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  - Brulet, Annie
AU  - Ćirković Veličković, Tanja
AU  - Combet, Sophie
AU  - Nikolić, Milan
AU  - Minić, Simeon
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6473
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 RPC 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 Ltd.
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 Brulet, 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 RPC 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 Ltd.",
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., Brulet, 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 Ltd.., 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, Brulet 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, Brulet, 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  - 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  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6898
AB  - Ovalbumin (OVA), a main protein of egg white, has characteristic structural fold of a
serpin-family of proteins, propensity to fibril formation and stability to digestion.
Microplastics (MPs) contaminating our food can interact with food proteins in the food
matrix and during digestion. In this study adsorption of OVA to polystyrene (PS) (110 μm
and 260 μm), polyethylene terephthalate (PET) (140 μm) MPs were investigated in acidic
(pH 3) and neutral (pH 7) conditions. Formations of corona on MPs were investigated
using isolated OVA and egg white protein extract comparatively. OVA adsorption depends
on MPs size, polymer chemistry and pH, being highest in acidic pH and higher for PS.
Adsorption of OVA to PS and PET reaches dynamic equilibrium after 4h resulting in
disruption of tertiary structure and formation of hard and soft corona around MPs. Shorter
fragments of OVA populate hard corona, while soft corona exclusively consist of full
length OVA, albeit in its non-native conformation. The conformational changes resemble
those induced by heat treatment with re-arrangement of α-β secondary structures.
Structural changes are striking for the OVA in corona around MPs. Soft corona OVA
preserves thermal and proteolytic stability, but loses ability to form fibrils upon heating.
OVA is abundantly present in corona around MPs also in the presence of other egg white
proteins. MPs contaminating food may bind and change structure and functional properties
of main egg white protein.
PB  - Kragujevac, Srbija : Prirodno-matematički fakultet, Univerzitet u Kragujevcu /  Kragujevac, Serbia : Faculty of Science, University of Kragujevac
C3  - VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike,” Zbornik apstrakata, 2. jun 2023. godine, Kragujevac / VI Symposium of a Serbian proteomic society: „Discussion and Application of  New Methods of Proteomics,“ Book of abstratcs,
T1  - Biocorona formation of hen egg white proteins onto the surface of polystyrene and polyethylene terephthalate
SP  - OP10
EP  - OP10
UR  - https://hdl.handle.net/21.15107/rcub_cer_6898
ER  - 

@conference{
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 = "2023",
abstract = "Ovalbumin (OVA), a main protein of egg white, has characteristic structural fold of a
serpin-family of proteins, propensity to fibril formation and stability to digestion.
Microplastics (MPs) contaminating our food can interact with food proteins in the food
matrix and during digestion. In this study adsorption of OVA to polystyrene (PS) (110 μm
and 260 μm), polyethylene terephthalate (PET) (140 μm) MPs were investigated in acidic
(pH 3) and neutral (pH 7) conditions. Formations of corona on MPs were investigated
using isolated OVA and egg white protein extract comparatively. OVA adsorption depends
on MPs size, polymer chemistry and pH, being highest in acidic pH and higher for PS.
Adsorption of OVA to PS and PET reaches dynamic equilibrium after 4h resulting in
disruption of tertiary structure and formation of hard and soft corona around MPs. Shorter
fragments of OVA populate hard corona, while soft corona exclusively consist of full
length OVA, albeit in its non-native conformation. The conformational changes resemble
those induced by heat treatment with re-arrangement of α-β secondary structures.
Structural changes are striking for the OVA in corona around MPs. Soft corona OVA
preserves thermal and proteolytic stability, but loses ability to form fibrils upon heating.
OVA is abundantly present in corona around MPs also in the presence of other egg white
proteins. MPs contaminating food may bind and change structure and functional properties
of main egg white protein.",
publisher = "Kragujevac, Srbija : Prirodno-matematički fakultet, Univerzitet u Kragujevcu /  Kragujevac, Serbia : Faculty of Science, University of Kragujevac",
journal = "VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike,” Zbornik apstrakata, 2. jun 2023. godine, Kragujevac / VI Symposium of a Serbian proteomic society: „Discussion and Application of  New Methods of Proteomics,“ Book of abstratcs,",
title = "Biocorona formation of hen egg white proteins onto the surface of polystyrene and polyethylene terephthalate",
pages = "OP10-OP10",
url = "https://hdl.handle.net/21.15107/rcub_cer_6898"
}

