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  - https://cer.ihtm.bg.ac.rs/handle/123456789/7686
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) post-translational 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.
PB  - FEBS Press
C3  - FEBS openbio, 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  - Supplement 2
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) post-translational 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.",
publisher = "FEBS Press",
journal = "FEBS openbio, 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 = "Supplement 2",
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 openbio, 48th FEBS Congress, 29 June - 3 July 2024, Milano Italy
FEBS Press., 14(Supplement 2), 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 openbio, 48th FEBS Congress, 29 June - 3 July 2024, Milano Italy. 2024;14(Supplement 2):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 openbio, 48th FEBS Congress, 29 June - 3 July 2024, Milano Italy, 14, no. Supplement 2 (2024):428-428,
https://doi.org/10.1002/2211-5463.13837 . .

TY  - JOUR
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  - https://cer.ihtm.bg.ac.rs/handle/123456789/7606
AB  - Contaminating microplastics can interact with food proteins in the food matrix and during digestion. This study investigated adsorption of chicken egg protein ovalbumin to polystyrene (PS, 110 and 260 μm) and polyethylene terephthalate (PET, 140 μm) MPs in acidic and neutral conditions and alterations in ovalbumin structure. Ovalbumin adsorption affinity depended on MPs size (smaller > larger), type (PS > PET) and pH (pH 3 > pH 7). In bulk solution, MPs does not change ovalbumin secondary structure significantly, but induces loosening (at pH 3) and tightening (at pH 7) of tertiary structure. Formed soft corona exclusively consists of full length non-native ovalbumin, while in hard corona also shorter ovalbumin fragments were found. At pH 7 soft corona ovalbumin has rearranged but still preserved level of ordered secondary structure, resulting in preserved thermostability and proteolytic stability, but decreased ability to form fibrils upon heating. Secondary structure changes in soft corona resemble changes in native ovalbumin induced by heat treatment (80 ◦C). Ovalbumin is abundantly present in corona around microplastics also in the presence of other egg white proteins. These results imply that microplastics contaminating food may bind and change structure and functional properties of the main egg white protein.
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 de Guzman, Maria Krishna and Aćimović, Jelena and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2024",
abstract = "Contaminating microplastics can interact with food proteins in the food matrix and during digestion. This study investigated adsorption of chicken egg protein ovalbumin to polystyrene (PS, 110 and 260 μm) and polyethylene terephthalate (PET, 140 μm) MPs in acidic and neutral conditions and alterations in ovalbumin structure. Ovalbumin adsorption affinity depended on MPs size (smaller > larger), type (PS > PET) and pH (pH 3 > pH 7). In bulk solution, MPs does not change ovalbumin secondary structure significantly, but induces loosening (at pH 3) and tightening (at pH 7) of tertiary structure. Formed soft corona exclusively consists of full length non-native ovalbumin, while in hard corona also shorter ovalbumin fragments were found. At pH 7 soft corona ovalbumin has rearranged but still preserved level of ordered secondary structure, resulting in preserved thermostability and proteolytic stability, but decreased ability to form fibrils upon heating. Secondary structure changes in soft corona resemble changes in native ovalbumin induced by heat treatment (80 ◦C). Ovalbumin is abundantly present in corona around microplastics also in the presence of other egg white proteins. These results imply that microplastics contaminating food may bind and change structure and functional properties of the main egg white protein.",
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., de Guzman, M. K., Aćimović, J., 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, de Guzman MK, Aćimović J, 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, de Guzman, Maria Krishna, Aćimović, Jelena, 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  - CONF
AU  - Aćimović, Jelena
AU  - Gligorijević, Nikola
AU  - Radomirović, Mirjana
AU  - Vasović, Tamara
AU  - Stojadinović, Marija
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7649
AB  - Microplastics (MPs) interact with proteins, forming a complex called a protein corona. This corona
alters the biological identity and properties of MPs, enabling them to evade the immune system,
persist longer in circulation, and disrupt cellular and molecular processes. Biofilm formation on
MPs occurs in several steps, starting with initial binding of molecules to form a hard corona,
followed by the formation of a soft corona. β-Lactoglobulin (BLG), a major whey protein in bovine
milk, is highly valued as a food ingredient but poses significant health risks to milk-allergic
individuals. This study aimed to understand BLG's interactions with selected MPs (polyethylene
terephthalate, PET, <80μm; polypropylene, PP, 63-180μm). BLG, isolated from
unpasteurized/pasteurized milk, was incubated with PP and PET in simulated physiological fluids.
The resulting coronas were analyzed using reduced SDS-PAGE electrophoresis and densitometry.
BLG exhibited low binding to both MPs, with pasteurized BLG showing the lowest binding to PP
(less than 1% of control in its soft corona). There were differences in the protein content of hard
coronas between pasteurized and unpasteurized BLG, with a slightly higher percentage of bound
proteins in the hard corona of unpasteurized BLG. Additionally, the protein profile of hard coronas
differed between PET and PP incubated with pasteurized BLG compared to those with
unpasteurized BLG. These findings suggest that the presence of MPs may affect the bioavailability
and allergenic properties of both pasteurized and unpasteurized BLG.
AB  - Interakcija mikroplastike (MP) s proteinima stvara kompleks poznat kao proteinska korona. U okviru korone, MP dobija nove biološke osobine, uključujući izbegavanje imunog sistema, dugotrajnije zadržavanje u cirkulaciji i ometanje ćelijskih procesa. Formiranje biofilma na površini MP je višestepeni proces, gde se nakon prvobitnog vezivanja molekula s visokim afinitetom i formiranja čvrste korone, može razviti i labavija korona u kasnijim fazama. β-laktoglobulin (BLG), glavni protein u surutki kravljeg mleka, često korišćen u hrani, može izazvati značajne zdravstvene probleme kod osoba alergičnih na mleko. Ovo istraživanje je imalo za cilj da pruži bolji uvid u interakcije između BLG kao alergena hrane i odabranih MP (polietilen-tereftalat, PET, <80μm; polipropilen, PP, 63-180μm). Izolovani nepasterizovani/pasterizovani BLG je inkubiran s PP i PET in vitro, u simuliranim fiziološkim tečnostima, a formirane korone su analizirane SDSPAGE elektroforezom pod redukujućim uslovima i denzitometrijom. Rezultati pokazuju da BLG slabo vezuje za obe MP. Postoji razlika u proteinima čvrstih korona između pasterizovanog i nepasterizovanog BLG, kao i u proteinskom profilu korona PP i PET inkubiranih s pasterizovanim ili nepasterizovanim BLG. Naši rezultati ukazuju da prisustvo MP može uticati na biodostupnost i alergene osobine i pasterizovanog i nepasterizovanog BLG.
PB  - Serbian Chemical Society
PB  - Srpsko hemijsko društvo
C3  - 60. Savetovanje Srpskog hemijskog društva - Kratki izvodi radova, Niš 8. i 9. jun 2024. godine
T1  - Soft i hard korona mikroplastike u interakciji sa alergenom β-laktoglobulinom kravljeg mleka
T1  - Soft and hard corona of microplastics interacted with allergenic bovine milk β-lactoglobulin
SP  - 53
EP  - 53
UR  - https://hdl.handle.net/21.15107/rcub_cer_7649
ER  - 

