TY  - CONF
AU  - Kaseke, Tafadzwa
AU  - Jovanović, Vesna B.
AU  - Ćirković Veličković, Tanja
PY  - 2024
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6571
AB  - Infants are exposed to and ingest more micro-and nanoplastics (MNPs) than any other age group1; however, the effect of MNPs on the digestion of proteins in infants is not known. Therefore, the current study investigated the in vitro digestion of cow’s milk proteins in the presence of polypropylene MNPs (PP-MNPs) in simulated gastric fluids (SGF) using infant digestion model (pH=5.0; pepsin activity=268 U/mL). The simulated in vitro digestion of skimmed (<1% fat) cow’s milk proteins in infants in the presence of PP-MPs (20 mg/mL; 63–180 μm in size) was done at 37 °C for 5, 30, and 120 min. The in vitro digestion experiment was repeated with different concentrations of PP-NPs (125, 250, and 500 μg/mL) for 30 min. Another experiment was set up using adult gastrointestinal conditions (pH=3.0; pepsin activity=2000 U/mL) for comparison purposes2. The final concentration of the cow’s milk protein in the digestion mixture was 1 mg/mL. Then, proteins binding to the PP-MNPs were extracted from the soft corona and hard corona using the centrifugation method and protein profiles were analyzed using SDS-PAGE. The bands of proteins of interest were carefully excised from the gels and analysed by LC–MS/MS. Both PP-MPs and PP-NPs negatively affected the digestion of proteins in infants, and binding was observed in both the soft and hard corona. Meanwhile, no significant effects of both PP-MPs and PP-NPs on protein digestion were observed in adults. These results suggest possible interference of MNPs with the utilization of proteins in infants, which could have detrimental health effects.
PB  - University of Belgrade – Faculty of Chemistry
C3  - VII Symposium of the Serbian Proteomics Association – SePA “Application of proteomics in biomedicine”, Belgrade, Serbia June 6th, 2024
T1  - Polypropylene micro-and nanoplastics affects the digestion of cow's milk proteins in infants
SP  - 21
EP  - 21
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6571
ER  - 

@conference{
author = "Kaseke, Tafadzwa and Jovanović, Vesna B. and Ćirković Veličković, Tanja",
year = "2024",
abstract = "Infants are exposed to and ingest more micro-and nanoplastics (MNPs) than any other age group1; however, the effect of MNPs on the digestion of proteins in infants is not known. Therefore, the current study investigated the in vitro digestion of cow’s milk proteins in the presence of polypropylene MNPs (PP-MNPs) in simulated gastric fluids (SGF) using infant digestion model (pH=5.0; pepsin activity=268 U/mL). The simulated in vitro digestion of skimmed (<1% fat) cow’s milk proteins in infants in the presence of PP-MPs (20 mg/mL; 63–180 μm in size) was done at 37 °C for 5, 30, and 120 min. The in vitro digestion experiment was repeated with different concentrations of PP-NPs (125, 250, and 500 μg/mL) for 30 min. Another experiment was set up using adult gastrointestinal conditions (pH=3.0; pepsin activity=2000 U/mL) for comparison purposes2. The final concentration of the cow’s milk protein in the digestion mixture was 1 mg/mL. Then, proteins binding to the PP-MNPs were extracted from the soft corona and hard corona using the centrifugation method and protein profiles were analyzed using SDS-PAGE. The bands of proteins of interest were carefully excised from the gels and analysed by LC–MS/MS. Both PP-MPs and PP-NPs negatively affected the digestion of proteins in infants, and binding was observed in both the soft and hard corona. Meanwhile, no significant effects of both PP-MPs and PP-NPs on protein digestion were observed in adults. These results suggest possible interference of MNPs with the utilization of proteins in infants, which could have detrimental health effects.",
publisher = "University of Belgrade – Faculty of Chemistry",
journal = "VII Symposium of the Serbian Proteomics Association – SePA “Application of proteomics in biomedicine”, Belgrade, Serbia June 6th, 2024",
title = "Polypropylene micro-and nanoplastics affects the digestion of cow's milk proteins in infants",
pages = "21-21",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6571"
}

Kaseke, T., Jovanović, V. B.,& Ćirković Veličković, T.. (2024). Polypropylene micro-and nanoplastics affects the digestion of cow's milk proteins in infants. in VII Symposium of the Serbian Proteomics Association – SePA “Application of proteomics in biomedicine”, Belgrade, Serbia June 6th, 2024
University of Belgrade – Faculty of Chemistry., 21-21.
https://hdl.handle.net/21.15107/rcub_cherry_6571

Kaseke T, Jovanović VB, Ćirković Veličković T. Polypropylene micro-and nanoplastics affects the digestion of cow's milk proteins in infants. in VII Symposium of the Serbian Proteomics Association – SePA “Application of proteomics in biomedicine”, Belgrade, Serbia June 6th, 2024. 2024;:21-21.
https://hdl.handle.net/21.15107/rcub_cherry_6571 .

Kaseke, Tafadzwa, Jovanović, Vesna B., Ćirković Veličković, Tanja, "Polypropylene micro-and nanoplastics affects the digestion of cow's milk proteins in infants" in VII Symposium of the Serbian Proteomics Association – SePA “Application of proteomics in biomedicine”, Belgrade, Serbia June 6th, 2024 (2024):21-21,
https://hdl.handle.net/21.15107/rcub_cherry_6571 .

TY  - CONF
AU  - Lujić, Tamara
AU  - Krstić Ristivojević, Maja
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Wimmer, Lukas
AU  - Dailey, Lea Ann
AU  - Ćirković Veličković, Tanja
PY  - 2024
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6576
AB  - Trypsin is the main protease in the intestine. Microplastics (MPs) have been previously shown to interact with and decrease the activity of some digestive enzymes, including pepsin and lipase. Red meat has been shown to be a source of allergy which has been linked to the galactose-alpha-1,3-galactose (alpha-Gal) posttranslational modification of proteins. Our aim was to investigate the effect of two types of MPs commonly found in the environment – polypropylene (PP) and polyethylene terephthalate (PET) – on the digestion of protein in beef meat extract and preservation of protein harboring the alpha-Gal epitope. Digestion of beef meat extract has been performed with trypsin in simulated intestinal fluid (SIF) in the presence of MPs. After digestion was stopped with a specific inhibitor, bulk beef meat extract was separated through centrifugation from the MPs. Soft coronas were obtained by washing the MPs with SIF. The hard corona was obtained by addition of a reducing buffer for electrophoresis sample preparation to the MPs with a heating step at 95°C. All samples were analyzed with SDS-PAG electrophoresis. Selected samples were further analyzed with anti-alpha-Gal antibodies using western blot. There is an observable difference between the digestion patterns of meat extract after 1 and 2 h of digestion in the presence of MPs compared to the control. Evolution of digestion is similar for both types of MPs, without regard to plastic type. It has also been confirmed that preserved proteins possess the alpha-Gal modification. As MPs presence does not change trypsin specific activity, the change in digestion pattern is presumed to be due to steric effects and/or interplay of enzyme/protein in the corona. This study suggests that MPs presence influences trypsin digestibility of meat proteins, including alpha-Gal-bearing allergens. This project has received funding from the European Union’s Horizon 2020 research and innovation programme under grant agreement No 965173.
PB  - FEBS Press
C3  - FEBS Open Bio, Mining biochemistry for human health and well‐being, 48th FEBS Congress, 29 June – 3 July 2024, Milano, Italy
T1  - Trypsin digestion of protein in beef meat extract in the presence of microplastics
VL  - 14
IS  - S2
SP  - 428
EP  - 428
DO  - 10.1002/2211-5463.13837
ER  - 

@conference{
author = "Lujić, Tamara and Krstić Ristivojević, Maja and Gligorijević, Nikola and Stanić-Vučinić, Dragana and Wimmer, Lukas and Dailey, Lea Ann and Ćirković Veličković, Tanja",
year = "2024",
abstract = "Trypsin is the main protease in the intestine. Microplastics (MPs) have been previously shown to interact with and decrease the activity of some digestive enzymes, including pepsin and lipase. Red meat has been shown to be a source of allergy which has been linked to the galactose-alpha-1,3-galactose (alpha-Gal) posttranslational modification of proteins. Our aim was to investigate the effect of two types of MPs commonly found in the environment – polypropylene (PP) and polyethylene terephthalate (PET) – on the digestion of protein in beef meat extract and preservation of protein harboring the alpha-Gal epitope. Digestion of beef meat extract has been performed with trypsin in simulated intestinal fluid (SIF) in the presence of MPs. After digestion was stopped with a specific inhibitor, bulk beef meat extract was separated through centrifugation from the MPs. Soft coronas were obtained by washing the MPs with SIF. The hard corona was obtained by addition of a reducing buffer for electrophoresis sample preparation to the MPs with a heating step at 95°C. All samples were analyzed with SDS-PAG electrophoresis. Selected samples were further analyzed with anti-alpha-Gal antibodies using western blot. There is an observable difference between the digestion patterns of meat extract after 1 and 2 h of digestion in the presence of MPs compared to the control. Evolution of digestion is similar for both types of MPs, without regard to plastic type. It has also been confirmed that preserved proteins possess the alpha-Gal modification. As MPs presence does not change trypsin specific activity, the change in digestion pattern is presumed to be due to steric effects and/or interplay of enzyme/protein in the corona. This study suggests that MPs presence influences trypsin digestibility of meat proteins, including alpha-Gal-bearing allergens. This project has received funding from the European Union’s Horizon 2020 research and innovation programme under grant agreement No 965173.",
publisher = "FEBS Press",
journal = "FEBS Open Bio, Mining biochemistry for human health and well‐being, 48th FEBS Congress, 29 June – 3 July 2024, Milano, Italy",
title = "Trypsin digestion of protein in beef meat extract in the presence of microplastics",
volume = "14",
number = "S2",
pages = "428-428",
doi = "10.1002/2211-5463.13837"
}

Lujić, T., Krstić Ristivojević, M., Gligorijević, N., Stanić-Vučinić, D., Wimmer, L., Dailey, L. A.,& Ćirković Veličković, T.. (2024). Trypsin digestion of protein in beef meat extract in the presence of microplastics. in FEBS Open Bio, Mining biochemistry for human health and well‐being, 48th FEBS Congress, 29 June – 3 July 2024, Milano, Italy
FEBS Press., 14(S2), 428-428.
https://doi.org/10.1002/2211-5463.13837

Lujić T, Krstić Ristivojević M, Gligorijević N, Stanić-Vučinić D, Wimmer L, Dailey LA, Ćirković Veličković T. Trypsin digestion of protein in beef meat extract in the presence of microplastics. in FEBS Open Bio, Mining biochemistry for human health and well‐being, 48th FEBS Congress, 29 June – 3 July 2024, Milano, Italy. 2024;14(S2):428-428.
doi:10.1002/2211-5463.13837 .

Lujić, Tamara, Krstić Ristivojević, Maja, Gligorijević, Nikola, Stanić-Vučinić, Dragana, Wimmer, Lukas, Dailey, Lea Ann, Ćirković Veličković, Tanja, "Trypsin digestion of protein in beef meat extract in the presence of microplastics" in FEBS Open Bio, Mining biochemistry for human health and well‐being, 48th FEBS Congress, 29 June – 3 July 2024, Milano, Italy, 14, no. S2 (2024):428-428,
https://doi.org/10.1002/2211-5463.13837 . .

TY  - DATA
AU  - Mutić, Tamara
AU  - Stanić-Vučinić, Dragana
AU  - Mutić, Jelena
AU  - Ilić, Miloš
AU  - Jovanović, Vesna B.
AU  - Aćimović, Jelena
AU  - Anđelković, Boban
AU  - Krishna de Guzman, Maria
AU  - Anđelković, Mirjana
AU  - Turkalj, Mirjana
AU  - Ćirković Veličković, Tanja
PY  - 2024
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6484
AB  - The experimental data for the results shown in the manuscript "Microplastic contamination of edible parts of commercially important mussels, clams and shrimps in different markets". Statistical investigation of the presence of microplastics in bivalve species using microFTIR. This dataset includes samples from various origins, including Sebia, South Korea, Croatia and Belgium, and includes species as diverse as shrimp, mussels and clams.
T1  - Research data no. 1 for the manuscript: Microplastics contamination of edible parts of commercially relevant species of mussels, clams and shrimps across various markets
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6484
ER  - 

@misc{
author = "Mutić, Tamara and Stanić-Vučinić, Dragana and Mutić, Jelena and Ilić, Miloš and Jovanović, Vesna B. and Aćimović, Jelena and Anđelković, Boban and Krishna de Guzman, Maria and Anđelković, Mirjana and Turkalj, Mirjana and Ćirković Veličković, Tanja",
year = "2024",
abstract = "The experimental data for the results shown in the manuscript "Microplastic contamination of edible parts of commercially important mussels, clams and shrimps in different markets". Statistical investigation of the presence of microplastics in bivalve species using microFTIR. This dataset includes samples from various origins, including Sebia, South Korea, Croatia and Belgium, and includes species as diverse as shrimp, mussels and clams.",
title = "Research data no. 1 for the manuscript: Microplastics contamination of edible parts of commercially relevant species of mussels, clams and shrimps across various markets",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6484"
}

Mutić, T., Stanić-Vučinić, D., Mutić, J., Ilić, M., Jovanović, V. B., Aćimović, J., Anđelković, B., Krishna de Guzman, M., Anđelković, M., Turkalj, M.,& Ćirković Veličković, T.. (2024). Research data no. 1 for the manuscript: Microplastics contamination of edible parts of commercially relevant species of mussels, clams and shrimps across various markets. .
https://hdl.handle.net/21.15107/rcub_cherry_6484

Mutić T, Stanić-Vučinić D, Mutić J, Ilić M, Jovanović VB, Aćimović J, Anđelković B, Krishna de Guzman M, Anđelković M, Turkalj M, Ćirković Veličković T. Research data no. 1 for the manuscript: Microplastics contamination of edible parts of commercially relevant species of mussels, clams and shrimps across various markets. 2024;.
https://hdl.handle.net/21.15107/rcub_cherry_6484 .

Mutić, Tamara, Stanić-Vučinić, Dragana, Mutić, Jelena, Ilić, Miloš, Jovanović, Vesna B., Aćimović, Jelena, Anđelković, Boban, Krishna de Guzman, Maria, Anđelković, Mirjana, Turkalj, Mirjana, Ćirković Veličković, Tanja, "Research data no. 1 for the manuscript: Microplastics contamination of edible parts of commercially relevant species of mussels, clams and shrimps across various markets" (2024),
https://hdl.handle.net/21.15107/rcub_cherry_6484 .