Gligorijević, N., Lujić, T., Mutić, T., Vasović, T., de Guzman, M. K., Aćimović, J., Stanić-Vučinić, D.,& Ćirković Veličković, T.. (2023). Biocorona formation of hen egg white proteins onto the surface of polystyrene and polyethylene terephthalate. in VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike,” Zbornik apstrakata, 2. jun 2023. godine, Kragujevac / VI Symposium of a Serbian proteomic society: „Discussion and Application of  New Methods of Proteomics,“ Book of abstratcs,
Kragujevac, Srbija : Prirodno-matematički fakultet, Univerzitet u Kragujevcu /  Kragujevac, Serbia : Faculty of Science, University of Kragujevac., OP10-OP10.
https://hdl.handle.net/21.15107/rcub_cer_6898

Gligorijević N, Lujić T, Mutić T, Vasović T, de Guzman MK, Aćimović J, Stanić-Vučinić D, Ćirković Veličković T. Biocorona formation of hen egg white proteins onto the surface of polystyrene and polyethylene terephthalate. in VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike,” Zbornik apstrakata, 2. jun 2023. godine, Kragujevac / VI Symposium of a Serbian proteomic society: „Discussion and Application of  New Methods of Proteomics,“ Book of abstratcs,. 2023;:OP10-OP10.
https://hdl.handle.net/21.15107/rcub_cer_6898 .

Gligorijević, Nikola, Lujić, Tamara, Mutić, Tamara, Vasović, Tamara, de Guzman, Maria Krishna, Aćimović, Jelena, Stanić-Vučinić, Dragana, Ćirković Veličković, Tanja, "Biocorona formation of hen egg white proteins onto the surface of polystyrene and polyethylene terephthalate" in VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike,” Zbornik apstrakata, 2. jun 2023. godine, Kragujevac / VI Symposium of a Serbian proteomic society: „Discussion and Application of  New Methods of Proteomics,“ Book of abstratcs, (2023):OP10-OP10,
https://hdl.handle.net/21.15107/rcub_cer_6898 .

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 .

TY  - JOUR
AU  - de Guzman, Maria Krishna
AU  - Stanić-Vučinić, Dragana
AU  - Gligorijević, Nikola
AU  - Wimmer, Lukas
AU  - Gasparyan, Manvel
AU  - Lujić, Tamara
AU  - Vasović, Tamara
AU  - Dailey, Lea Ann
AU  - Van Haute, Sam
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6466
AB  - Human ingestion of microplastics (MPs) is common and inevitable due to the widespread contamination of food items, but implications on the gastric digestion of food proteins are still unknown. In this study, the interactions between pepsin and polystyrene (PS) MPs were evaluated by investigating enzyme activity and conformation in a simulated human gastric environment in the presence or absence of PS MPs. The impact on food digestion was also assessed by monitoring the kinetics of protein hydrolysis through static in vitro gastric digestion of cow's milk contaminated with PS. The binding of pepsin to PS showed that the surface chemistry of MPs dictates binding affinity. The key contributor to pepsin adsorption seems to be π−π interactions between the aromatic residues and the PS phenyl rings. During quick exposure (10 min) of pepsin to increasing concentrations (222, 2219, 22188 particles/mL) of 10 μm PS (PS10) and 100 μm PS (PS100), total enzymatic activities were not affected remarkably. However, upon prolonged exposure at 1 and 2 h, preferential binding of pepsin to the small, low zeta-potential PS caused structural changes in the protein which led to a significant reduction of its activity. Digestion of cow's milk mixed with PS10 resulted in transient accumulation of larger peptides (10–35 kDa) and reduced bioavailability of short peptides (2–9 kDa) in the gastric phase. This, however, was only observed at extremely high PS10 concentration (0.3 mg/mL or 5.46E+05 particles/mL). The digestion of milk peptides, bound preferentially over pepsin within the hard corona on the PS10 surface, was delayed up to 15 min in comparison to bulk protein digestion. Intact caseins, otherwise rapidly digested, remained bound to PS10 in the hard corona for up to 15 min. This work presents valuable insights regarding the interaction of MPs, food proteins, and pepsin, and their dynamics during gastric digestion.
PB  - Elsevier Ltd.
T2  - Environmental Pollution
T1  - Small polystyrene microplastics interfere with the breakdown of milk proteins during static in vitro simulated human gastric digestion
VL  - 335
SP  - 122282
DO  - 10.1016/j.envpol.2023.122282
ER  - 