@conference{
author = "Aćimović, Jelena and Gligorijević, Nikola and Radomirović, Mirjana and Vasović, Tamara and Stojadinović, Marija and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2024",
abstract = "Microplastics (MPs) interact with proteins, forming a complex called a protein corona. This corona
alters the biological identity and properties of MPs, enabling them to evade the immune system,
persist longer in circulation, and disrupt cellular and molecular processes. Biofilm formation on
MPs occurs in several steps, starting with initial binding of molecules to form a hard corona,
followed by the formation of a soft corona. β-Lactoglobulin (BLG), a major whey protein in bovine
milk, is highly valued as a food ingredient but poses significant health risks to milk-allergic
individuals. This study aimed to understand BLG's interactions with selected MPs (polyethylene
terephthalate, PET, <80μm; polypropylene, PP, 63-180μm). BLG, isolated from
unpasteurized/pasteurized milk, was incubated with PP and PET in simulated physiological fluids.
The resulting coronas were analyzed using reduced SDS-PAGE electrophoresis and densitometry.
BLG exhibited low binding to both MPs, with pasteurized BLG showing the lowest binding to PP
(less than 1% of control in its soft corona). There were differences in the protein content of hard
coronas between pasteurized and unpasteurized BLG, with a slightly higher percentage of bound
proteins in the hard corona of unpasteurized BLG. Additionally, the protein profile of hard coronas
differed between PET and PP incubated with pasteurized BLG compared to those with
unpasteurized BLG. These findings suggest that the presence of MPs may affect the bioavailability
and allergenic properties of both pasteurized and unpasteurized BLG., Interakcija mikroplastike (MP) s proteinima stvara kompleks poznat kao proteinska korona. U okviru korone, MP dobija nove biološke osobine, uključujući izbegavanje imunog sistema, dugotrajnije zadržavanje u cirkulaciji i ometanje ćelijskih procesa. Formiranje biofilma na površini MP je višestepeni proces, gde se nakon prvobitnog vezivanja molekula s visokim afinitetom i formiranja čvrste korone, može razviti i labavija korona u kasnijim fazama. β-laktoglobulin (BLG), glavni protein u surutki kravljeg mleka, često korišćen u hrani, može izazvati značajne zdravstvene probleme kod osoba alergičnih na mleko. Ovo istraživanje je imalo za cilj da pruži bolji uvid u interakcije između BLG kao alergena hrane i odabranih MP (polietilen-tereftalat, PET, <80μm; polipropilen, PP, 63-180μm). Izolovani nepasterizovani/pasterizovani BLG je inkubiran s PP i PET in vitro, u simuliranim fiziološkim tečnostima, a formirane korone su analizirane SDSPAGE elektroforezom pod redukujućim uslovima i denzitometrijom. Rezultati pokazuju da BLG slabo vezuje za obe MP. Postoji razlika u proteinima čvrstih korona između pasterizovanog i nepasterizovanog BLG, kao i u proteinskom profilu korona PP i PET inkubiranih s pasterizovanim ili nepasterizovanim BLG. Naši rezultati ukazuju da prisustvo MP može uticati na biodostupnost i alergene osobine i pasterizovanog i nepasterizovanog BLG.",
publisher = "Serbian Chemical Society, Srpsko hemijsko društvo",
journal = "60. Savetovanje Srpskog hemijskog društva - Kratki izvodi radova, Niš 8. i 9. jun 2024. godine",
title = "Soft i hard korona mikroplastike u interakciji sa alergenom β-laktoglobulinom kravljeg mleka, Soft and hard corona of microplastics interacted with allergenic bovine milk β-lactoglobulin",
pages = "53-53",
url = "https://hdl.handle.net/21.15107/rcub_cer_7649"
}