TY  - CONF
AU  - Kaseke, Tafadzwa
AU  - Ćirković Veličković, Tanja
PY  - 2024
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6560
AB  - Microplastics (MPs) of various morphologies have been ubiquitously detected in the environment, food, drinking water, and biota and may pose a threat to food safety and human health. Interestingly, the highest reported concentration of MPs comes from the processing of foods in plastic packaging. MPs exposure to humans is more prevalent in infants than in any other age group due to the use of polypropylene (PP)-based products in formula preparation. Although the effect of MPs on human health is still controversial, multiple studies conducted using in vivo and in vitro animal models have suggested that MPs can lead to a variety of health problems for humans, including gastrointestinal disorders, obesity, inflammation, cardiovascular disease, disruption of the endocrine system, and damage to vital organs including the liver and spleen. In addition, MPs could disrupt the digestion and bioavailability of important nutrients such as proteins, affecting the proper functioning of the human body, or triggering chronic health diseases and allergic reactions. Meanwhile, cow’s milk forms an essential part of the diet of infants as a source of protein and other nutrients and a primary component of infant formula. MPs have been found in milk products, including prepared infant formula. Despite the overwhelming evidence of the presence of MPs in infant foods, the literature remains deficient in information relating to the impact of MPs on the digestion and absorption of proteins in infants. This research gap gave birth to the European Union’s Horizon Europe-funded Microprot project. The broad aim of the Microprot project is to investigate the impact of polypropylene-based MPs from plastic packaging material on the digestibility of proteins in adults and infants. Therefore, the occurrence of MPs in various foods and their potential effect on health will be presented, highlighting the approach and impact of the Microprot project.
C3  - 3rd International UNIfood Conference, 28th-29th June 2024, University of Belgrade
T1  - Impact of microplastics originating from formula preparation on protein digestion in infant digestion models
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6560
ER  - 

@conference{
author = "Kaseke, Tafadzwa and Ćirković Veličković, Tanja",
year = "2024",
abstract = "Microplastics (MPs) of various morphologies have been ubiquitously detected in the environment, food, drinking water, and biota and may pose a threat to food safety and human health. Interestingly, the highest reported concentration of MPs comes from the processing of foods in plastic packaging. MPs exposure to humans is more prevalent in infants than in any other age group due to the use of polypropylene (PP)-based products in formula preparation. Although the effect of MPs on human health is still controversial, multiple studies conducted using in vivo and in vitro animal models have suggested that MPs can lead to a variety of health problems for humans, including gastrointestinal disorders, obesity, inflammation, cardiovascular disease, disruption of the endocrine system, and damage to vital organs including the liver and spleen. In addition, MPs could disrupt the digestion and bioavailability of important nutrients such as proteins, affecting the proper functioning of the human body, or triggering chronic health diseases and allergic reactions. Meanwhile, cow’s milk forms an essential part of the diet of infants as a source of protein and other nutrients and a primary component of infant formula. MPs have been found in milk products, including prepared infant formula. Despite the overwhelming evidence of the presence of MPs in infant foods, the literature remains deficient in information relating to the impact of MPs on the digestion and absorption of proteins in infants. This research gap gave birth to the European Union’s Horizon Europe-funded Microprot project. The broad aim of the Microprot project is to investigate the impact of polypropylene-based MPs from plastic packaging material on the digestibility of proteins in adults and infants. Therefore, the occurrence of MPs in various foods and their potential effect on health will be presented, highlighting the approach and impact of the Microprot project.",
journal = "3rd International UNIfood Conference, 28th-29th June 2024, University of Belgrade",
title = "Impact of microplastics originating from formula preparation on protein digestion in infant digestion models",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6560"
}

Kaseke, T.,& Ćirković Veličković, T.. (2024). Impact of microplastics originating from formula preparation on protein digestion in infant digestion models. in 3rd International UNIfood Conference, 28th-29th June 2024, University of Belgrade.
https://hdl.handle.net/21.15107/rcub_cherry_6560

Kaseke T, Ćirković Veličković T. Impact of microplastics originating from formula preparation on protein digestion in infant digestion models. in 3rd International UNIfood Conference, 28th-29th June 2024, University of Belgrade. 2024;.
https://hdl.handle.net/21.15107/rcub_cherry_6560 .

Kaseke, Tafadzwa, Ćirković Veličković, Tanja, "Impact of microplastics originating from formula preparation on protein digestion in infant digestion models" in 3rd International UNIfood Conference, 28th-29th June 2024, University of Belgrade (2024),
https://hdl.handle.net/21.15107/rcub_cherry_6560 .

TY  - CONF
AU  - Đukić, Teodora
AU  - Khulal, Urmila
AU  - Smiljanić, Katarina
AU  - Vasović, Tamara
AU  - Aćimović, Jelena
AU  - Rajković, Andreja
AU  - Ćirković Veličković, Tanja
PY  - 2024
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6539
AB  - Protein modifications (PMs) are covalent changes occurring on amino acid (AA) side chains of
proteins via enzymatic action or spontaneously. They increase the protein structure complexity
from the level of the genome to the proteome, and can determine their activity and, interactions1.
It has been shown, on myofibrillar fish proteins that oxidative modifications depending on their
saturation can decrease or enhance protein digestability2. Thus in this study shellfish meat samples
were subjected to cooking followed by simulated INFOGEST in vitro gastrointestinal digestion
protocol. Mass Spectrometry and in gel based proteomics, were used to detect PMs and digestion
resistan peptides of raw and cooked shellfish meat samples with a foucs on major shellfish allergens:
sarcoplasmic calcium-binding protein (SBP) and tropomyosin (TPM). Lastly, identified PMs
were marked on TPM alignment from shrimp, oyster and abalone species, to gain insight into their
pattern on the known IgE binding epitopes. Focusing on oxidative PMs, mostly on oxidation of Met,
it was confirmed that, in all shellfish samples, PMs on TPM and SBP were more predominant after
cooking. For instance in abalone, double oxidation of Met was only detected in cooked samples
(sulfone M68 and M81). Another indicator of oxidative stress, 4-hydroxynonenal (HNE), was identified
on shrimp TPM and, notably HNE was 21 times more abundant in the cooked sample. Study
highlights the susceptibility of immunodominant epitopes in major shellfish allergens to oxidative
PMs, which could impact interactions with the immune system in sensitive individuals. Significant
resistance to digestion was demonstrated by paramyosin fragments in abalone and oyster suggesting
the need for further analysis of their allergenicity. SBP of raw shrimp was strikingly resistant
to both gastric and intestinal digestion. Moreover, our results indicate that oxidative modifications
may decrease the stability of proteins like shrimp TPM, making them more digestible in thermally
treated samples, highlighting a potential strategy for reducing allergenicity.
PB  - University of Belgrade – Faculty of Chemistry
C3  - VII Symposium of the Serbian Proteomics Association – SePA “Application of proteomics in biomedicine”, Belgrade, Serbia June 6th, 2024
T1  - Insights into oxidative protein modifications in shellfish allergens: Impact of GI digestion following thermal treatment
SP  - 10
EP  - 10
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6539
ER  - 

@conference{
author = "Đukić, Teodora and Khulal, Urmila and Smiljanić, Katarina and Vasović, Tamara and Aćimović, Jelena and Rajković, Andreja and Ćirković Veličković, Tanja",
year = "2024",
abstract = "Protein modifications (PMs) are covalent changes occurring on amino acid (AA) side chains of
proteins via enzymatic action or spontaneously. They increase the protein structure complexity
from the level of the genome to the proteome, and can determine their activity and, interactions1.
It has been shown, on myofibrillar fish proteins that oxidative modifications depending on their
saturation can decrease or enhance protein digestability2. Thus in this study shellfish meat samples
were subjected to cooking followed by simulated INFOGEST in vitro gastrointestinal digestion
protocol. Mass Spectrometry and in gel based proteomics, were used to detect PMs and digestion
resistan peptides of raw and cooked shellfish meat samples with a foucs on major shellfish allergens:
sarcoplasmic calcium-binding protein (SBP) and tropomyosin (TPM). Lastly, identified PMs
were marked on TPM alignment from shrimp, oyster and abalone species, to gain insight into their
pattern on the known IgE binding epitopes. Focusing on oxidative PMs, mostly on oxidation of Met,
it was confirmed that, in all shellfish samples, PMs on TPM and SBP were more predominant after
cooking. For instance in abalone, double oxidation of Met was only detected in cooked samples
(sulfone M68 and M81). Another indicator of oxidative stress, 4-hydroxynonenal (HNE), was identified
on shrimp TPM and, notably HNE was 21 times more abundant in the cooked sample. Study
highlights the susceptibility of immunodominant epitopes in major shellfish allergens to oxidative
PMs, which could impact interactions with the immune system in sensitive individuals. Significant
resistance to digestion was demonstrated by paramyosin fragments in abalone and oyster suggesting
the need for further analysis of their allergenicity. SBP of raw shrimp was strikingly resistant
to both gastric and intestinal digestion. Moreover, our results indicate that oxidative modifications
may decrease the stability of proteins like shrimp TPM, making them more digestible in thermally
treated samples, highlighting a potential strategy for reducing allergenicity.",
publisher = "University of Belgrade – Faculty of Chemistry",
journal = "VII Symposium of the Serbian Proteomics Association – SePA “Application of proteomics in biomedicine”, Belgrade, Serbia June 6th, 2024",
title = "Insights into oxidative protein modifications in shellfish allergens: Impact of GI digestion following thermal treatment",
pages = "10-10",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6539"
}

Đukić, T., Khulal, U., Smiljanić, K., Vasović, T., Aćimović, J., Rajković, A.,& Ćirković Veličković, T.. (2024). Insights into oxidative protein modifications in shellfish allergens: Impact of GI digestion following thermal treatment. in VII Symposium of the Serbian Proteomics Association – SePA “Application of proteomics in biomedicine”, Belgrade, Serbia June 6th, 2024
University of Belgrade – Faculty of Chemistry., 10-10.
https://hdl.handle.net/21.15107/rcub_cherry_6539

Đukić T, Khulal U, Smiljanić K, Vasović T, Aćimović J, Rajković A, Ćirković Veličković T. Insights into oxidative protein modifications in shellfish allergens: Impact of GI digestion following thermal treatment. in VII Symposium of the Serbian Proteomics Association – SePA “Application of proteomics in biomedicine”, Belgrade, Serbia June 6th, 2024. 2024;:10-10.
https://hdl.handle.net/21.15107/rcub_cherry_6539 .

Đukić, Teodora, Khulal, Urmila, Smiljanić, Katarina, Vasović, Tamara, Aćimović, Jelena, Rajković, Andreja, Ćirković Veličković, Tanja, "Insights into oxidative protein modifications in shellfish allergens: Impact of GI digestion following thermal treatment" in VII Symposium of the Serbian Proteomics Association – SePA “Application of proteomics in biomedicine”, Belgrade, Serbia June 6th, 2024 (2024):10-10,
https://hdl.handle.net/21.15107/rcub_cherry_6539 .

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Lujić, Tamara
AU  - Mutić, Tamara
AU  - Vasović, Tamara
AU  - Aćimović, Jelena
AU  - de Guzman, Maria Krishna
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković Veličković, Tanja
PY  - 2024
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6510
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties
VL  - 267
SP  - 131564
DO  - 10.1016/j.ijbiomac.2024.131564
ER  - 

@article{
author = "Gligorijević, Nikola and Lujić, Tamara and Mutić, Tamara and Vasović, Tamara and Aćimović, Jelena and de Guzman, Maria Krishna and Stanić-Vučinić, Dragana and Ćirković Veličković, Tanja",
year = "2024",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties",
volume = "267",
pages = "131564",
doi = "10.1016/j.ijbiomac.2024.131564"
}

Gligorijević, N., Lujić, T., Mutić, T., Vasović, T., Aćimović, J., de Guzman, M. K., Stanić-Vučinić, D.,& Ćirković Veličković, T.. (2024). Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties. in International Journal of Biological Macromolecules
Elsevier., 267, 131564.
https://doi.org/10.1016/j.ijbiomac.2024.131564

Gligorijević N, Lujić T, Mutić T, Vasović T, Aćimović J, de Guzman MK, Stanić-Vučinić D, Ćirković Veličković T. Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties. in International Journal of Biological Macromolecules. 2024;267:131564.
doi:10.1016/j.ijbiomac.2024.131564 .

Gligorijević, Nikola, Lujić, Tamara, Mutić, Tamara, Vasović, Tamara, Aćimović, Jelena, de Guzman, Maria Krishna, Stanić-Vučinić, Dragana, Ćirković Veličković, Tanja, "Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties" in International Journal of Biological Macromolecules, 267 (2024):131564,
https://doi.org/10.1016/j.ijbiomac.2024.131564 . .

TY  - DATA
AU  - Gligorijević, Nikola
AU  - Lujić, Tamara
AU  - Mutić, Tamara
AU  - Vasović, Tamara
AU  - Aćimović, Jelena
AU  - de Guzman, Maria Krishna
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković Veličković, Tanja
PY  - 2024
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6469
AB  - Research data for the unpublished paper: Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties. Densitometry analysis of ovalbumin band intensity after digestion in the presence of microplastics on SDS-PAGE gels.
T1  - Research data no. 2 for the manuscript: Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6469
ER  - 

@misc{
author = "Gligorijević, Nikola and Lujić, Tamara and Mutić, Tamara and Vasović, Tamara and Aćimović, Jelena and de Guzman, Maria Krishna and Stanić-Vučinić, Dragana and Ćirković Veličković, Tanja",
year = "2024",
abstract = "Research data for the unpublished paper: Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties. Densitometry analysis of ovalbumin band intensity after digestion in the presence of microplastics on SDS-PAGE gels.",
title = "Research data no. 2 for the manuscript: Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6469"
}

Gligorijević, N., Lujić, T., Mutić, T., Vasović, T., Aćimović, J., de Guzman, M. K., Stanić-Vučinić, D.,& Ćirković Veličković, T.. (2024). Research data no. 2 for the manuscript: Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties. .
https://hdl.handle.net/21.15107/rcub_cherry_6469

Gligorijević N, Lujić T, Mutić T, Vasović T, Aćimović J, de Guzman MK, Stanić-Vučinić D, Ćirković Veličković T. Research data no. 2 for the manuscript: Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties. 2024;.
https://hdl.handle.net/21.15107/rcub_cherry_6469 .

Gligorijević, Nikola, Lujić, Tamara, Mutić, Tamara, Vasović, Tamara, Aćimović, Jelena, de Guzman, Maria Krishna, Stanić-Vučinić, Dragana, Ćirković Veličković, Tanja, "Research data no. 2 for the manuscript: Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties" (2024),
https://hdl.handle.net/21.15107/rcub_cherry_6469 .