@article{
author = "de Guzman, Maria Krishna and Stanić-Vučinić, Dragana and Gligorijević, Nikola and Wimmer, Lukas and Gasparyan, Manvel and Lujić, Tamara and Vasović, Tamara and Dailey, Lea Ann and Van Haute, Sam and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "Human ingestion of microplastics (MPs) is common and inevitable due to the widespread contamination of food items, but implications on the gastric digestion of food proteins are still unknown. In this study, the interactions between pepsin and polystyrene (PS) MPs were evaluated by investigating enzyme activity and conformation in a simulated human gastric environment in the presence or absence of PS MPs. The impact on food digestion was also assessed by monitoring the kinetics of protein hydrolysis through static in vitro gastric digestion of cow's milk contaminated with PS. The binding of pepsin to PS showed that the surface chemistry of MPs dictates binding affinity. The key contributor to pepsin adsorption seems to be π−π interactions between the aromatic residues and the PS phenyl rings. During quick exposure (10 min) of pepsin to increasing concentrations (222, 2219, 22188 particles/mL) of 10 μm PS (PS10) and 100 μm PS (PS100), total enzymatic activities were not affected remarkably. However, upon prolonged exposure at 1 and 2 h, preferential binding of pepsin to the small, low zeta-potential PS caused structural changes in the protein which led to a significant reduction of its activity. Digestion of cow's milk mixed with PS10 resulted in transient accumulation of larger peptides (10–35 kDa) and reduced bioavailability of short peptides (2–9 kDa) in the gastric phase. This, however, was only observed at extremely high PS10 concentration (0.3 mg/mL or 5.46E+05 particles/mL). The digestion of milk peptides, bound preferentially over pepsin within the hard corona on the PS10 surface, was delayed up to 15 min in comparison to bulk protein digestion. Intact caseins, otherwise rapidly digested, remained bound to PS10 in the hard corona for up to 15 min. This work presents valuable insights regarding the interaction of MPs, food proteins, and pepsin, and their dynamics during gastric digestion.",
publisher = "Elsevier Ltd.",
journal = "Environmental Pollution",
title = "Small polystyrene microplastics interfere with the breakdown of milk proteins during static in vitro simulated human gastric digestion",
volume = "335",
pages = "122282",
doi = "10.1016/j.envpol.2023.122282"
}

de Guzman, M. K., Stanić-Vučinić, D., Gligorijević, N., Wimmer, L., Gasparyan, M., Lujić, T., Vasović, T., Dailey, L. A., Van Haute, S.,& Ćirković-Veličković, T.. (2023). Small polystyrene microplastics interfere with the breakdown of milk proteins during static in vitro simulated human gastric digestion. in Environmental Pollution
Elsevier Ltd.., 335, 122282.
https://doi.org/10.1016/j.envpol.2023.122282

de Guzman MK, Stanić-Vučinić D, Gligorijević N, Wimmer L, Gasparyan M, Lujić T, Vasović T, Dailey LA, Van Haute S, Ćirković-Veličković T. Small polystyrene microplastics interfere with the breakdown of milk proteins during static in vitro simulated human gastric digestion. in Environmental Pollution. 2023;335:122282.
doi:10.1016/j.envpol.2023.122282 .

de Guzman, Maria Krishna, Stanić-Vučinić, Dragana, Gligorijević, Nikola, Wimmer, Lukas, Gasparyan, Manvel, Lujić, Tamara, Vasović, Tamara, Dailey, Lea Ann, Van Haute, Sam, Ćirković-Veličković, Tanja, "Small polystyrene microplastics interfere with the breakdown of milk proteins during static in vitro simulated human gastric digestion" in Environmental Pollution, 335 (2023):122282,
https://doi.org/10.1016/j.envpol.2023.122282 . .