Aćimović, J., Gligorijević, N., Radomirović, M., Vasović, T., Stojadinović, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2024). Soft i hard korona mikroplastike u interakciji sa alergenom β-laktoglobulinom kravljeg mleka. in 60. Savetovanje Srpskog hemijskog društva - Kratki izvodi radova, Niš 8. i 9. jun 2024. godine
Serbian Chemical Society., 53-53.
https://hdl.handle.net/21.15107/rcub_cer_7649

Aćimović J, Gligorijević N, Radomirović M, Vasović T, Stojadinović M, Stanić-Vučinić D, Ćirković-Veličković T. Soft i hard korona mikroplastike u interakciji sa alergenom β-laktoglobulinom kravljeg mleka. in 60. Savetovanje Srpskog hemijskog društva - Kratki izvodi radova, Niš 8. i 9. jun 2024. godine. 2024;:53-53.
https://hdl.handle.net/21.15107/rcub_cer_7649 .

Aćimović, Jelena, Gligorijević, Nikola, Radomirović, Mirjana, Vasović, Tamara, Stojadinović, Marija, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Soft i hard korona mikroplastike u interakciji sa alergenom β-laktoglobulinom kravljeg mleka" in 60. Savetovanje Srpskog hemijskog društva - Kratki izvodi radova, Niš 8. i 9. jun 2024. godine (2024):53-53,
https://hdl.handle.net/21.15107/rcub_cer_7649 .

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  - https://cer.ihtm.bg.ac.rs/handle/123456789/7473
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.
PB  - Italian Proteomics Association
C3  - XVII International Italian Proteomics Association Annual Meeting in partnership with the Hellenic Proteomics Society and Serbian Proteomics Association, "Proteomics and Metabolomics towards Global Health", November 29th-December 1st, 2023, Ospedale Isola Tiberina - Gemelli Isola,  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_cer_7473
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.",
publisher = "Italian Proteomics Association",
journal = "XVII International Italian Proteomics Association Annual Meeting in partnership with the Hellenic Proteomics Society and Serbian Proteomics Association, "Proteomics and Metabolomics towards Global Health", November 29th-December 1st, 2023, Ospedale Isola Tiberina - Gemelli Isola,  Roma, Italy",
title = "Proteomic insight into allergenic food corona on polyethylene terephthalate microplastics",
pages = "11-11",
url = "https://hdl.handle.net/21.15107/rcub_cer_7473"
}

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 XVII International Italian Proteomics Association Annual Meeting in partnership with the Hellenic Proteomics Society and Serbian Proteomics Association, "Proteomics and Metabolomics towards Global Health", November 29th-December 1st, 2023, Ospedale Isola Tiberina - Gemelli Isola,  Roma, Italy
Italian Proteomics Association., 11-11.
https://hdl.handle.net/21.15107/rcub_cer_7473

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 XVII International Italian Proteomics Association Annual Meeting in partnership with the Hellenic Proteomics Society and Serbian Proteomics Association, "Proteomics and Metabolomics towards Global Health", November 29th-December 1st, 2023, Ospedale Isola Tiberina - Gemelli Isola,  Roma, Italy. 2023;:11-11.
https://hdl.handle.net/21.15107/rcub_cer_7473 .

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 XVII International Italian Proteomics Association Annual Meeting in partnership with the Hellenic Proteomics Society and Serbian Proteomics Association, "Proteomics and Metabolomics towards Global Health", November 29th-December 1st, 2023, Ospedale Isola Tiberina - Gemelli Isola,  Roma, Italy (2023):11-11,
https://hdl.handle.net/21.15107/rcub_cer_7473 .