TY  - DATA
AU  - Gligorijević, Nikola
AU  - Lujić, Tamara
AU  - Mutić, Tamara
AU  - Vasović, Tamara
AU  - de Guzman, Maria Krishna
AU  - Aćimović, Jelena
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković Veličković, Tanja
PY  - 2024
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6465
AB  - Data used for the analysis of pepsin interaction with polystyrene microplastic of 10 and 100 µm in size. Binding isotherms data were used for the construction of binding isotherms from which binding between pepsin and polystyrene microplastic was described. Structural features of pepsin in the presence of polystyrene were analysed by CD spectrometry and spectrofluorimetry.
T1  - Research data no. 1 for the manuscript: Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6465
ER  - 

@misc{
author = "Gligorijević, Nikola and Lujić, Tamara and Mutić, Tamara and Vasović, Tamara and de Guzman, Maria Krishna and Aćimović, Jelena and Stanić-Vučinić, Dragana and Ćirković Veličković, Tanja",
year = "2024",
abstract = "Data used for the analysis of pepsin interaction with polystyrene microplastic of 10 and 100 µm in size. Binding isotherms data were used for the construction of binding isotherms from which binding between pepsin and polystyrene microplastic was described. Structural features of pepsin in the presence of polystyrene were analysed by CD spectrometry and spectrofluorimetry.",
title = "Research data no. 1 for the manuscript: Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6465"
}

Gligorijević, N., Lujić, T., Mutić, T., Vasović, T., de Guzman, M. K., Aćimović, J., Stanić-Vučinić, D.,& Ćirković Veličković, T.. (2024). Research data no. 1 for the manuscript: Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties. .
https://hdl.handle.net/21.15107/rcub_cherry_6465

Gligorijević N, Lujić T, Mutić T, Vasović T, de Guzman MK, Aćimović J, Stanić-Vučinić D, Ćirković Veličković T. Research data no. 1 for the manuscript: Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties. 2024;.
https://hdl.handle.net/21.15107/rcub_cherry_6465 .

Gligorijević, Nikola, Lujić, Tamara, Mutić, Tamara, Vasović, Tamara, de Guzman, Maria Krishna, Aćimović, Jelena, Stanić-Vučinić, Dragana, Ćirković Veličković, Tanja, "Research data no. 1 for the manuscript: Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties" (2024),
https://hdl.handle.net/21.15107/rcub_cherry_6465 .

TY  - JOUR
AU  - Khulal, Urmila
AU  - Đukić, Teodora
AU  - Smiljanić, Katarina
AU  - Vasović, Tamara
AU  - Aćimović, Jelena
AU  - Rajković, Andreja
AU  - Ćirković Veličković, Tanja
PY  - 2024
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6437
AB  - Meat samples were subjected to thermal processing combined with simulated INFOGEST in vitro gastrointestinal (GI) digestion. Protein modifications (PMs) were screened with commercially available PM-specific antibodies. Specific proteins at 20, 37, 50, and 65 kDa react to more than 3 PM-specific antibodies among meat proteins. Lysine methylation and methionine oxidation were the most prominent PMs in WB. Mass spectrometry confirmed bands at ≈20 kDa as allergenic proteins: sarcoplasmic calcium-binding protein in oyster, 37 kDa as tropomyosin in shrimp, oyster, and abalone. MS-identified PMs of shellfish allergens were aligned to the IgE binding epitopes. GI digestion-resistant peptides of shellfish proteins were identified as paramyosins in oyster and abalone and SBP in shrimp. Our results point to the high susceptibility of immunodominant epitopes of major shellfish allergens to PMs. In TPM, saturation of oxidative modification increases with thermal processing resulting in higher susceptibility of TPM to gastric digestion.
PB  - Elsevier
T2  - Journal of Functional Foods
T1  - Protein modifications screening of raw and thermally treated meat gastrointestinal digesta
VL  - 113
SP  - 106052
DO  - 10.1016/j.jff.2024.106052
ER  - 

@article{
author = "Khulal, Urmila and Đukić, Teodora and Smiljanić, Katarina and Vasović, Tamara and Aćimović, Jelena and Rajković, Andreja and Ćirković Veličković, Tanja",
year = "2024",
abstract = "Meat samples were subjected to thermal processing combined with simulated INFOGEST in vitro gastrointestinal (GI) digestion. Protein modifications (PMs) were screened with commercially available PM-specific antibodies. Specific proteins at 20, 37, 50, and 65 kDa react to more than 3 PM-specific antibodies among meat proteins. Lysine methylation and methionine oxidation were the most prominent PMs in WB. Mass spectrometry confirmed bands at ≈20 kDa as allergenic proteins: sarcoplasmic calcium-binding protein in oyster, 37 kDa as tropomyosin in shrimp, oyster, and abalone. MS-identified PMs of shellfish allergens were aligned to the IgE binding epitopes. GI digestion-resistant peptides of shellfish proteins were identified as paramyosins in oyster and abalone and SBP in shrimp. Our results point to the high susceptibility of immunodominant epitopes of major shellfish allergens to PMs. In TPM, saturation of oxidative modification increases with thermal processing resulting in higher susceptibility of TPM to gastric digestion.",
publisher = "Elsevier",
journal = "Journal of Functional Foods",
title = "Protein modifications screening of raw and thermally treated meat gastrointestinal digesta",
volume = "113",
pages = "106052",
doi = "10.1016/j.jff.2024.106052"
}

Khulal, U., Đukić, T., Smiljanić, K., Vasović, T., Aćimović, J., Rajković, A.,& Ćirković Veličković, T.. (2024). Protein modifications screening of raw and thermally treated meat gastrointestinal digesta. in Journal of Functional Foods
Elsevier., 113, 106052.
https://doi.org/10.1016/j.jff.2024.106052

Khulal U, Đukić T, Smiljanić K, Vasović T, Aćimović J, Rajković A, Ćirković Veličković T. Protein modifications screening of raw and thermally treated meat gastrointestinal digesta. in Journal of Functional Foods. 2024;113:106052.
doi:10.1016/j.jff.2024.106052 .

Khulal, Urmila, Đukić, Teodora, Smiljanić, Katarina, Vasović, Tamara, Aćimović, Jelena, Rajković, Andreja, Ćirković Veličković, Tanja, "Protein modifications screening of raw and thermally treated meat gastrointestinal digesta" in Journal of Functional Foods, 113 (2024):106052,
https://doi.org/10.1016/j.jff.2024.106052 . .

TY  - JOUR
AU  - Nedić, Olgica
AU  - Penezić, Ana
AU  - Minić, Simeon
AU  - Radomirović, Mirjana Ž.
AU  - Nikolić, Milan
AU  - Ćirković Veličković, Tanja
AU  - Gligorijević, Nikola
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6028
AB  - Common to all biological systems and living organisms are molecular interactions, which
may lead to specific physiological events. Most often, a cascade of events occurs, establishing an equilibrium between possibly competing and/or synergistic processes. Biochemical pathways that sustain life depend on multiple intrinsic and extrinsic factors contributing to aging and/or diseases. This article deals with food antioxidants and human proteins from the circulation, their interaction, their effect on the structure, properties, and function of antioxidant-bound proteins, and the possible impact of complex formation on antioxidants. An overview of studies examining interactions between individual antioxidant compounds and major blood proteins is presented with findings. Investigating antioxidant/protein interactions at the level of the human organism and determining antioxidant distribution between proteins and involvement in the particular physiological role is a very complex and challenging task. However, by knowing the role of a particular protein in certain pathology or aging, and the effect exerted by a particular antioxidant bound to it, it is possible to recommend specific food intake or resistance to it to improve the condition or slow down the process.
PB  - MDPI
T2  - Antioxidants
T1  - Food Antioxidants and Their Interaction with Human Proteins
VL  - 12
IS  - 4
SP  - 815
DO  - 10.3390/antiox12040815
ER  - 

@article{
author = "Nedić, Olgica and Penezić, Ana and Minić, Simeon and Radomirović, Mirjana Ž. and Nikolić, Milan and Ćirković Veličković, Tanja and Gligorijević, Nikola",
year = "2023",
abstract = "Common to all biological systems and living organisms are molecular interactions, which
may lead to specific physiological events. Most often, a cascade of events occurs, establishing an equilibrium between possibly competing and/or synergistic processes. Biochemical pathways that sustain life depend on multiple intrinsic and extrinsic factors contributing to aging and/or diseases. This article deals with food antioxidants and human proteins from the circulation, their interaction, their effect on the structure, properties, and function of antioxidant-bound proteins, and the possible impact of complex formation on antioxidants. An overview of studies examining interactions between individual antioxidant compounds and major blood proteins is presented with findings. Investigating antioxidant/protein interactions at the level of the human organism and determining antioxidant distribution between proteins and involvement in the particular physiological role is a very complex and challenging task. However, by knowing the role of a particular protein in certain pathology or aging, and the effect exerted by a particular antioxidant bound to it, it is possible to recommend specific food intake or resistance to it to improve the condition or slow down the process.",
publisher = "MDPI",
journal = "Antioxidants",
title = "Food Antioxidants and Their Interaction with Human Proteins",
volume = "12",
number = "4",
pages = "815",
doi = "10.3390/antiox12040815"
}

Nedić, O., Penezić, A., Minić, S., Radomirović, M. Ž., Nikolić, M., Ćirković Veličković, T.,& Gligorijević, N.. (2023). Food Antioxidants and Their Interaction with Human Proteins. in Antioxidants
MDPI., 12(4), 815.
https://doi.org/10.3390/antiox12040815

Nedić O, Penezić A, Minić S, Radomirović MŽ, Nikolić M, Ćirković Veličković T, Gligorijević N. Food Antioxidants and Their Interaction with Human Proteins. in Antioxidants. 2023;12(4):815.
doi:10.3390/antiox12040815 .

Nedić, Olgica, Penezić, Ana, Minić, Simeon, Radomirović, Mirjana Ž., Nikolić, Milan, Ćirković Veličković, Tanja, Gligorijević, Nikola, "Food Antioxidants and Their Interaction with Human Proteins" in Antioxidants, 12, no. 4 (2023):815,
https://doi.org/10.3390/antiox12040815 . .

TY  - JOUR
AU  - Veličković, Luka
AU  - Simović, Ana
AU  - Gligorijević, Nikola
AU  - Thureau, Aurélien
AU  - Obradović, Milica
AU  - Vasović, Tamara
AU  - Sotiroudis, Georgios
AU  - Zoumpanioti, Maria
AU  - Brûlet, Annie
AU  - Ćirković Veličković, Tanja
AU  - Combet, Sophie
AU  - Nikolić, Milan
AU  - Minić, Simeon
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6273
AB  - This study aimed to purify, characterise and stabilise the natural food colourant, R-phycocyanin (R-PC), from the red algae Porphyra spp. (Nori). We purified R-PC from dried Nori flakes with a high purity ratio (A618/A280 ≥ 3.4) in native form (α-helix content 53%). SAXS measurements revealed that R-PC is trimeric ((αβ)3) in solution. The thermal denaturation of α-helix revealed one transition (Tm at 52 °C), while the pH stability study showed R-PC is stable in the pH range 4–8. The thermal treatment of R-PC at 60 °C has detrimental and irreversible effects on R-PC colour and antioxidant capacity (22 % of residual capacity). However, immobilisation of R-PC within calcium alginate beads completely preserves R-PC colour and mainly retains its antioxidant ability (78 % of residual capacity). Results give new insights into the stability of R-PC and preservation of its purple colour and bioactivity by encapsulation in calcium alginate beads.
PB  - Elsevier
T2  - Food Chemistry
T1  - Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant
VL  - 426
SP  - 136669
DO  - 10.1016/j.foodchem.2023.136669
ER  - 

@article{
author = "Veličković, Luka and Simović, Ana and Gligorijević, Nikola and Thureau, Aurélien and Obradović, Milica and Vasović, Tamara and Sotiroudis, Georgios and Zoumpanioti, Maria and Brûlet, Annie and Ćirković Veličković, Tanja and Combet, Sophie and Nikolić, Milan and Minić, Simeon",
year = "2023",
abstract = "This study aimed to purify, characterise and stabilise the natural food colourant, R-phycocyanin (R-PC), from the red algae Porphyra spp. (Nori). We purified R-PC from dried Nori flakes with a high purity ratio (A618/A280 ≥ 3.4) in native form (α-helix content 53%). SAXS measurements revealed that R-PC is trimeric ((αβ)3) in solution. The thermal denaturation of α-helix revealed one transition (Tm at 52 °C), while the pH stability study showed R-PC is stable in the pH range 4–8. The thermal treatment of R-PC at 60 °C has detrimental and irreversible effects on R-PC colour and antioxidant capacity (22 % of residual capacity). However, immobilisation of R-PC within calcium alginate beads completely preserves R-PC colour and mainly retains its antioxidant ability (78 % of residual capacity). Results give new insights into the stability of R-PC and preservation of its purple colour and bioactivity by encapsulation in calcium alginate beads.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant",
volume = "426",
pages = "136669",
doi = "10.1016/j.foodchem.2023.136669"
}

Veličković, L., Simović, A., Gligorijević, N., Thureau, A., Obradović, M., Vasović, T., Sotiroudis, G., Zoumpanioti, M., Brûlet, A., Ćirković Veličković, T., Combet, S., Nikolić, M.,& Minić, S.. (2023). Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant. in Food Chemistry
Elsevier., 426, 136669.
https://doi.org/10.1016/j.foodchem.2023.136669

Veličković L, Simović A, Gligorijević N, Thureau A, Obradović M, Vasović T, Sotiroudis G, Zoumpanioti M, Brûlet A, Ćirković Veličković T, Combet S, Nikolić M, Minić S. Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant. in Food Chemistry. 2023;426:136669.
doi:10.1016/j.foodchem.2023.136669 .

Veličković, Luka, Simović, Ana, Gligorijević, Nikola, Thureau, Aurélien, Obradović, Milica, Vasović, Tamara, Sotiroudis, Georgios, Zoumpanioti, Maria, Brûlet, Annie, Ćirković Veličković, Tanja, Combet, Sophie, Nikolić, Milan, Minić, Simeon, "Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant" in Food Chemistry, 426 (2023):136669,
https://doi.org/10.1016/j.foodchem.2023.136669 . .