TY  - CONF
AU  - Vasović, Tamara
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Nikolić, Milan
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6821
AB  - Oxidative stress undoubtedly accompanies mental disorders, and
the pleiotropic effects of atypical antipsychotics, recommended
drugs in the treatment of psychosis, are not clarified at the
molecular level. Catalase is one of the key enzymes of the primary
antioxidant protection system. This work studied the binding
of second-generation antipsychotic drug Clozapine to
commercial bovine liver catalase. Using various spectroscopic
methods under simulated physiological conditions, we found
moderate binding affinity of clozapine for catalase (Ka ~ 2x105
M-1), the binding influenced the secondary and tertiary structure
of protein (according to UV-VIS and CD spectroscopy) and it
managed to slightly increase its thermal stability. In AAPH
induced oxidation experiments, we found that clozapine efficiently
protects catalase from free-radicals oxidation and preserves
its activity. Clozapine affects catalase activity in dose
dependant manner, having no significant effect at lower concentrations
but significantly inhibiting enzyme at saturating concentrations.
In conclusion, our results indicate that the effect of
direct binding of clozapine to catalase can be both beneficial and
harmful and that this effect is dose dependent.
PB  - Wiley
C3  - FEBS Open Bio
T1  - Antipsychotic clozapine binds catalase and preserves its activity in oxidative environment
VL  - 12
IS  - Supplement 1
SP  - 264
EP  - 264
DO  - 10.1002/2211-5463.13440
ER  - 

@conference{
author = "Vasović, Tamara and Gligorijević, Nikola and Minić, Simeon and Nikolić, Milan",
year = "2022",
abstract = "Oxidative stress undoubtedly accompanies mental disorders, and
the pleiotropic effects of atypical antipsychotics, recommended
drugs in the treatment of psychosis, are not clarified at the
molecular level. Catalase is one of the key enzymes of the primary
antioxidant protection system. This work studied the binding
of second-generation antipsychotic drug Clozapine to
commercial bovine liver catalase. Using various spectroscopic
methods under simulated physiological conditions, we found
moderate binding affinity of clozapine for catalase (Ka ~ 2x105
M-1), the binding influenced the secondary and tertiary structure
of protein (according to UV-VIS and CD spectroscopy) and it
managed to slightly increase its thermal stability. In AAPH
induced oxidation experiments, we found that clozapine efficiently
protects catalase from free-radicals oxidation and preserves
its activity. Clozapine affects catalase activity in dose
dependant manner, having no significant effect at lower concentrations
but significantly inhibiting enzyme at saturating concentrations.
In conclusion, our results indicate that the effect of
direct binding of clozapine to catalase can be both beneficial and
harmful and that this effect is dose dependent.",
publisher = "Wiley",
journal = "FEBS Open Bio",
title = "Antipsychotic clozapine binds catalase and preserves its activity in oxidative environment",
volume = "12",
number = "Supplement 1",
pages = "264-264",
doi = "10.1002/2211-5463.13440"
}

Vasović, T., Gligorijević, N., Minić, S.,& Nikolić, M.. (2022). Antipsychotic clozapine binds catalase and preserves its activity in oxidative environment. in FEBS Open Bio
Wiley., 12(Supplement 1), 264-264.
https://doi.org/10.1002/2211-5463.13440

Vasović T, Gligorijević N, Minić S, Nikolić M. Antipsychotic clozapine binds catalase and preserves its activity in oxidative environment. in FEBS Open Bio. 2022;12(Supplement 1):264-264.
doi:10.1002/2211-5463.13440 .

Vasović, Tamara, Gligorijević, Nikola, Minić, Simeon, Nikolić, Milan, "Antipsychotic clozapine binds catalase and preserves its activity in oxidative environment" in FEBS Open Bio, 12, no. Supplement 1 (2022):264-264,
https://doi.org/10.1002/2211-5463.13440 . .

TY  - JOUR
AU  - Vujatović, Tamara B.
AU  - Vitorović - Todorović, Maja D.
AU  - Cvijetić, Ilija
AU  - Vasović, Tamara
AU  - Nikolić, Milan R.
AU  - Novaković, Irena
AU  - Bjelogrlić, Snežana
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4853
AB  - In the present work, the α, β-double bond of the aroylacrylic acid phenylamides was suitably modified to optimize the toxicity–antiproliferative activity ratio of the resulting compounds 1 –5 . The phenylamides were modified by Michael’s addition of suitably chosen piperidine-containing fragments: 1-amino-N- benzylpiperidine ( a1 ), 4-benzylpiperidine ( a2 ), and N , N -dimethyl- N -[2-(1-piperazinyl)-ethyl]amine ( a3 ). The compounds exerted micromolar activity toward three cancer cell lines, A549, LoVo, and Skov-3, caus- ing apoptotic cell death. It was shown that the nature of the cyclic amine moiety at position C2 of the compounds is probably the primary determinant of anticancer activity toward tested cell lines and the acute toxicity toward brine shrimp ( Artemia salina ). The majority of compounds revealed the ability to vigorously induce mitochondrial superoxide anion generation in all treated cell lines, which together with cell cycle arrest at the S phase and activation of intrinsic caspase cascade, indicates the possibility that apoptosis was triggered due to irreparable chromosomal damage by acute oxidative stress. Two deriva- tives also exerted significant antibacterial activity with one order of magnitude higher potency than chlo- ramphenicol in most of the investigated bacterial strains. Also, the drug-like properties for all compounds were estimated by available software tools.
PB  - Elsevier
T2  - Journal of Molecular Structure
T1  - Novel derivatives of aroylacrylic acid phenylamides as inducers of apoptosis through the ROS-mediated pathway in several cancer cell lines
VL  - 1250
SP  - 131702
DO  - 10.1016/j.molstruc.2021.131702
ER  - 

