecular weight. The rest of the isoforms were slightly shifted
toward more acidic pI and at a similar molecular weight as the three dominant isoforms.",
publisher = "Kragujevac : Univerzitet, Prirodno-matematički fakultet",
journal = "Zbornik apstrakata, VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike”, 2. jun 2023. godine, Kragujevac",
title = "Identification of isoforms of shelfish tropomyosin",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5951"
}

Krstić-Ristivojević, M., Vasović, T., Smiljanić, K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2023). Identification of isoforms of shelfish tropomyosin. in Zbornik apstrakata, VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike”, 2. jun 2023. godine, Kragujevac
Kragujevac : Univerzitet, Prirodno-matematički fakultet..
https://hdl.handle.net/21.15107/rcub_cherry_5951

Krstić-Ristivojević M, Vasović T, Smiljanić K, Stanić-Vučinić D, Ćirković-Veličković T. Identification of isoforms of shelfish tropomyosin. in Zbornik apstrakata, VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike”, 2. jun 2023. godine, Kragujevac. 2023;.
https://hdl.handle.net/21.15107/rcub_cherry_5951 .

Krstić-Ristivojević, Maja, Vasović, Tamara, Smiljanić, Katarina, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Identification of isoforms of shelfish tropomyosin" in Zbornik apstrakata, VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike”, 2. jun 2023. godine, Kragujevac (2023),
https://hdl.handle.net/21.15107/rcub_cherry_5951 .

TY  - JOUR
AU  - Gligorijeviž, Nikola
AU  - Radomirović, Mirjana Ž.
AU  - Nedić, Olgica
AU  - Stojadinović, Marija M.
AU  - Khulal, Urmila
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4784
AB  - The worldwide outbreak of COVID-19 was caused by a pathogenic virus called Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2). Therapies against SARS-CoV-2 target the virus or human cells or the immune system. However, therapies based on specific antibodies, such as vaccines and monoclonal antibodies, may become inefficient enough when the virus changes its antigenicity due to mutations. Polyphenols are the major class of bioactive compounds in nature, exerting diverse health effects based on their direct antioxidant activity and their effects in the modulation of intracellular signaling. There are currently numerous clinical trials investigating the effects of polyphenols in prophylaxis and the treatment of COVID-19, from symptomatic, via moderate and severe COVID-19 treatment, to anti-fibrotic treatment in discharged COVID-19 patients. Antiviral activities of polyphenols and their impact on immune system modulation could serve as a solid basis for developing polyphenol-based natural approaches for preventing and treating COVID-19.
PB  - MDPI
T2  - International Journal of Molecular Sciences
T1  - Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention
VL  - 22
IS  - 22
SP  - 12385
DO  - 10.3390/ijms222212385
ER  - 

@article{
author = "Gligorijeviž, Nikola and Radomirović, Mirjana Ž. and Nedić, Olgica and Stojadinović, Marija M. and Khulal, Urmila and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "The worldwide outbreak of COVID-19 was caused by a pathogenic virus called Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2). Therapies against SARS-CoV-2 target the virus or human cells or the immune system. However, therapies based on specific antibodies, such as vaccines and monoclonal antibodies, may become inefficient enough when the virus changes its antigenicity due to mutations. Polyphenols are the major class of bioactive compounds in nature, exerting diverse health effects based on their direct antioxidant activity and their effects in the modulation of intracellular signaling. There are currently numerous clinical trials investigating the effects of polyphenols in prophylaxis and the treatment of COVID-19, from symptomatic, via moderate and severe COVID-19 treatment, to anti-fibrotic treatment in discharged COVID-19 patients. Antiviral activities of polyphenols and their impact on immune system modulation could serve as a solid basis for developing polyphenol-based natural approaches for preventing and treating COVID-19.",
publisher = "MDPI",
journal = "International Journal of Molecular Sciences",
title = "Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention",
volume = "22",
number = "22",
pages = "12385",
doi = "10.3390/ijms222212385"
}

Gligorijeviž, N., Radomirović, M. Ž., Nedić, O., Stojadinović, M. M., Khulal, U., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention. in International Journal of Molecular Sciences
MDPI., 22(22), 12385.
https://doi.org/10.3390/ijms222212385

Gligorijeviž N, Radomirović MŽ, Nedić O, Stojadinović MM, Khulal U, Stanić-Vučinić D, Ćirković-Veličković T. Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention. in International Journal of Molecular Sciences. 2021;22(22):12385.
doi:10.3390/ijms222212385 .

Gligorijeviž, Nikola, Radomirović, Mirjana Ž., Nedić, Olgica, Stojadinović, Marija M., Khulal, Urmila, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention" in International Journal of Molecular Sciences, 22, no. 22 (2021):12385,
https://doi.org/10.3390/ijms222212385 . .