TY  - JOUR
AU  - Veličković, Luka
AU  - Simović, Ana
AU  - Gligorijević, Nikola
AU  - Thureau, Aurelien
AU  - Obradović, Milica
AU  - Vasović, Tamara
AU  - Sotiroudis, Georgios
AU  - Zoumpanioti, Maria
AU  - Brûlet, Annie
AU  - Ćirković Veličković, Tanja
AU  - Combet, Sophie
AU  - Nikolić, Milan
AU  - Minić, Simeon
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6420
AB  - This study aimed to purify, characterise and stabilise the natural food colourant, R-phycocyanin (R-PC), from thered algae Porphyra spp. (Nori). We purified R-PC from dried Nori flakes with a high purity ratio (A618/A280 ≥ 3.4)in native form (α-helix content 53%). SAXS measurements revealed that R-PC is trimeric ((αβ)3) in solution. Thethermal denaturation of α-helix revealed one transition (Tm at 52 ◦C), while the pH stability study showed R-PC isstable in the pH range 4–8. The thermal treatment of R-PC at 60 ◦C has detrimental and irreversible effects on RPCcolour and antioxidant capacity (22 % of residual capacity). However, immobilisation of R-PC within calciumalginate beads completely preserves R-PC colour and mainly retains its antioxidant ability (78 % of residualcapacity). Results give new insights into the stability of R-PC and preservation of its purple colour and bioactivityby encapsulation in calcium alginate beads.
PB  - Elsevier
T2  - Food Chemistry
T1  - Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant
VL  - 426
SP  - 136669
DO  - 10.1016/j.foodchem.2023.136669
ER  - 

@article{
author = "Veličković, Luka and Simović, Ana and Gligorijević, Nikola and Thureau, Aurelien and Obradović, Milica and Vasović, Tamara and Sotiroudis, Georgios and Zoumpanioti, Maria and Brûlet, Annie and Ćirković Veličković, Tanja and Combet, Sophie and Nikolić, Milan and Minić, Simeon",
year = "2023",
abstract = "This study aimed to purify, characterise and stabilise the natural food colourant, R-phycocyanin (R-PC), from thered algae Porphyra spp. (Nori). We purified R-PC from dried Nori flakes with a high purity ratio (A618/A280 ≥ 3.4)in native form (α-helix content 53%). SAXS measurements revealed that R-PC is trimeric ((αβ)3) in solution. Thethermal denaturation of α-helix revealed one transition (Tm at 52 ◦C), while the pH stability study showed R-PC isstable in the pH range 4–8. The thermal treatment of R-PC at 60 ◦C has detrimental and irreversible effects on RPCcolour and antioxidant capacity (22 % of residual capacity). However, immobilisation of R-PC within calciumalginate beads completely preserves R-PC colour and mainly retains its antioxidant ability (78 % of residualcapacity). Results give new insights into the stability of R-PC and preservation of its purple colour and bioactivityby encapsulation in calcium alginate beads.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant",
volume = "426",
pages = "136669",
doi = "10.1016/j.foodchem.2023.136669"
}

Veličković, L., Simović, A., Gligorijević, N., Thureau, A., Obradović, M., Vasović, T., Sotiroudis, G., Zoumpanioti, M., Brûlet, A., Ćirković Veličković, T., Combet, S., Nikolić, M.,& Minić, S.. (2023). Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant. in Food Chemistry
Elsevier., 426, 136669.
https://doi.org/10.1016/j.foodchem.2023.136669

Veličković L, Simović A, Gligorijević N, Thureau A, Obradović M, Vasović T, Sotiroudis G, Zoumpanioti M, Brûlet A, Ćirković Veličković T, Combet S, Nikolić M, Minić S. Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant. in Food Chemistry. 2023;426:136669.
doi:10.1016/j.foodchem.2023.136669 .

Veličković, Luka, Simović, Ana, Gligorijević, Nikola, Thureau, Aurelien, Obradović, Milica, Vasović, Tamara, Sotiroudis, Georgios, Zoumpanioti, Maria, Brûlet, Annie, Ćirković Veličković, Tanja, Combet, Sophie, Nikolić, Milan, Minić, Simeon, "Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant" in Food Chemistry, 426 (2023):136669,
https://doi.org/10.1016/j.foodchem.2023.136669 . .

TY  - CONF
AU  - Đukić, Teodora
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Ćirković Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6538
AB  - A bottom-up proteomic study, using high-resolution tandem mass spectrometry (HRMS) and, PEAKS Studio X+ was performed to investigate the impact of peanut roasting on readily soluble allergens and their post-translational modification (PTM) profiles. Among four major peanut allergen groups, we found that Ara h 3 prevails in raw peanut extract (PE), similar to Ara h 1, while the opposite is true for Ara h 6, which is enriched in roasted PE; Ara h 2 bands are near the same intensity. HRMS detected more than 40 different types of modification in raw and roasted samples. Distinct variations in the types and occurrence of specific amino acid PTMs were identified between allergens present in raw and roasted samples. Roasting affected the most frequent modifications by enrichment of Ox, HyP, carbamoylation (KR), and deamidation. The PMs could also be mapped to the regions of IgE-binding epitopes of Ara h 1-3 and Ara h 6. As porcine trypsin is used for HRMS sample preparation and is also a digestive protease, hindrance effects to trypsin efficacy regarding PTMs were assessed. Roasting caused dihydroxylation and formylation PTMs with hindrance effects to trypsin efficacy, while methylation on several K/R showed opposite effects. In the case of methylated R342, results suggested facilitation of tryptic performance at modified residue compared to unmodified counterpart, while in the rest of the seven genuine sequences containing modified residues, the trend was opposite. Further exploration of how different PTMs could affect digestion efficiencies of major gastric and intestinal peptidases is currently in works and a much-needed assessment to better understand the role of PTMs.
PB  - Faculty of Chemistry, Serbian Chemical Society
C3  - Book of Abstracts, Serbian Biochemical Society Twelfth Conference "Bicehemistry in Biotechnology", September 21st, 2023
T1  - Mass spectrometry analysis reveals impact of peanut roasting on post-translational modifications of key allergens and  their hinderance of trypsin digestion
SP  - 146
EP  - 146
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6538
ER  - 

@conference{
author = "Đukić, Teodora and Smiljanić, Katarina and Prodić, Ivana and Ćirković Veličković, Tanja",
year = "2023",
abstract = "A bottom-up proteomic study, using high-resolution tandem mass spectrometry (HRMS) and, PEAKS Studio X+ was performed to investigate the impact of peanut roasting on readily soluble allergens and their post-translational modification (PTM) profiles. Among four major peanut allergen groups, we found that Ara h 3 prevails in raw peanut extract (PE), similar to Ara h 1, while the opposite is true for Ara h 6, which is enriched in roasted PE; Ara h 2 bands are near the same intensity. HRMS detected more than 40 different types of modification in raw and roasted samples. Distinct variations in the types and occurrence of specific amino acid PTMs were identified between allergens present in raw and roasted samples. Roasting affected the most frequent modifications by enrichment of Ox, HyP, carbamoylation (KR), and deamidation. The PMs could also be mapped to the regions of IgE-binding epitopes of Ara h 1-3 and Ara h 6. As porcine trypsin is used for HRMS sample preparation and is also a digestive protease, hindrance effects to trypsin efficacy regarding PTMs were assessed. Roasting caused dihydroxylation and formylation PTMs with hindrance effects to trypsin efficacy, while methylation on several K/R showed opposite effects. In the case of methylated R342, results suggested facilitation of tryptic performance at modified residue compared to unmodified counterpart, while in the rest of the seven genuine sequences containing modified residues, the trend was opposite. Further exploration of how different PTMs could affect digestion efficiencies of major gastric and intestinal peptidases is currently in works and a much-needed assessment to better understand the role of PTMs.",
publisher = "Faculty of Chemistry, Serbian Chemical Society",
journal = "Book of Abstracts, Serbian Biochemical Society Twelfth Conference "Bicehemistry in Biotechnology", September 21st, 2023",
title = "Mass spectrometry analysis reveals impact of peanut roasting on post-translational modifications of key allergens and  their hinderance of trypsin digestion",
pages = "146-146",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6538"
}

Đukić, T., Smiljanić, K., Prodić, I.,& Ćirković Veličković, T.. (2023). Mass spectrometry analysis reveals impact of peanut roasting on post-translational modifications of key allergens and  their hinderance of trypsin digestion. in Book of Abstracts, Serbian Biochemical Society Twelfth Conference "Bicehemistry in Biotechnology", September 21st, 2023
Faculty of Chemistry, Serbian Chemical Society., 146-146.
https://hdl.handle.net/21.15107/rcub_cherry_6538

Đukić T, Smiljanić K, Prodić I, Ćirković Veličković T. Mass spectrometry analysis reveals impact of peanut roasting on post-translational modifications of key allergens and  their hinderance of trypsin digestion. in Book of Abstracts, Serbian Biochemical Society Twelfth Conference "Bicehemistry in Biotechnology", September 21st, 2023. 2023;:146-146.
https://hdl.handle.net/21.15107/rcub_cherry_6538 .

Đukić, Teodora, Smiljanić, Katarina, Prodić, Ivana, Ćirković Veličković, Tanja, "Mass spectrometry analysis reveals impact of peanut roasting on post-translational modifications of key allergens and  their hinderance of trypsin digestion" in Book of Abstracts, Serbian Biochemical Society Twelfth Conference "Bicehemistry in Biotechnology", September 21st, 2023 (2023):146-146,
https://hdl.handle.net/21.15107/rcub_cherry_6538 .

TY  - JOUR
AU  - Djapovic, Milica
AU  - Apostolović, Danijela
AU  - Postic, Vojislava
AU  - Lujić, Tamara
AU  - Jovanović, Vesna B.
AU  - Stanić-Vučinić, Dragana
AU  - van Hage, Marianne
AU  - Maslak, Veselin
AU  - Ćirković Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6433
AB  - Manufactured nanoplastic particles (NPs) are indispensable for in vitro and in vivo testing and a health risk assessment of this emerging environmental contaminant is needed. The high surface area and inherent hydrophobicity of plastic materials makes the production of NPs devoid of any contaminants very challenging. In this study, we produced nanoprecipitated polyethylene terephthalate (PET) NPs (300 nm hydrodynamic diameter) with an overall yield of 0.76%. The presence of the ionic surfactant sodium dodecyl sulfate (SDS) was characterized by 1H NMR, where the relative ratio of NP/surfactant was monitored on the basis of the chemical shifts characteristic of PET and SDS. For a wide range of surfactant/NP ratios (17:100 to 1.2:100), the measured zeta potential changed from −42.10 to −34.93 mV, but with an NP concentration up to 100 μg/mL, no clear differences were observed in the cellular assays performed in protein-rich media on primary human cells. The remaining impurities contributed to the outcome of the biological assays applied in protein-free buffers, such as human red blood cell hemolysis. The presence of SDS increased the NP-induced hemolysis by 1.5% in protein-rich buffer and by 7.5% in protein-free buffer. As the size, shape, zeta potential, and contaminants of NPs may all be relevant parameters for the biological effects of NPs, the relative quantification of impurities exemplified in our work by the application of 1H NMR for PET NPs and the ionic surfactant SDS could be a valuable auxiliary method in the quality control of manufactured NPs.
PB  - MDPI
T2  - Polymers
T1  - Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes
VL  - 15
IS  - 24
SP  - 4703
DO  - 10.3390/polym15244703
ER  - 

@article{
author = "Djapovic, Milica and Apostolović, Danijela and Postic, Vojislava and Lujić, Tamara and Jovanović, Vesna B. and Stanić-Vučinić, Dragana and van Hage, Marianne and Maslak, Veselin and Ćirković Veličković, Tanja",
year = "2023",
abstract = "Manufactured nanoplastic particles (NPs) are indispensable for in vitro and in vivo testing and a health risk assessment of this emerging environmental contaminant is needed. The high surface area and inherent hydrophobicity of plastic materials makes the production of NPs devoid of any contaminants very challenging. In this study, we produced nanoprecipitated polyethylene terephthalate (PET) NPs (300 nm hydrodynamic diameter) with an overall yield of 0.76%. The presence of the ionic surfactant sodium dodecyl sulfate (SDS) was characterized by 1H NMR, where the relative ratio of NP/surfactant was monitored on the basis of the chemical shifts characteristic of PET and SDS. For a wide range of surfactant/NP ratios (17:100 to 1.2:100), the measured zeta potential changed from −42.10 to −34.93 mV, but with an NP concentration up to 100 μg/mL, no clear differences were observed in the cellular assays performed in protein-rich media on primary human cells. The remaining impurities contributed to the outcome of the biological assays applied in protein-free buffers, such as human red blood cell hemolysis. The presence of SDS increased the NP-induced hemolysis by 1.5% in protein-rich buffer and by 7.5% in protein-free buffer. As the size, shape, zeta potential, and contaminants of NPs may all be relevant parameters for the biological effects of NPs, the relative quantification of impurities exemplified in our work by the application of 1H NMR for PET NPs and the ionic surfactant SDS could be a valuable auxiliary method in the quality control of manufactured NPs.",
publisher = "MDPI",
journal = "Polymers",
title = "Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes",
volume = "15",
number = "24",
pages = "4703",
doi = "10.3390/polym15244703"
}

Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V. B., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers
MDPI., 15(24), 4703.
https://doi.org/10.3390/polym15244703

Djapovic M, Apostolović D, Postic V, Lujić T, Jovanović VB, Stanić-Vučinić D, van Hage M, Maslak V, Ćirković Veličković T. Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers. 2023;15(24):4703.
doi:10.3390/polym15244703 .

Djapovic, Milica, Apostolović, Danijela, Postic, Vojislava, Lujić, Tamara, Jovanović, Vesna B., Stanić-Vučinić, Dragana, van Hage, Marianne, Maslak, Veselin, Ćirković Veličković, Tanja, "Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes" in Polymers, 15, no. 24 (2023):4703,
https://doi.org/10.3390/polym15244703 . .

TY  - DATA
AU  - Đapović, Milica
AU  - Apostolović, Danijela
AU  - Postić, Vojislava
AU  - Lujić, Tamara
AU  - Jovanović, Vesna B.
AU  - Stanić-Vučinić, Dragana
AU  - Van Hage, Marianne
AU  - Maslak, Veselin
AU  - Ćirković Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6460
AB  - Percentage of hemolysis of RBC in the presence of washed PET NPs and
unwashed NPs (with SDS) determined by incubation of human red blood cells (RBCs) from
three healthy donors. Output from the  Shimadzu UV/ViS 1800 (Kyoto, Japan) nspectrometer - raw spectral data and the calculation of percentages of hemolysis (procesesd data).
PB  - MDPI
T2  - Polymers
T1  - Research data no.1 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers
MDPI., 15(24), 4703.
https://doi.org/10.3390/polym15244703
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6460
ER  - 

@misc{
author = "Đapović, Milica and Apostolović, Danijela and Postić, Vojislava and Lujić, Tamara and Jovanović, Vesna B. and Stanić-Vučinić, Dragana and Van Hage, Marianne and Maslak, Veselin and Ćirković Veličković, Tanja",
year = "2023",
abstract = "Percentage of hemolysis of RBC in the presence of washed PET NPs and
unwashed NPs (with SDS) determined by incubation of human red blood cells (RBCs) from
three healthy donors. Output from the  Shimadzu UV/ViS 1800 (Kyoto, Japan) nspectrometer - raw spectral data and the calculation of percentages of hemolysis (procesesd data).",
publisher = "MDPI",
journal = "Polymers",
title = "Research data no.1 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers
MDPI., 15(24), 4703.
https://doi.org/10.3390/polym15244703",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6460"
}

Đapović, M., Apostolović, D., Postić, V., Lujić, T., Jovanović, V. B., Stanić-Vučinić, D., Van Hage, M., Maslak, V.,& Ćirković Veličković, T.. (2023). Research data no.1 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers
MDPI., 15(24), 4703.
https://doi.org/10.3390/polym15244703. in Polymers
MDPI..
https://hdl.handle.net/21.15107/rcub_cherry_6460

Đapović M, Apostolović D, Postić V, Lujić T, Jovanović VB, Stanić-Vučinić D, Van Hage M, Maslak V, Ćirković Veličković T. Research data no.1 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers
MDPI., 15(24), 4703.
https://doi.org/10.3390/polym15244703. in Polymers. 2023;.
https://hdl.handle.net/21.15107/rcub_cherry_6460 .