@article{
author = "Vujatović, Tamara B. and Vitorović - Todorović, Maja D. and Cvijetić, Ilija and Vasović, Tamara and Nikolić, Milan R. and Novaković, Irena and Bjelogrlić, Snežana",
year = "2022",
abstract = "In the present work, the α, β-double bond of the aroylacrylic acid phenylamides was suitably modified to optimize the toxicity–antiproliferative activity ratio of the resulting compounds 1 –5 . The phenylamides were modified by Michael’s addition of suitably chosen piperidine-containing fragments: 1-amino-N- benzylpiperidine ( a1 ), 4-benzylpiperidine ( a2 ), and N , N -dimethyl- N -[2-(1-piperazinyl)-ethyl]amine ( a3 ). The compounds exerted micromolar activity toward three cancer cell lines, A549, LoVo, and Skov-3, caus- ing apoptotic cell death. It was shown that the nature of the cyclic amine moiety at position C2 of the compounds is probably the primary determinant of anticancer activity toward tested cell lines and the acute toxicity toward brine shrimp ( Artemia salina ). The majority of compounds revealed the ability to vigorously induce mitochondrial superoxide anion generation in all treated cell lines, which together with cell cycle arrest at the S phase and activation of intrinsic caspase cascade, indicates the possibility that apoptosis was triggered due to irreparable chromosomal damage by acute oxidative stress. Two deriva- tives also exerted significant antibacterial activity with one order of magnitude higher potency than chlo- ramphenicol in most of the investigated bacterial strains. Also, the drug-like properties for all compounds were estimated by available software tools.",
publisher = "Elsevier",
journal = "Journal of Molecular Structure",
title = "Novel derivatives of aroylacrylic acid phenylamides as inducers of apoptosis through the ROS-mediated pathway in several cancer cell lines",
volume = "1250",
pages = "131702",
doi = "10.1016/j.molstruc.2021.131702"
}

Vujatović, T. B., Vitorović - Todorović, M. D., Cvijetić, I., Vasović, T., Nikolić, M. R., Novaković, I.,& Bjelogrlić, S.. (2022). Novel derivatives of aroylacrylic acid phenylamides as inducers of apoptosis through the ROS-mediated pathway in several cancer cell lines. in Journal of Molecular Structure
Elsevier., 1250, 131702.
https://doi.org/10.1016/j.molstruc.2021.131702

Vujatović TB, Vitorović - Todorović MD, Cvijetić I, Vasović T, Nikolić MR, Novaković I, Bjelogrlić S. Novel derivatives of aroylacrylic acid phenylamides as inducers of apoptosis through the ROS-mediated pathway in several cancer cell lines. in Journal of Molecular Structure. 2022;1250:131702.
doi:10.1016/j.molstruc.2021.131702 .

Vujatović, Tamara B., Vitorović - Todorović, Maja D., Cvijetić, Ilija, Vasović, Tamara, Nikolić, Milan R., Novaković, Irena, Bjelogrlić, Snežana, "Novel derivatives of aroylacrylic acid phenylamides as inducers of apoptosis through the ROS-mediated pathway in several cancer cell lines" in Journal of Molecular Structure, 1250 (2022):131702,
https://doi.org/10.1016/j.molstruc.2021.131702 . .