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Lević, Steva M.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
AU  - Nedić, Olgica
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4862
AB  - Fibrinogen is a plasma protein that is highly susceptible to oxidation. Because of this chemical modification, fibrinogen acquires thrombogenic characteristics under different pathophysiological conditions. Increased carbonyl content and reduced porosity impair the degradation of formed fibrin mediated by plasmin. Fibrinogen is capable of interacting with many proteins, ions, and small molecules. These interactions can modify the functions of this protein. The discovery of new binding partners that may protect fibrinogen from harmful oxidation and, thus, preserve its normal function is essential. Some of the newly detected interactions between fibrinogen and small, natural bioactive molecules, together with the influence of these interactions on the structure and function of fibrinogen, will be presented in this text.
PB  - University of Novi Sad - Faculty of Sciences, Department of Biology
T2  - Biologia Serbica
T1  - Ligand binding to fibrinogen influences its structure and function
VL  - 43
IS  - 1
DO  - 10.5281/zenodo.5512285
ER  - 

@article{
author = "Gligorijević, Nikola and Minić, Simeon L. and Radomirović, Mirjana Ž. and Lević, Steva M. and Nikolić, Milan and Ćirković-Veličković, Tanja and Nedić, Olgica",
year = "2021",
abstract = "Fibrinogen is a plasma protein that is highly susceptible to oxidation. Because of this chemical modification, fibrinogen acquires thrombogenic characteristics under different pathophysiological conditions. Increased carbonyl content and reduced porosity impair the degradation of formed fibrin mediated by plasmin. Fibrinogen is capable of interacting with many proteins, ions, and small molecules. These interactions can modify the functions of this protein. The discovery of new binding partners that may protect fibrinogen from harmful oxidation and, thus, preserve its normal function is essential. Some of the newly detected interactions between fibrinogen and small, natural bioactive molecules, together with the influence of these interactions on the structure and function of fibrinogen, will be presented in this text.",
publisher = "University of Novi Sad - Faculty of Sciences, Department of Biology",
journal = "Biologia Serbica",
title = "Ligand binding to fibrinogen influences its structure and function",
volume = "43",
number = "1",
doi = "10.5281/zenodo.5512285"
}

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

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

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

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Radomirović, Mirjana Ž.
AU  - Rajković, Andreja
AU  - Nedić, Olgica
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4235
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, as it was later discovered that the presence of antioxidants, including resveratrol, have beneficial effects. We hypothesized that resveratrol may have a more direct role in protection from harmful oxidation, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetry demonstrated that resveratrol is capable of binding to fibrinogen, the main protein in the coagulation process, which is also important as a food additive. Various spectroscopic methods determined that binding does not cause fibrinogen unfolding or destabilization since protein melting temperature remains unchanged. A mutually protective effect against the free radical-induced oxidation of polyphenol and fibrinogen was found. The presence of fibrinogen caused only a negligible masking effect of the antioxidative abilities of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing its potential bioavailability. Due to its interaction with fibrinogen, resveratrol may serve as an antioxidant at the site of injury. 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  - Multidisciplinary Digital Publishing Institute (MDPI)
T2  - Foods
T1  - Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation
VL  - 9
IS  - 6
SP  - 780
DO  - 10.3390/foods9060780
ER  - 

@article{
author = "Gligorijević, Nikola and Radomirović, Mirjana Ž. and Rajković, Andreja and Nedić, Olgica and Ćirković-Veličković, Tanja",
year = "2020",
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, as it was later discovered that the presence of antioxidants, including resveratrol, have beneficial effects. We hypothesized that resveratrol may have a more direct role in protection from harmful oxidation, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetry demonstrated that resveratrol is capable of binding to fibrinogen, the main protein in the coagulation process, which is also important as a food additive. Various spectroscopic methods determined that binding does not cause fibrinogen unfolding or destabilization since protein melting temperature remains unchanged. A mutually protective effect against the free radical-induced oxidation of polyphenol and fibrinogen was found. The presence of fibrinogen caused only a negligible masking effect of the antioxidative abilities of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing its potential bioavailability. Due to its interaction with fibrinogen, resveratrol may serve as an antioxidant at the site of injury. 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 = "Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "Foods",
title = "Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation",
volume = "9",
number = "6",
pages = "780",
doi = "10.3390/foods9060780"
}

Gligorijević, N., Radomirović, M. Ž., Rajković, A., Nedić, O.,& Ćirković-Veličković, T.. (2020). Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation. in Foods
Multidisciplinary Digital Publishing Institute (MDPI)., 9(6), 780.
https://doi.org/10.3390/foods9060780

Gligorijević N, Radomirović MŽ, Rajković A, Nedić O, Ćirković-Veličković T. Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation. in Foods. 2020;9(6):780.
doi:10.3390/foods9060780 .

Gligorijević, Nikola, Radomirović, Mirjana Ž., Rajković, Andreja, Nedić, Olgica, Ćirković-Veličković, Tanja, "Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation" in Foods, 9, no. 6 (2020):780,
https://doi.org/10.3390/foods9060780 . .