Đapović, Milica, Apostolović, Danijela, Postić, Vojislava, Lujić, Tamara, Jovanović, Vesna B., Stanić-Vučinić, Dragana, Van Hage, Marianne, Maslak, Veselin, Ćirković Veličković, Tanja, "Research data no.1 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers
MDPI., 15(24), 4703.
https://doi.org/10.3390/polym15244703" in Polymers (2023),
https://hdl.handle.net/21.15107/rcub_cherry_6460 .

TY  - DATA
AU  - Đapović, Milica
AU  - Apostolović, Danijela
AU  - Poštić, Vojislava
AU  - Lujić, Tamara
AU  - Jovanović, Vesna B.
AU  - Stanić-Vučinić, Dragana
AU  - van Hage, Marianne
AU  - Maslak, Veselin
AU  - Ćirković Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6464
AB  - Determination of hydrodynamic diameter of PET NPs washed and dispersed in water, BSA (0.05%), and SDS (0.1%), and NPs unwashed and dispersed in water.  Zeta potential, mobility, and conductivity determination in PET NPs at different stages of purification. Output from the Malvern zetasizer Nano-ZS ZEN 3600 (Malvern Panalytical, Malvern, UK).
PB  - MDPI
T2  - Polymers
T1  - Research data no. 2 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers MDPI., 15(24), 4703. https://doi.org/10.3390/polym15244703
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6464
ER  - 

@misc{
author = "Đapović, Milica and Apostolović, Danijela and Poštić, Vojislava and Lujić, Tamara and Jovanović, Vesna B. and Stanić-Vučinić, Dragana and van Hage, Marianne and Maslak, Veselin and Ćirković Veličković, Tanja",
year = "2023",
abstract = "Determination of hydrodynamic diameter of PET NPs washed and dispersed in water, BSA (0.05%), and SDS (0.1%), and NPs unwashed and dispersed in water.  Zeta potential, mobility, and conductivity determination in PET NPs at different stages of purification. Output from the Malvern zetasizer Nano-ZS ZEN 3600 (Malvern Panalytical, Malvern, UK).",
publisher = "MDPI",
journal = "Polymers",
title = "Research data no. 2 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers MDPI., 15(24), 4703. https://doi.org/10.3390/polym15244703",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6464"
}

Đapović, M., Apostolović, D., Poštić, V., Lujić, T., Jovanović, V. B., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković Veličković, T.. (2023). Research data no. 2 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers MDPI., 15(24), 4703. https://doi.org/10.3390/polym15244703. in Polymers
MDPI..
https://hdl.handle.net/21.15107/rcub_cherry_6464

Đapović M, Apostolović D, Poštić V, Lujić T, Jovanović VB, Stanić-Vučinić D, van Hage M, Maslak V, Ćirković Veličković T. Research data no. 2 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers MDPI., 15(24), 4703. https://doi.org/10.3390/polym15244703. in Polymers. 2023;.
https://hdl.handle.net/21.15107/rcub_cherry_6464 .

Đapović, Milica, Apostolović, Danijela, Poštić, Vojislava, Lujić, Tamara, Jovanović, Vesna B., Stanić-Vučinić, Dragana, van Hage, Marianne, Maslak, Veselin, Ćirković Veličković, Tanja, "Research data no. 2 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers MDPI., 15(24), 4703. https://doi.org/10.3390/polym15244703" in Polymers (2023),
https://hdl.handle.net/21.15107/rcub_cherry_6464 .

TY  - DATA
AU  - Đapović, Milica
AU  - Apostolović, Danijela
AU  - Poštić, Vojislava
AU  - Lujić, Tamara
AU  - Jovanović, Vesna B.
AU  - Stanić-Vučinić, Dragana
AU  - van Hage, Marianne
AU  - Maslak, Veselin
AU  - Ćirković Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6467
AB  - The presence of the ionic surfactant sodium dodecyl sulfate (SDS) was characterized by 1H NMR, where the relative ratio of NP/surfactant was monitored on the basis of the chemical shifts characteristic of PET and SDS. 1H NMR spectra of the NPs preparation before and during all the washing steps. Determination of SDS Level in Corona of PET NPs by 1H NMR. Output from the Varian/Agilent NMR 400 MHz. NMR spectra were processed in Mnova software.
PB  - MDPI
T2  - Polymers
T1  - Research data no. 3 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers MDPI., 15(24), 4703. https://doi.org/10.3390/polym15244703
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6467
ER  - 

@misc{
author = "Đapović, Milica and Apostolović, Danijela and Poštić, Vojislava and Lujić, Tamara and Jovanović, Vesna B. and Stanić-Vučinić, Dragana and van Hage, Marianne and Maslak, Veselin and Ćirković Veličković, Tanja",
year = "2023",
abstract = "The presence of the ionic surfactant sodium dodecyl sulfate (SDS) was characterized by 1H NMR, where the relative ratio of NP/surfactant was monitored on the basis of the chemical shifts characteristic of PET and SDS. 1H NMR spectra of the NPs preparation before and during all the washing steps. Determination of SDS Level in Corona of PET NPs by 1H NMR. Output from the Varian/Agilent NMR 400 MHz. NMR spectra were processed in Mnova software.",
publisher = "MDPI",
journal = "Polymers",
title = "Research data no. 3 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers MDPI., 15(24), 4703. https://doi.org/10.3390/polym15244703",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6467"
}

Đapović, M., Apostolović, D., Poštić, V., Lujić, T., Jovanović, V. B., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković Veličković, T.. (2023). Research data no. 3 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers MDPI., 15(24), 4703. https://doi.org/10.3390/polym15244703. in Polymers
MDPI..
https://hdl.handle.net/21.15107/rcub_cherry_6467

Đapović M, Apostolović D, Poštić V, Lujić T, Jovanović VB, Stanić-Vučinić D, van Hage M, Maslak V, Ćirković Veličković T. Research data no. 3 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers MDPI., 15(24), 4703. https://doi.org/10.3390/polym15244703. in Polymers. 2023;.
https://hdl.handle.net/21.15107/rcub_cherry_6467 .

Đapović, Milica, Apostolović, Danijela, Poštić, Vojislava, Lujić, Tamara, Jovanović, Vesna B., Stanić-Vučinić, Dragana, van Hage, Marianne, Maslak, Veselin, Ćirković Veličković, Tanja, "Research data no. 3 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers MDPI., 15(24), 4703. https://doi.org/10.3390/polym15244703" in Polymers (2023),
https://hdl.handle.net/21.15107/rcub_cherry_6467 .

TY  - DATA
AU  - Đapović, Milica
AU  - Apostolović, Danijela
AU  - Poštić, Vojislava
AU  - Lujić, Tamara
AU  - Jovanović, Vesna B.
AU  - Stanić-Vučinić, Dragana
AU  - van Hage, Marianne
AU  - Maslak, Veselin
AU  - Ćirković Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6468
AB  - Size distributions (by intensity percentage) of NPs washed suspended in different dispersants, water,BSA (0.05%),SDS (0.1 %). Distributions data from different combined fractions: from NP-10 to NP-30; from NP-40 to NP-60 and from NP-70 to NP-90. Output from the Malvern zetasizer Nano-ZS ZEN 3600 (Malvern Panalytical, Malvern, UK).
PB  - MDPI
T2  - Polymers
T1  - Research data no. 4 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers MDPI., 15(24), 4703. https://doi.org/10.3390/polym15244703
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6468
ER  - 

@misc{
author = "Đapović, Milica and Apostolović, Danijela and Poštić, Vojislava and Lujić, Tamara and Jovanović, Vesna B. and Stanić-Vučinić, Dragana and van Hage, Marianne and Maslak, Veselin and Ćirković Veličković, Tanja",
year = "2023",
abstract = "Size distributions (by intensity percentage) of NPs washed suspended in different dispersants, water,BSA (0.05%),SDS (0.1 %). Distributions data from different combined fractions: from NP-10 to NP-30; from NP-40 to NP-60 and from NP-70 to NP-90. Output from the Malvern zetasizer Nano-ZS ZEN 3600 (Malvern Panalytical, Malvern, UK).",
publisher = "MDPI",
journal = "Polymers",
title = "Research data no. 4 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers MDPI., 15(24), 4703. https://doi.org/10.3390/polym15244703",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6468"
}

Đapović, M., Apostolović, D., Poštić, V., Lujić, T., Jovanović, V. B., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković Veličković, T.. (2023). Research data no. 4 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers MDPI., 15(24), 4703. https://doi.org/10.3390/polym15244703. in Polymers
MDPI..
https://hdl.handle.net/21.15107/rcub_cherry_6468

Đapović M, Apostolović D, Poštić V, Lujić T, Jovanović VB, Stanić-Vučinić D, van Hage M, Maslak V, Ćirković Veličković T. Research data no. 4 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers MDPI., 15(24), 4703. https://doi.org/10.3390/polym15244703. in Polymers. 2023;.
https://hdl.handle.net/21.15107/rcub_cherry_6468 .

Đapović, Milica, Apostolović, Danijela, Poštić, Vojislava, Lujić, Tamara, Jovanović, Vesna B., Stanić-Vučinić, Dragana, van Hage, Marianne, Maslak, Veselin, Ćirković Veličković, Tanja, "Research data no. 4 for: Djapovic, M., Apostolović, D., Postic, V., Lujić, T., Jovanović, V., Stanić-Vučinić, D., van Hage, M., Maslak, V.,& Ćirković-Veličković, T.. (2023). Characterization of Nanoprecipitated PET Nanoplastics by 1H NMR and Impact of Residual Ionic Surfactant on Viability of Human Primary Mononuclear Cells and Hemolysis of Erythrocytes. in Polymers MDPI., 15(24), 4703. https://doi.org/10.3390/polym15244703" in Polymers (2023),
https://hdl.handle.net/21.15107/rcub_cherry_6468 .

TY  - GEN
AU  - Ćirković Veličković, Tanja
AU  - Gnjatović, Marija
AU  - Ćujić, Danica
AU  - Todorović, Aleksandra
AU  - Stanić-Vučinić, Dragana
AU  - Đukić, Teodora
AU  - Mladenović, Maja
AU  - Vasović, Tamara
AU  - Stojadinović, Marija
AU  - Krstić-Ristivojević, Maja
AU  - Jovanović, Vesna B.
AU  - Simović, Ana
AU  - Radosavljević, Jelena
AU  - Aćimović, Jelena M.
AU  - Radomirović, Mirjana Ž.
AU  - Stojanović, Marijana
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6014
AB  - Нови корона вирус (SARS CoV-2) који се појавио у Вухану 2019. године припада групи једноланчаних РНК вируса [1]. Представља нови инфективни агенс за хуману популацију и веома је брзо детектован у великом броју земаља. Узрочник је респираторних инфекција које могу да буду праћене и веома тешком клиничком сликом. Брзо ширење, одсуство имунитета на овај вирус и одсуство поузданих тестова за детекцију вируса у тренутку избијања пандемије су болест изазвану овим вирусом брзо претворили у здравствени и друштвени проблем највишег приоритета на глобалном нивоу. Иако су највеће биотехнолошке компаније убрзано почеле са развојем и масовном производњом дијагностичких тестова и вакцина, њихова доступност у тренуцима највеће потражње је и даље недовољна, а цене истих су лимитирајући фактор за бољу контролу болести и ширења пандемије [2]. Развој сопствених и одржива производња тестова и вакцина за COVID-19 су од великог друштвеног значаја. Важан предуслов за одрживу производњу тестова је доступност рекомбинантних антигена вируса и могућност производње истих на великој скали за потребе производње домаћих тестова. Овим техничким решењем се описује добијање два кључна антигена новог корона вируса рекомбинантном технологијом и њихова примена у серолошком ЕЛИСА тесту који производи Институт за примену нуклеарне енергије, ИНЕП, као и за добијање реагенаса за детекцију антигена новог корона вируса (специфичних антитела). У првој фази, оптимизоване су секвенце протеина које су подигле осетљивост постојећих серолошких тестова. Иновативност нашег приступа се огледа и у разрађеним експерименталним протоколима за добијање рекомбинантних протеина нуклеокапсида на великој скали, као и у солубилној форми, што олакшава поступак пречишћавања. Избор фрагмента нуклеокапсида који се хетеролого експримира у солубилној форми, а специфично детектује антитела и генерише јак имуни одговор током имунизације животиња (имуногеност) на основу прегледа познатих епитопских секвенци је кључна иновација овог техничког решења. Ово је први пример успешно примењеног рекомбинатног протеина произведеног у Србији у дијагностичком тесту који је регистрован
код Агенције за лекове и медицинска средства Републике Србије (број решења 515-02-02370-21-002), а који је примену нашао и на међународном нивоу.
T1  - Dobijanje rekombinantnog imunogenog fragmenta proteina nukleokapsida SARS-CoV-2 virusa za proizvodnju reagenasa i dijagnostičkih testova na novi korona virus
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6014
ER  - 