TY  - JOUR
AU  - Vujatović, Tamara B.
AU  - Vitorović - Todorović, Maja D.
AU  - Cvijetić, Ilija
AU  - Vasović, Tamara
AU  - Nikolić, Milan R.
AU  - Novaković, Irena
AU  - Bjelogrlić, Snežana
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4857
AB  - In the present work, the α, β-double bond of the aroylacrylic acid phenylamides was suitably modified to optimize the toxicity–antiproliferative activity ratio of the resulting compounds 1 –5 . The phenylamides were modified by Michael’s addition of suitably chosen piperidine-containing fragments: 1-amino-N- benzylpiperidine ( a1 ), 4-benzylpiperidine ( a2 ), and N , N -dimethyl- N -[2-(1-piperazinyl)-ethyl]amine ( a3 ). The compounds exerted micromolar activity toward three cancer cell lines, A549, LoVo, and Skov-3, caus- ing apoptotic cell death. It was shown that the nature of the cyclic amine moiety at position C2 of the compounds is probably the primary determinant of anticancer activity toward tested cell lines and the acute toxicity toward brine shrimp ( Artemia salina ). The majority of compounds revealed the ability to vigorously induce mitochondrial superoxide anion generation in all treated cell lines, which together with cell cycle arrest at the S phase and activation of intrinsic caspase cascade, indicates the possibility that apoptosis was triggered due to irreparable chromosomal damage by acute oxidative stress. Two deriva- tives also exerted significant antibacterial activity with one order of magnitude higher potency than chlo- ramphenicol in most of the investigated bacterial strains. Also, the drug-like properties for all compounds were estimated by available software tools.
PB  - Elsevier
T2  - Journal of Molecular Structure
T1  - Novel derivatives of aroylacrylic acid phenylamides as inducers of apoptosis through the ROS-mediated pathway in several cancer cell lines
VL  - 1250
SP  - 131702
DO  - 10.1016/j.molstruc.2021.131702
ER  - 

@article{
author = "Vujatović, Tamara B. and Vitorović - Todorović, Maja D. and Cvijetić, Ilija and Vasović, Tamara and Nikolić, Milan R. and Novaković, Irena and Bjelogrlić, Snežana",
year = "2022",
abstract = "In the present work, the α, β-double bond of the aroylacrylic acid phenylamides was suitably modified to optimize the toxicity–antiproliferative activity ratio of the resulting compounds 1 –5 . The phenylamides were modified by Michael’s addition of suitably chosen piperidine-containing fragments: 1-amino-N- benzylpiperidine ( a1 ), 4-benzylpiperidine ( a2 ), and N , N -dimethyl- N -[2-(1-piperazinyl)-ethyl]amine ( a3 ). The compounds exerted micromolar activity toward three cancer cell lines, A549, LoVo, and Skov-3, caus- ing apoptotic cell death. It was shown that the nature of the cyclic amine moiety at position C2 of the compounds is probably the primary determinant of anticancer activity toward tested cell lines and the acute toxicity toward brine shrimp ( Artemia salina ). The majority of compounds revealed the ability to vigorously induce mitochondrial superoxide anion generation in all treated cell lines, which together with cell cycle arrest at the S phase and activation of intrinsic caspase cascade, indicates the possibility that apoptosis was triggered due to irreparable chromosomal damage by acute oxidative stress. Two deriva- tives also exerted significant antibacterial activity with one order of magnitude higher potency than chlo- ramphenicol in most of the investigated bacterial strains. Also, the drug-like properties for all compounds were estimated by available software tools.",
publisher = "Elsevier",
journal = "Journal of Molecular Structure",
title = "Novel derivatives of aroylacrylic acid phenylamides as inducers of apoptosis through the ROS-mediated pathway in several cancer cell lines",
volume = "1250",
pages = "131702",
doi = "10.1016/j.molstruc.2021.131702"
}

Vujatović, T. B., Vitorović - Todorović, M. D., Cvijetić, I., Vasović, T., Nikolić, M. R., Novaković, I.,& Bjelogrlić, S.. (2022). Novel derivatives of aroylacrylic acid phenylamides as inducers of apoptosis through the ROS-mediated pathway in several cancer cell lines. in Journal of Molecular Structure
Elsevier., 1250, 131702.
https://doi.org/10.1016/j.molstruc.2021.131702

Vujatović TB, Vitorović - Todorović MD, Cvijetić I, Vasović T, Nikolić MR, Novaković I, Bjelogrlić S. Novel derivatives of aroylacrylic acid phenylamides as inducers of apoptosis through the ROS-mediated pathway in several cancer cell lines. in Journal of Molecular Structure. 2022;1250:131702.
doi:10.1016/j.molstruc.2021.131702 .