@misc{
author = "Ćirković Veličković, Tanja and Gnjatović, Marija and Ćujić, Danica and Todorović, Aleksandra and Stanić-Vučinić, Dragana and Đukić, Teodora and Mladenović, Maja and Vasović, Tamara and Stojadinović, Marija and Krstić-Ristivojević, Maja and Jovanović, Vesna B. and Simović, Ana and Radosavljević, Jelena and Aćimović, Jelena M. and Radomirović, Mirjana Ž. and Stojanović, Marijana",
year = "2023",
abstract = "Нови корона вирус (SARS CoV-2) који се појавио у Вухану 2019. године припада групи једноланчаних РНК вируса [1]. Представља нови инфективни агенс за хуману популацију и веома је брзо детектован у великом броју земаља. Узрочник је респираторних инфекција које могу да буду праћене и веома тешком клиничком сликом. Брзо ширење, одсуство имунитета на овај вирус и одсуство поузданих тестова за детекцију вируса у тренутку избијања пандемије су болест изазвану овим вирусом брзо претворили у здравствени и друштвени проблем највишег приоритета на глобалном нивоу. Иако су највеће биотехнолошке компаније убрзано почеле са развојем и масовном производњом дијагностичких тестова и вакцина, њихова доступност у тренуцима највеће потражње је и даље недовољна, а цене истих су лимитирајући фактор за бољу контролу болести и ширења пандемије [2]. Развој сопствених и одржива производња тестова и вакцина за COVID-19 су од великог друштвеног значаја. Важан предуслов за одрживу производњу тестова је доступност рекомбинантних антигена вируса и могућност производње истих на великој скали за потребе производње домаћих тестова. Овим техничким решењем се описује добијање два кључна антигена новог корона вируса рекомбинантном технологијом и њихова примена у серолошком ЕЛИСА тесту који производи Институт за примену нуклеарне енергије, ИНЕП, као и за добијање реагенаса за детекцију антигена новог корона вируса (специфичних антитела). У првој фази, оптимизоване су секвенце протеина које су подигле осетљивост постојећих серолошких тестова. Иновативност нашег приступа се огледа и у разрађеним експерименталним протоколима за добијање рекомбинантних протеина нуклеокапсида на великој скали, као и у солубилној форми, што олакшава поступак пречишћавања. Избор фрагмента нуклеокапсида који се хетеролого експримира у солубилној форми, а специфично детектује антитела и генерише јак имуни одговор током имунизације животиња (имуногеност) на основу прегледа познатих епитопских секвенци је кључна иновација овог техничког решења. Ово је први пример успешно примењеног рекомбинатног протеина произведеног у Србији у дијагностичком тесту који је регистрован
код Агенције за лекове и медицинска средства Републике Србије (број решења 515-02-02370-21-002), а који је примену нашао и на међународном нивоу.",
title = "Dobijanje rekombinantnog imunogenog fragmenta proteina nukleokapsida SARS-CoV-2 virusa za proizvodnju reagenasa i dijagnostičkih testova na novi korona virus",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6014"
}

Ćirković Veličković, T., Gnjatović, M., Ćujić, D., Todorović, A., Stanić-Vučinić, D., Đukić, T., Mladenović, M., Vasović, T., Stojadinović, M., Krstić-Ristivojević, M., Jovanović, V. B., Simović, A., Radosavljević, J., Aćimović, J. M., Radomirović, M. Ž.,& Stojanović, M.. (2023). Dobijanje rekombinantnog imunogenog fragmenta proteina nukleokapsida SARS-CoV-2 virusa za proizvodnju reagenasa i dijagnostičkih testova na novi korona virus. .
https://hdl.handle.net/21.15107/rcub_cherry_6014

Ćirković Veličković T, Gnjatović M, Ćujić D, Todorović A, Stanić-Vučinić D, Đukić T, Mladenović M, Vasović T, Stojadinović M, Krstić-Ristivojević M, Jovanović VB, Simović A, Radosavljević J, Aćimović JM, Radomirović MŽ, Stojanović M. Dobijanje rekombinantnog imunogenog fragmenta proteina nukleokapsida SARS-CoV-2 virusa za proizvodnju reagenasa i dijagnostičkih testova na novi korona virus. 2023;.
https://hdl.handle.net/21.15107/rcub_cherry_6014 .

Ćirković Veličković, Tanja, Gnjatović, Marija, Ćujić, Danica, Todorović, Aleksandra, Stanić-Vučinić, Dragana, Đukić, Teodora, Mladenović, Maja, Vasović, Tamara, Stojadinović, Marija, Krstić-Ristivojević, Maja, Jovanović, Vesna B., Simović, Ana, Radosavljević, Jelena, Aćimović, Jelena M., Radomirović, Mirjana Ž., Stojanović, Marijana, "Dobijanje rekombinantnog imunogenog fragmenta proteina nukleokapsida SARS-CoV-2 virusa za proizvodnju reagenasa i dijagnostičkih testova na novi korona virus" (2023),
https://hdl.handle.net/21.15107/rcub_cherry_6014 .

TY  - JOUR
AU  - Mladenović Stokanić, Maja
AU  - Simović, Ana
AU  - Jovanović, Vesna B.
AU  - Radomirović, Mirjana
AU  - Udovićki, Božidar
AU  - Krstić Ristivojević, Maja
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Aćimović, Jelena
AU  - Sabljić, Ljiljana
AU  - Lukić, Ivana
AU  - Kovačević, Ana
AU  - Cujić, Danica
AU  - Gnjatović, Marija
AU  - Smiljanić, Katarina
AU  - Stojadinović, Marija
AU  - Radosavljević, Jelena
AU  - Stanić-Vučinić, Dragana
AU  - Stojanović, Marijana
AU  - Rajković, Andreja
AU  - Ćirković Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6436
AB  - In this study, a cost-effective sandwich ELISA test, based on polyclonal antibodies, for routine quantification SARS-CoV-2 nucleocapsid (N) protein was developed. The recombinant N protein was produced and used for the production of mice and rabbit antisera. Polyclonal N protein-specific antibodies served as capture and detection antibodies. The prototype ELISA has LOD 0.93 ng/mL and LOQ 5.3 ng/mL, with a linear range of 1.52–48.83 ng/mL. N protein heat pretreatment (56 °C, 1 h) decreased, while pretreatment with 1% Triton X-100 increased analytical ELISA sensitivity. The diagnostic specificity of ELISA was 100% (95% CI, 91.19–100.00%) and sensitivity was 52.94% (95% CI, 35.13–70.22%) compared to rtRT-PCR (Ct < 40). Profoundly higher sensitivity was obtained using patient samples mostly containing Wuhan-similar variants (Wuhan, alpha, and delta), 62.50% (95% CI, 40.59 to 81.20%), in comparison to samples mostly containing Wuhan-distant variants (Omicron) 30.00% (6.67–65.25%). The developed product has relatively high diagnostic sensitivity in relation to its analytical sensitivity due to the usage of polyclonal antibodies from two species, providing a wide repertoire of antibodies against multiple N protein epitopes. Moreover, the fast, simple, and inexpensive production of polyclonal antibodies, as the most expensive assay components, would result in affordable antigen tests.
PB  - MDPI
T2  - International Journal of Molecular Sciences
T1  - Sandwich ELISA for the Quantification of Nucleocapsid Protein of SARS-CoV-2 Based on Polyclonal Antibodies from Two Different Species
VL  - 25
IS  - 1
SP  - 333
DO  - 10.3390/ijms25010333
ER  - 

@article{
author = "Mladenović Stokanić, Maja and Simović, Ana and Jovanović, Vesna B. and Radomirović, Mirjana and Udovićki, Božidar and Krstić Ristivojević, Maja and Đukić, Teodora and Vasović, Tamara and Aćimović, Jelena and Sabljić, Ljiljana and Lukić, Ivana and Kovačević, Ana and Cujić, Danica and Gnjatović, Marija and Smiljanić, Katarina and Stojadinović, Marija and Radosavljević, Jelena and Stanić-Vučinić, Dragana and Stojanović, Marijana and Rajković, Andreja and Ćirković Veličković, Tanja",
year = "2023",
abstract = "In this study, a cost-effective sandwich ELISA test, based on polyclonal antibodies, for routine quantification SARS-CoV-2 nucleocapsid (N) protein was developed. The recombinant N protein was produced and used for the production of mice and rabbit antisera. Polyclonal N protein-specific antibodies served as capture and detection antibodies. The prototype ELISA has LOD 0.93 ng/mL and LOQ 5.3 ng/mL, with a linear range of 1.52–48.83 ng/mL. N protein heat pretreatment (56 °C, 1 h) decreased, while pretreatment with 1% Triton X-100 increased analytical ELISA sensitivity. The diagnostic specificity of ELISA was 100% (95% CI, 91.19–100.00%) and sensitivity was 52.94% (95% CI, 35.13–70.22%) compared to rtRT-PCR (Ct < 40). Profoundly higher sensitivity was obtained using patient samples mostly containing Wuhan-similar variants (Wuhan, alpha, and delta), 62.50% (95% CI, 40.59 to 81.20%), in comparison to samples mostly containing Wuhan-distant variants (Omicron) 30.00% (6.67–65.25%). The developed product has relatively high diagnostic sensitivity in relation to its analytical sensitivity due to the usage of polyclonal antibodies from two species, providing a wide repertoire of antibodies against multiple N protein epitopes. Moreover, the fast, simple, and inexpensive production of polyclonal antibodies, as the most expensive assay components, would result in affordable antigen tests.",
publisher = "MDPI",
journal = "International Journal of Molecular Sciences",
title = "Sandwich ELISA for the Quantification of Nucleocapsid Protein of SARS-CoV-2 Based on Polyclonal Antibodies from Two Different Species",
volume = "25",
number = "1",
pages = "333",
doi = "10.3390/ijms25010333"
}

Mladenović Stokanić, M., Simović, A., Jovanović, V. B., Radomirović, M., Udovićki, B., Krstić Ristivojević, M., Đukić, T., Vasović, T., Aćimović, J., Sabljić, L., Lukić, I., Kovačević, A., Cujić, D., Gnjatović, M., Smiljanić, K., Stojadinović, M., Radosavljević, J., Stanić-Vučinić, D., Stojanović, M., Rajković, A.,& Ćirković Veličković, T.. (2023). Sandwich ELISA for the Quantification of Nucleocapsid Protein of SARS-CoV-2 Based on Polyclonal Antibodies from Two Different Species. in International Journal of Molecular Sciences
MDPI., 25(1), 333.
https://doi.org/10.3390/ijms25010333

Mladenović Stokanić M, Simović A, Jovanović VB, Radomirović M, Udovićki B, Krstić Ristivojević M, Đukić T, Vasović T, Aćimović J, Sabljić L, Lukić I, Kovačević A, Cujić D, Gnjatović M, Smiljanić K, Stojadinović M, Radosavljević J, Stanić-Vučinić D, Stojanović M, Rajković A, Ćirković Veličković T. Sandwich ELISA for the Quantification of Nucleocapsid Protein of SARS-CoV-2 Based on Polyclonal Antibodies from Two Different Species. in International Journal of Molecular Sciences. 2023;25(1):333.
doi:10.3390/ijms25010333 .

Mladenović Stokanić, Maja, Simović, Ana, Jovanović, Vesna B., Radomirović, Mirjana, Udovićki, Božidar, Krstić Ristivojević, Maja, Đukić, Teodora, Vasović, Tamara, Aćimović, Jelena, Sabljić, Ljiljana, Lukić, Ivana, Kovačević, Ana, Cujić, Danica, Gnjatović, Marija, Smiljanić, Katarina, Stojadinović, Marija, Radosavljević, Jelena, Stanić-Vučinić, Dragana, Stojanović, Marijana, Rajković, Andreja, Ćirković Veličković, Tanja, "Sandwich ELISA for the Quantification of Nucleocapsid Protein of SARS-CoV-2 Based on Polyclonal Antibodies from Two Different Species" in International Journal of Molecular Sciences, 25, no. 1 (2023):333,
https://doi.org/10.3390/ijms25010333 . .

TY  - CONF
AU  - Lujić, Tamara
AU  - Gligorijević, Nikola
AU  - Jovanović, Vesna B.
AU  - Aćimović, Jelena
AU  - Mitić, Dragana
AU  - Vasović, Tamara
AU  - Stojadinović, Marija
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6424
AB  - Microplastics is abundant in the environment, food and beverages and get ingested by humans. Its complex interplay with proteins lead to formation of corona. Tightly bound proteins represent hard corona, while weaker binding partners are found in soft corona. Separation of hard and soft corona of allergenic proteins of shrimps, eggs and cow’s milk, tropomyosin (TPM), ovalbumin (OVA) and beta-lactoglobulin (BLG) and identification of binding partners by proteomics was aim of our study.
Allergenic proteins were purified from egg white, shrimps and cow’s milk. Binding to polyethylene terephthalate microplastics (PET) (70-100 m) was probed at pH 7 for purified allergens and egg white proteins. After establishment of binding equilibrium, soft and hard corona were separated and analyzed by SDS PAGE, followed by identification of bound proteins by nanoLC-HRMS. Binding of all allergenic proteins was observed in both soft and hard corona. Soft corona contains exclusively intact, full length OVA, TPM and BLG. Hard corona is enriched for truncated OVA and oligomers of TPM. OVA fragments are partially or fully enfolded and have higher level of exposed hydrophobic patches resulting in higher affinity for PET microplastics. In comparison to OVA and TPM, hard corona of BLG is less abundant under similar conditions. BLG is compact globular protein with lower level of exposed hydrophobic patches in comparison to ovalbumin and tropomyosin. In hard corona, trace amounts of contaminating alfa-lactalbumin become enriched. In the presence of egg white protein extract OVA forms both SC and HC on microplastics, being the dominant protein of hard corona (with ovotransferrin). Lysozyme and ovomucin are present only in hard corona. Both proteins are known for their strong bioactivity and represent a small fraction of total egg white proteins.
Our results show that allergenic proteins form hard corona on PET microplastics. Among egg white proteins, minor proteins such as lysozyme and ovomucin become enriched. Denaturing effect of strong binding to microplastics may change functional characteristics of allergens and bioactive proteins of foods and should be further investigated in functional assays.
Acknowledgment: This study was supported by IMPTOX European Union's Horizon 2020 research and innovation program (grant number 965173).
PB  - Italian Proteomics Association
C3  - ItPA HPS and SePA XVII International Congress: Proteomics and Metabolomics towards Global Health, November 29th – December 1st, 2023, Roma, Italy
T1  - Proteomic insight into allergenic food corona on polyethylene terephthalate microplastics
SP  - 11
EP  - 11
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6424
ER  - 

@conference{
author = "Lujić, Tamara and Gligorijević, Nikola and Jovanović, Vesna B. and Aćimović, Jelena and Mitić, Dragana and Vasović, Tamara and Stojadinović, Marija and Stanić-Vučinić, Dragana and Ćirković Veličković, Tanja",
year = "2023",
abstract = "Microplastics is abundant in the environment, food and beverages and get ingested by humans. Its complex interplay with proteins lead to formation of corona. Tightly bound proteins represent hard corona, while weaker binding partners are found in soft corona. Separation of hard and soft corona of allergenic proteins of shrimps, eggs and cow’s milk, tropomyosin (TPM), ovalbumin (OVA) and beta-lactoglobulin (BLG) and identification of binding partners by proteomics was aim of our study.
Allergenic proteins were purified from egg white, shrimps and cow’s milk. Binding to polyethylene terephthalate microplastics (PET) (70-100 m) was probed at pH 7 for purified allergens and egg white proteins. After establishment of binding equilibrium, soft and hard corona were separated and analyzed by SDS PAGE, followed by identification of bound proteins by nanoLC-HRMS. Binding of all allergenic proteins was observed in both soft and hard corona. Soft corona contains exclusively intact, full length OVA, TPM and BLG. Hard corona is enriched for truncated OVA and oligomers of TPM. OVA fragments are partially or fully enfolded and have higher level of exposed hydrophobic patches resulting in higher affinity for PET microplastics. In comparison to OVA and TPM, hard corona of BLG is less abundant under similar conditions. BLG is compact globular protein with lower level of exposed hydrophobic patches in comparison to ovalbumin and tropomyosin. In hard corona, trace amounts of contaminating alfa-lactalbumin become enriched. In the presence of egg white protein extract OVA forms both SC and HC on microplastics, being the dominant protein of hard corona (with ovotransferrin). Lysozyme and ovomucin are present only in hard corona. Both proteins are known for their strong bioactivity and represent a small fraction of total egg white proteins.
Our results show that allergenic proteins form hard corona on PET microplastics. Among egg white proteins, minor proteins such as lysozyme and ovomucin become enriched. Denaturing effect of strong binding to microplastics may change functional characteristics of allergens and bioactive proteins of foods and should be further investigated in functional assays.
Acknowledgment: This study was supported by IMPTOX European Union's Horizon 2020 research and innovation program (grant number 965173).",
publisher = "Italian Proteomics Association",
journal = "ItPA HPS and SePA XVII International Congress: Proteomics and Metabolomics towards Global Health, November 29th – December 1st, 2023, Roma, Italy",
title = "Proteomic insight into allergenic food corona on polyethylene terephthalate microplastics",
pages = "11-11",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6424"
}

Lujić, T., Gligorijević, N., Jovanović, V. B., Aćimović, J., Mitić, D., Vasović, T., Stojadinović, M., Stanić-Vučinić, D.,& Ćirković Veličković, T.. (2023). Proteomic insight into allergenic food corona on polyethylene terephthalate microplastics. in ItPA HPS and SePA XVII International Congress: Proteomics and Metabolomics towards Global Health, November 29th – December 1st, 2023, Roma, Italy
Italian Proteomics Association., 11-11.
https://hdl.handle.net/21.15107/rcub_cherry_6424

Lujić T, Gligorijević N, Jovanović VB, Aćimović J, Mitić D, Vasović T, Stojadinović M, Stanić-Vučinić D, Ćirković Veličković T. Proteomic insight into allergenic food corona on polyethylene terephthalate microplastics. in ItPA HPS and SePA XVII International Congress: Proteomics and Metabolomics towards Global Health, November 29th – December 1st, 2023, Roma, Italy. 2023;:11-11.
https://hdl.handle.net/21.15107/rcub_cherry_6424 .

Lujić, Tamara, Gligorijević, Nikola, Jovanović, Vesna B., Aćimović, Jelena, Mitić, Dragana, Vasović, Tamara, Stojadinović, Marija, Stanić-Vučinić, Dragana, Ćirković Veličković, Tanja, "Proteomic insight into allergenic food corona on polyethylene terephthalate microplastics" in ItPA HPS and SePA XVII International Congress: Proteomics and Metabolomics towards Global Health, November 29th – December 1st, 2023, Roma, Italy (2023):11-11,
https://hdl.handle.net/21.15107/rcub_cherry_6424 .

TY  - CONF
AU  - Krstić-Ristivojević, Maja
AU  - Jovanović, Vesna B.
AU  - Radomirović, Mirjana Ž.
AU  - Trifunović, Olga
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6024
AB  - In the last 50 years, the annual per capita consumption of seafood products worldwide has more than doubled, from almost 10 kg in 1960 to over 20 kg in 2014. Seafood protein is an essential part of the diet in many countries, particularly where total protein intake is low [1]. However, as defined by the European Community, fish, and shellfish tropomyosins (TPM) are major allergens and major causes of anaphylaxis [2]. The increasing prevalence of food allergies is consistent with the increasing pollution of soil and water with plastic particles. To investigate the potential link between increasing plastic pollution and increasing food allergy prevalence, we aim to develop methods for precise and accurate monitoring of allergens and plastic in real seafood samples.
TPM was isolated from shrimp (Litopenaeus vannamei), clams (Venerupis philippinarum), and mussels (Mytilus galloprovincialis). The obtained in-house TPM proteins from three different sources were resolved using two-dimensional polyacrylamide gel electrophoresis (2D-PAGE). The concentration of TPM in seashell samples from different geographical origin was determined using a sandwich Enzyme-Linked Immunosorbent Assay (ELISA) with prior optimization of adequate TPM standard curve using commercial and non-commercial in-house prepared TPM standards.
TPM standards resolved via 2D-PAGE revealed the presence of two isoforms of shrimp and mussels TPM standard, one dominant and one less abundant isoform. Two isoforms from both seafood sources, shrimp and mussels, are slightly different in molecular weight and pI value. As for the TPM standard obtained from clams, the 2D electrophoregram showed possibly eight isoforms with small differences in mass and pI values. Furthermore, the presence of three dominant isoforms can be observed that differ slightly in molecular mass, while other isoforms also differ in pI value. The ELISA results, regarding TPM standard curve optimization, showed that in both the commercial shrimp TPM and in-house shrimp TPM standards, sigmoidal concentration dependence is present in a range of 50 to 0.05 ng/ml, using serial double dilutions. On the other hand, TPM standards isolated from mussels and clams show sigmoidal concentration dependence in the range of 45 to 0.044 μg/ml with using the identical combination of capture and detection antibodies and serial double dilutions. TPM concentrations in clams and mussel samples extrapolated from standard curves of commercial shrimp TPM standard and corresponding in-house TPM standards are presented in Table 1.
Differences in TPM concentration of the same sample using different TPM standards differ from 40 to 600 times, which strongly indicates that the right choice of TPM standard is a critical step for accurate and precise determination of TPM concentration in seafood samples.
PB  - Beograd : Srpsko hemijsko društvo
C3  - XXII EuroFoodChem conference, 14th-16th June, 2023. In: Book of Abstracts
T1  - Tropomyosin quantification in seafood samples-right choice of standard makes a difference
SP  - 132
EP  - 132
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6024
ER  - 

@conference{
author = "Krstić-Ristivojević, Maja and Jovanović, Vesna B. and Radomirović, Mirjana Ž. and Trifunović, Olga and Stanić-Vučinić, Dragana and Ćirković Veličković, Tanja",
year = "2023",
abstract = "In the last 50 years, the annual per capita consumption of seafood products worldwide has more than doubled, from almost 10 kg in 1960 to over 20 kg in 2014. Seafood protein is an essential part of the diet in many countries, particularly where total protein intake is low [1]. However, as defined by the European Community, fish, and shellfish tropomyosins (TPM) are major allergens and major causes of anaphylaxis [2]. The increasing prevalence of food allergies is consistent with the increasing pollution of soil and water with plastic particles. To investigate the potential link between increasing plastic pollution and increasing food allergy prevalence, we aim to develop methods for precise and accurate monitoring of allergens and plastic in real seafood samples.
TPM was isolated from shrimp (Litopenaeus vannamei), clams (Venerupis philippinarum), and mussels (Mytilus galloprovincialis). The obtained in-house TPM proteins from three different sources were resolved using two-dimensional polyacrylamide gel electrophoresis (2D-PAGE). The concentration of TPM in seashell samples from different geographical origin was determined using a sandwich Enzyme-Linked Immunosorbent Assay (ELISA) with prior optimization of adequate TPM standard curve using commercial and non-commercial in-house prepared TPM standards.
TPM standards resolved via 2D-PAGE revealed the presence of two isoforms of shrimp and mussels TPM standard, one dominant and one less abundant isoform. Two isoforms from both seafood sources, shrimp and mussels, are slightly different in molecular weight and pI value. As for the TPM standard obtained from clams, the 2D electrophoregram showed possibly eight isoforms with small differences in mass and pI values. Furthermore, the presence of three dominant isoforms can be observed that differ slightly in molecular mass, while other isoforms also differ in pI value. The ELISA results, regarding TPM standard curve optimization, showed that in both the commercial shrimp TPM and in-house shrimp TPM standards, sigmoidal concentration dependence is present in a range of 50 to 0.05 ng/ml, using serial double dilutions. On the other hand, TPM standards isolated from mussels and clams show sigmoidal concentration dependence in the range of 45 to 0.044 μg/ml with using the identical combination of capture and detection antibodies and serial double dilutions. TPM concentrations in clams and mussel samples extrapolated from standard curves of commercial shrimp TPM standard and corresponding in-house TPM standards are presented in Table 1.
Differences in TPM concentration of the same sample using different TPM standards differ from 40 to 600 times, which strongly indicates that the right choice of TPM standard is a critical step for accurate and precise determination of TPM concentration in seafood samples.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "XXII EuroFoodChem conference, 14th-16th June, 2023. In: Book of Abstracts",
title = "Tropomyosin quantification in seafood samples-right choice of standard makes a difference",
pages = "132-132",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6024"
}

Krstić-Ristivojević, M., Jovanović, V. B., Radomirović, M. Ž., Trifunović, O., Stanić-Vučinić, D.,& Ćirković Veličković, T.. (2023). Tropomyosin quantification in seafood samples-right choice of standard makes a difference. in XXII EuroFoodChem conference, 14th-16th June, 2023. In: Book of Abstracts
Beograd : Srpsko hemijsko društvo., 132-132.
https://hdl.handle.net/21.15107/rcub_cherry_6024

Krstić-Ristivojević M, Jovanović VB, Radomirović MŽ, Trifunović O, Stanić-Vučinić D, Ćirković Veličković T. Tropomyosin quantification in seafood samples-right choice of standard makes a difference. in XXII EuroFoodChem conference, 14th-16th June, 2023. In: Book of Abstracts. 2023;:132-132.
https://hdl.handle.net/21.15107/rcub_cherry_6024 .

Krstić-Ristivojević, Maja, Jovanović, Vesna B., Radomirović, Mirjana Ž., Trifunović, Olga, Stanić-Vučinić, Dragana, Ćirković Veličković, Tanja, "Tropomyosin quantification in seafood samples-right choice of standard makes a difference" in XXII EuroFoodChem conference, 14th-16th June, 2023. In: Book of Abstracts (2023):132-132,
https://hdl.handle.net/21.15107/rcub_cherry_6024 .

TY  - CONF
AU  - Jovanović, Vesna B.
AU  - Radomirović, Mirjana Ž.
AU  - Krstić-Ristivojević, Maja
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6023
AB  - In the last several decades, the trend of seafood consumption has significantly increased not only in the countries with a tradition of seafood consumption, but also in other ones [1]. The increase in the world's population and the awareness of healthy food, the globalization of markets, and the development of aquaculture are some of the factors that have led to this trend. The aquaculture of shellfish like clams, mussels, oysters and scallops has been very developed all around the world and the food products based on them have become part of the daily diet for many consumers. In addition, these food products are considered healthy food because of the high content of proteins and essential fatty acids, but their consumption may carry some risks of food allergy. Tropomyosin from shellfish (TPM) is the major allergen responsible for the development of anaphylaxis in persons with food allergy. The content of TPM in shellfish and its bioavailability from food products can have potential influence on the sensitization of consumers to TPM. It is known that food processing can change the bioavailability of food allergens [2]. The main goal of this study was the investigation of how processing and packaging of shellfish samples can affect the content of TPM in them.
For this study, clam Venerupis philippinarum was chosen as the species with the highest world aquaculture production [1]. After the purchasing of live clams, the animals were separated into 5 groups for the next treatments: fresh live (control group), freshly removed inner content was kept at +4°C for 3 days (three days` shelf-life), frozen in a plastic bag and kept at -20 °C during 7 days, marinated and kept in a glass jar at room temperature during 8 days and freshly boiled. After processing and packaging of samples, the total protein extracts were prepared in 10 mM sodium phosphate buffer pH 7.4 1M NaCl, 1 mM PMSF and the concentration of total proteins was determined by BCA method. The concentration of TPM in the total protein extracts was determined using a sandwich Enzyme-Linked Immunosorbent Assay (ELISA) using in-house prepared clams` TPM standard. The content of TPM (μg) in the samples was expressed per mg of extracted soluble proteins, individual animal and grams of soft wet tissue.
The cooked samples have significantly higher TPM content expressed per gram of soft wet tissue compared to all other treatments. Food processing such as freezing, marinating, or extending the shelf-life at 4°C by 3 days has very little effect on the change in TPM content per gram of soft wet tissue compared to the fresh samples. The processing of clams, like cooking or marinating, caused the content of total soluble extracted proteins to be three to four times lower compared to the other three treatments. In these samples the obtained ratio of the total TPM/ total soluble extracted proteins ratio was the highest. This result can be explained by the fact that TPM is thermostable and stays soluble after cooking, while other proteins become insoluble because of denaturation. The lower ratio of TPM/ total soluble extracted proteins was found in marinated samples compared to the cooked samples. The lowest total tropomyosin/ total soluble extracted proteins ratio was found in 3 days’ shelf-life. Treatments like cooking, marinating and keeping the inner content of the shell at +4°C can significantly affect extractability of proteins, particularly affecting the ratio of major allergen TPM in the total protein extracts. Further studies are needed to examine bioaccessibility of TPM in different biologically relevant fluids (gastric/intestinal) and during digestion in relation to the processing conditions.
PB  - Beograd : Srpsko hemijsko društvo
C3  - XXII EuroFoodChem conference, Book of Abstracts, 14th-16th June, 2023.
T1  - The effect of food processing and packaging of clams on the content of tropomyosin
SP  - 240
EP  - 240
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6023
ER  - 

@conference{
author = "Jovanović, Vesna B. and Radomirović, Mirjana Ž. and Krstić-Ristivojević, Maja and Stanić-Vučinić, Dragana and Ćirković Veličković, Tanja",
year = "2023",
abstract = "In the last several decades, the trend of seafood consumption has significantly increased not only in the countries with a tradition of seafood consumption, but also in other ones [1]. The increase in the world's population and the awareness of healthy food, the globalization of markets, and the development of aquaculture are some of the factors that have led to this trend. The aquaculture of shellfish like clams, mussels, oysters and scallops has been very developed all around the world and the food products based on them have become part of the daily diet for many consumers. In addition, these food products are considered healthy food because of the high content of proteins and essential fatty acids, but their consumption may carry some risks of food allergy. Tropomyosin from shellfish (TPM) is the major allergen responsible for the development of anaphylaxis in persons with food allergy. The content of TPM in shellfish and its bioavailability from food products can have potential influence on the sensitization of consumers to TPM. It is known that food processing can change the bioavailability of food allergens [2]. The main goal of this study was the investigation of how processing and packaging of shellfish samples can affect the content of TPM in them.
For this study, clam Venerupis philippinarum was chosen as the species with the highest world aquaculture production [1]. After the purchasing of live clams, the animals were separated into 5 groups for the next treatments: fresh live (control group), freshly removed inner content was kept at +4°C for 3 days (three days` shelf-life), frozen in a plastic bag and kept at -20 °C during 7 days, marinated and kept in a glass jar at room temperature during 8 days and freshly boiled. After processing and packaging of samples, the total protein extracts were prepared in 10 mM sodium phosphate buffer pH 7.4 1M NaCl, 1 mM PMSF and the concentration of total proteins was determined by BCA method. The concentration of TPM in the total protein extracts was determined using a sandwich Enzyme-Linked Immunosorbent Assay (ELISA) using in-house prepared clams` TPM standard. The content of TPM (μg) in the samples was expressed per mg of extracted soluble proteins, individual animal and grams of soft wet tissue.
The cooked samples have significantly higher TPM content expressed per gram of soft wet tissue compared to all other treatments. Food processing such as freezing, marinating, or extending the shelf-life at 4°C by 3 days has very little effect on the change in TPM content per gram of soft wet tissue compared to the fresh samples. The processing of clams, like cooking or marinating, caused the content of total soluble extracted proteins to be three to four times lower compared to the other three treatments. In these samples the obtained ratio of the total TPM/ total soluble extracted proteins ratio was the highest. This result can be explained by the fact that TPM is thermostable and stays soluble after cooking, while other proteins become insoluble because of denaturation. The lower ratio of TPM/ total soluble extracted proteins was found in marinated samples compared to the cooked samples. The lowest total tropomyosin/ total soluble extracted proteins ratio was found in 3 days’ shelf-life. Treatments like cooking, marinating and keeping the inner content of the shell at +4°C can significantly affect extractability of proteins, particularly affecting the ratio of major allergen TPM in the total protein extracts. Further studies are needed to examine bioaccessibility of TPM in different biologically relevant fluids (gastric/intestinal) and during digestion in relation to the processing conditions.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "XXII EuroFoodChem conference, Book of Abstracts, 14th-16th June, 2023.",
title = "The effect of food processing and packaging of clams on the content of tropomyosin",
pages = "240-240",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6023"
}