Vujatović, Tamara B., Vitorović - Todorović, Maja D., Cvijetić, Ilija, Vasović, Tamara, Nikolić, Milan R., Novaković, Irena, Bjelogrlić, Snežana, "Novel derivatives of aroylacrylic acid phenylamides as inducers of apoptosis through the ROS-mediated pathway in several cancer cell lines" in Journal of Molecular Structure, 1250 (2022):131702,
https://doi.org/10.1016/j.molstruc.2021.131702 . .

TY  - JOUR
AU  - Minić, Simeon
AU  - Radomirović, Mirjana
AU  - Savkovic, Nina
AU  - Radibratović, Milica
AU  - Mihailović, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković Veličković, Tanja
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2420
AB  - In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions
VL  - 269
SP  - 43
EP  - 52
DO  - 10.1016/j.foodchem.2018.06.138
ER  - 

@article{
author = "Minić, Simeon and Radomirović, Mirjana and Savkovic, Nina and Radibratović, Milica and Mihailović, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš and Stanić-Vučinić, Dragana and Ćirković Veličković, Tanja",
year = "2018",
abstract = "In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions",
volume = "269",
pages = "43-52",
doi = "10.1016/j.foodchem.2018.06.138"
}

Minić, S., Radomirović, M., Savkovic, N., Radibratović, M., Mihailović, J., Vasović, T., Nikolić, M., Milčić, M., Stanić-Vučinić, D.,& Ćirković Veličković, T.. (2018). Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. in Food Chemistry
Elsevier Sci Ltd, Oxford., 269, 43-52.
https://doi.org/10.1016/j.foodchem.2018.06.138

Minić S, Radomirović M, Savkovic N, Radibratović M, Mihailović J, Vasović T, Nikolić M, Milčić M, Stanić-Vučinić D, Ćirković Veličković T. Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. in Food Chemistry. 2018;269:43-52.
doi:10.1016/j.foodchem.2018.06.138 .

Minić, Simeon, Radomirović, Mirjana, Savkovic, Nina, Radibratović, Milica, Mihailović, Jelena, Vasović, Tamara, Nikolić, Milan, Milčić, Miloš, Stanić-Vučinić, Dragana, Ćirković Veličković, Tanja, "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions" in Food Chemistry, 269 (2018):43-52,
https://doi.org/10.1016/j.foodchem.2018.06.138 . .

TY  - JOUR
AU  - Minić, Simeon
AU  - Radomirović, Mirjana
AU  - Savkovic, Nina
AU  - Radibratović, Milica
AU  - Mihailović, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković Veličković, Tanja
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3022
AB  - In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions
VL  - 269
SP  - 43
EP  - 52
DO  - 10.1016/j.foodchem.2018.06.138
ER  - 

@article{
author = "Minić, Simeon and Radomirović, Mirjana and Savkovic, Nina and Radibratović, Milica and Mihailović, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš and Stanić-Vučinić, Dragana and Ćirković Veličković, Tanja",
year = "2018",
abstract = "In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions",
volume = "269",
pages = "43-52",
doi = "10.1016/j.foodchem.2018.06.138"
}

Minić, S., Radomirović, M., Savkovic, N., Radibratović, M., Mihailović, J., Vasović, T., Nikolić, M., Milčić, M., Stanić-Vučinić, D.,& Ćirković Veličković, T.. (2018). Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. in Food Chemistry
Elsevier Sci Ltd, Oxford., 269, 43-52.
https://doi.org/10.1016/j.foodchem.2018.06.138

Minić S, Radomirović M, Savkovic N, Radibratović M, Mihailović J, Vasović T, Nikolić M, Milčić M, Stanić-Vučinić D, Ćirković Veličković T. Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. in Food Chemistry. 2018;269:43-52.
doi:10.1016/j.foodchem.2018.06.138 .

Minić, Simeon, Radomirović, Mirjana, Savkovic, Nina, Radibratović, Milica, Mihailović, Jelena, Vasović, Tamara, Nikolić, Milan, Milčić, Miloš, Stanić-Vučinić, Dragana, Ćirković Veličković, Tanja, "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions" in Food Chemistry, 269 (2018):43-52,
https://doi.org/10.1016/j.foodchem.2018.06.138 . .