Jovanović, V. B., Radomirović, M. Ž., Krstić-Ristivojević, M., Stanić-Vučinić, D.,& Ćirković Veličković, T.. (2023). The effect of food processing and packaging of clams on the content of tropomyosin. in XXII EuroFoodChem conference, Book of Abstracts, 14th-16th June, 2023.
Beograd : Srpsko hemijsko društvo., 240-240.
https://hdl.handle.net/21.15107/rcub_cherry_6023

Jovanović VB, Radomirović MŽ, Krstić-Ristivojević M, Stanić-Vučinić D, Ćirković Veličković T. The effect of food processing and packaging of clams on the content of tropomyosin. in XXII EuroFoodChem conference, Book of Abstracts, 14th-16th June, 2023.. 2023;:240-240.
https://hdl.handle.net/21.15107/rcub_cherry_6023 .

Jovanović, Vesna B., Radomirović, Mirjana Ž., Krstić-Ristivojević, Maja, Stanić-Vučinić, Dragana, Ćirković Veličković, Tanja, "The effect of food processing and packaging of clams on the content of tropomyosin" in XXII EuroFoodChem conference, Book of Abstracts, 14th-16th June, 2023. (2023):240-240,
https://hdl.handle.net/21.15107/rcub_cherry_6023 .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Bićanin, Maša
AU  - Udovički, Božidar
AU  - Krstić-Ristivojević, Maja
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Jovanović, Vesna B.
AU  - Stanić-Vučinić, Dragana
AU  - Rajković, Andreja
AU  - Ćirković Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6021
AB  - Accurately diagnosing people with suspected SARS-CoV-2 infection is essential to help manage COVID-19. Currently available SARS-CoV-2 diagnostics detect either RNA of the virus by RT-PCR or the presence of viral antigens in biological fluids by ELISA or similar techniques. Low sensitivity of antigen tests could lead to the risk of false negative results. Therefore, this study aimed to develop a highly sensitive immuno-PCR method for quantifying SARS-CoV-2 nucleocapsid (N) protein that combines the specificity of sandwich ELISA with the sensitivity of PCR. Recombinant N protein fragment was produced in E. coli as an expression system and purified using immobilized metal ion affinity chromatography. The antibodies against the N protein were raised in rabbits and mice. High-affinity polyclonal mice and rabbit N protein-specific antisera were purified using ammonium sulfate precipitation and used to develop sandwich ELISA for the quantification of N protein. Mice polyclonal serum was used as a capture for N protein. N
protein bound to mice antibodies was detected with rabbit polyclonal sera. A double-stranded amino-DNA molecule of 77 base pairs was PCR-synthesized, covalently conjugated to a secondary goat anti-rabbit antibody and subsequently amplified and quantified by real-time PCR. The results were compared to analogous sandwich ELISA consisting of alkaline phosphatase-labeled goat anti-rabbit antibody. The sensitivity of immuno-PCR for quantification of N protein was increased by up to 7-fold compared to analogous ELISA, having a limit of detection of 92 pg/mL and a limit of quantification of 840 pg/mL. The developed immuno-PCR method thus has the potential to be used as a new antigen test for COVID-19 and beyond.
PB  - Federation of European Biochemical Societies, Wiley
C3  - The 47th FEBS Congress, 8th-12th July, 2023. In: FEBS Open Bio, 13: Suppl. 2
T1  - Development of immuno-PCR for sensitive quantification of SARS-CoV-2 nucleocapsid protein
SP  - 44
EP  - 44
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6021
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Bićanin, Maša and Udovički, Božidar and Krstić-Ristivojević, Maja and Đukić, Teodora and Vasović, Tamara and Jovanović, Vesna B. and Stanić-Vučinić, Dragana and Rajković, Andreja and Ćirković Veličković, Tanja",
year = "2023",
abstract = "Accurately diagnosing people with suspected SARS-CoV-2 infection is essential to help manage COVID-19. Currently available SARS-CoV-2 diagnostics detect either RNA of the virus by RT-PCR or the presence of viral antigens in biological fluids by ELISA or similar techniques. Low sensitivity of antigen tests could lead to the risk of false negative results. Therefore, this study aimed to develop a highly sensitive immuno-PCR method for quantifying SARS-CoV-2 nucleocapsid (N) protein that combines the specificity of sandwich ELISA with the sensitivity of PCR. Recombinant N protein fragment was produced in E. coli as an expression system and purified using immobilized metal ion affinity chromatography. The antibodies against the N protein were raised in rabbits and mice. High-affinity polyclonal mice and rabbit N protein-specific antisera were purified using ammonium sulfate precipitation and used to develop sandwich ELISA for the quantification of N protein. Mice polyclonal serum was used as a capture for N protein. N
protein bound to mice antibodies was detected with rabbit polyclonal sera. A double-stranded amino-DNA molecule of 77 base pairs was PCR-synthesized, covalently conjugated to a secondary goat anti-rabbit antibody and subsequently amplified and quantified by real-time PCR. The results were compared to analogous sandwich ELISA consisting of alkaline phosphatase-labeled goat anti-rabbit antibody. The sensitivity of immuno-PCR for quantification of N protein was increased by up to 7-fold compared to analogous ELISA, having a limit of detection of 92 pg/mL and a limit of quantification of 840 pg/mL. The developed immuno-PCR method thus has the potential to be used as a new antigen test for COVID-19 and beyond.",
publisher = "Federation of European Biochemical Societies, Wiley",
journal = "The 47th FEBS Congress, 8th-12th July, 2023. In: FEBS Open Bio, 13: Suppl. 2",
title = "Development of immuno-PCR for sensitive quantification of SARS-CoV-2 nucleocapsid protein",
pages = "44-44",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6021"
}

Radomirović, M. Ž., Bićanin, M., Udovički, B., Krstić-Ristivojević, M., Đukić, T., Vasović, T., Jovanović, V. B., Stanić-Vučinić, D., Rajković, A.,& Ćirković Veličković, T.. (2023). Development of immuno-PCR for sensitive quantification of SARS-CoV-2 nucleocapsid protein. in The 47th FEBS Congress, 8th-12th July, 2023. In: FEBS Open Bio, 13: Suppl. 2
Federation of European Biochemical Societies, Wiley., 44-44.
https://hdl.handle.net/21.15107/rcub_cherry_6021

Radomirović MŽ, Bićanin M, Udovički B, Krstić-Ristivojević M, Đukić T, Vasović T, Jovanović VB, Stanić-Vučinić D, Rajković A, Ćirković Veličković T. Development of immuno-PCR for sensitive quantification of SARS-CoV-2 nucleocapsid protein. in The 47th FEBS Congress, 8th-12th July, 2023. In: FEBS Open Bio, 13: Suppl. 2. 2023;:44-44.
https://hdl.handle.net/21.15107/rcub_cherry_6021 .

Radomirović, Mirjana Ž., Bićanin, Maša, Udovički, Božidar, Krstić-Ristivojević, Maja, Đukić, Teodora, Vasović, Tamara, Jovanović, Vesna B., Stanić-Vučinić, Dragana, Rajković, Andreja, Ćirković Veličković, Tanja, "Development of immuno-PCR for sensitive quantification of SARS-CoV-2 nucleocapsid protein" in The 47th FEBS Congress, 8th-12th July, 2023. In: FEBS Open Bio, 13: Suppl. 2 (2023):44-44,
https://hdl.handle.net/21.15107/rcub_cherry_6021 .

TY  - DATA
AU  - Abdelhameed, Shorok A. M.
AU  - de Azambuja, Francisco
AU  - Vasović, Tamara
AU  - Savić, Nada D.
AU  - Ćirković Veličković, Tanja
AU  - Parac-Vogt, Tatjana N.
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5816
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5840
AB  - Oxidative modifications of proteins are key to many applications in biotechnology. Metal-catalyzed oxidation reactions efficiently oxidize proteins but with low selectivity, and are highly dependent on the protein surface residues to direct the reaction. Herein, we demonstrate that discrete inorganic ligands such as polyoxometalates enable an efficient and selective protein oxidative cleavage. In the presence of ascorbate (1 mM), the Cu-substituted polyoxometalate K8[Cu2+(H2O)(α2-P2W17O61)], (CuIIWD, 0.05 mM) selectively cleave hen egg white lysozyme under physiological conditions (pH =7.5, 37 °C) producing only four bands in the gel electropherogram (12.7, 11, 10, and 5 kDa). Liquid chromatography/mass spectrometry analysis reveals a regioselective cleavage in the vicinity of crystallographic CuIIWD/lysozyme interaction sites. Mechanistically, polyoxometalate is critical to position the Cu at the protein surface and limit the generation of oxidative species to the proximity of binding sites. Ultimately, this study outlines the potential of discrete, designable metal oxo clusters as catalysts for the selective modification of proteins through radical mechanisms under non-denaturing conditions.
PB  - Springer Nature
T2  - Nature Communications
T1  - Supplementary material for: Abdelhameed, S. A. M., de Azambuja, F., Vasović, T., Savić, N. D., Ćirković-Veličković, T.,& Parac-Vogt, T. N.. (2023). Regioselective protein oxidative cleavage enabled by enzyme-like recognition of an inorganic metal oxo cluster ligand. in Nature Communications Springer Nature., 14(1), 486. https://doi.org/10.1038/s41467-023-36085-z
VL  - 14
IS  - 1
SP  - 486
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5840
ER  - 

@misc{
author = "Abdelhameed, Shorok A. M. and de Azambuja, Francisco and Vasović, Tamara and Savić, Nada D. and Ćirković Veličković, Tanja and Parac-Vogt, Tatjana N.",
year = "2023",
abstract = "Oxidative modifications of proteins are key to many applications in biotechnology. Metal-catalyzed oxidation reactions efficiently oxidize proteins but with low selectivity, and are highly dependent on the protein surface residues to direct the reaction. Herein, we demonstrate that discrete inorganic ligands such as polyoxometalates enable an efficient and selective protein oxidative cleavage. In the presence of ascorbate (1 mM), the Cu-substituted polyoxometalate K8[Cu2+(H2O)(α2-P2W17O61)], (CuIIWD, 0.05 mM) selectively cleave hen egg white lysozyme under physiological conditions (pH =7.5, 37 °C) producing only four bands in the gel electropherogram (12.7, 11, 10, and 5 kDa). Liquid chromatography/mass spectrometry analysis reveals a regioselective cleavage in the vicinity of crystallographic CuIIWD/lysozyme interaction sites. Mechanistically, polyoxometalate is critical to position the Cu at the protein surface and limit the generation of oxidative species to the proximity of binding sites. Ultimately, this study outlines the potential of discrete, designable metal oxo clusters as catalysts for the selective modification of proteins through radical mechanisms under non-denaturing conditions.",
publisher = "Springer Nature",
journal = "Nature Communications",
title = "Supplementary material for: Abdelhameed, S. A. M., de Azambuja, F., Vasović, T., Savić, N. D., Ćirković-Veličković, T.,& Parac-Vogt, T. N.. (2023). Regioselective protein oxidative cleavage enabled by enzyme-like recognition of an inorganic metal oxo cluster ligand. in Nature Communications Springer Nature., 14(1), 486. https://doi.org/10.1038/s41467-023-36085-z",
volume = "14",
number = "1",
pages = "486",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5840"
}

Abdelhameed, S. A. M., de Azambuja, F., Vasović, T., Savić, N. D., Ćirković Veličković, T.,& Parac-Vogt, T. N.. (2023). Supplementary material for: Abdelhameed, S. A. M., de Azambuja, F., Vasović, T., Savić, N. D., Ćirković-Veličković, T.,& Parac-Vogt, T. N.. (2023). Regioselective protein oxidative cleavage enabled by enzyme-like recognition of an inorganic metal oxo cluster ligand. in Nature Communications Springer Nature., 14(1), 486. https://doi.org/10.1038/s41467-023-36085-z. in Nature Communications
Springer Nature., 14(1), 486.
https://hdl.handle.net/21.15107/rcub_cherry_5840

Abdelhameed SAM, de Azambuja F, Vasović T, Savić ND, Ćirković Veličković T, Parac-Vogt TN. Supplementary material for: Abdelhameed, S. A. M., de Azambuja, F., Vasović, T., Savić, N. D., Ćirković-Veličković, T.,& Parac-Vogt, T. N.. (2023). Regioselective protein oxidative cleavage enabled by enzyme-like recognition of an inorganic metal oxo cluster ligand. in Nature Communications Springer Nature., 14(1), 486. https://doi.org/10.1038/s41467-023-36085-z. in Nature Communications. 2023;14(1):486.
https://hdl.handle.net/21.15107/rcub_cherry_5840 .

Abdelhameed, Shorok A. M., de Azambuja, Francisco, Vasović, Tamara, Savić, Nada D., Ćirković Veličković, Tanja, Parac-Vogt, Tatjana N., "Supplementary material for: Abdelhameed, S. A. M., de Azambuja, F., Vasović, T., Savić, N. D., Ćirković-Veličković, T.,& Parac-Vogt, T. N.. (2023). Regioselective protein oxidative cleavage enabled by enzyme-like recognition of an inorganic metal oxo cluster ligand. in Nature Communications Springer Nature., 14(1), 486. https://doi.org/10.1038/s41467-023-36085-z" in Nature Communications, 14, no. 1 (2023):486,
https://hdl.handle.net/21.15107/rcub_cherry_5840 .