Stanić-Vučinić, Dragana

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Authority KeyName Variants
orcid::0000-0003-2576-3074
  • Stanić-Vučinić, Dragana (67)
  • Stanić, Dragana (14)
Projects
Molecular properties and modifications of some respiratory and nutritional allergens Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research
FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics Rational design and synthesis of biologically active and coordination compounds and functional materials, relevant for (bio)nanotechnology
Ispitivanje strukture i funkcije biološki važnih makromolekula u fiziološkim i patološkim stanjima COST Action [FA 1005]
Ghent University Global Campus, Belgian Special Research Fund BOF StG No. 01N01718. Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200168 (University of Belgrade, Faculty of Chemistry)
Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200288 (Innovation Center of the Faculty of Chemistry) Hemijske i biohemijske konsekvence metal-ligand interakcija, II. deo
Serbian Academy of Sciences and Arts Project F-26. COST Action [FA1402]
Modeling and Numerical Simulations of Complex Many-Body Systems CAPSIDO – Developement of the assays for detection of SARS Cov-2 virus capsid proteins in biological fluids of COVID19 patients
Serbian Academy of Sciences and Arts GA No. F-26. UNDP project "Preventing and Responding to COVID-19 in At-risk areas - Sustainable production of the serological IgG test for SARS CoV-2 in Serbia".
Austrian Federal Ministry of Economy Austrian Research Promotion Agency (FFG Project) [822768]
COST Action [928] COST Action [FA1005]
COST Actions [928, FA1005] Immunomodulatory effects of environmental xenobiotics and biotic factors on the populations of mouse-like rodents
Razvoj novih terapijskih postupaka u prevenciji i lečenju bolesti jetre: Uloga i mehanizam delovanja polinezasićenih masnih kiselina Laura Bassi Centers of Expertise program
MEST, MEST-CT-2005-020924 Stockholm County Council
Swedish Research Council The Serbian Academy of Sciences and Arts, grant number F-26
UK Biological and Biotechnological Sciences Research Council

Author's Bibliography

Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2

Đukić, Teodora; Mladenović, Maja; Stanić-Vučinić, Dragana; Radosavljević, Jelena; Smiljanić, Katarina; Sabljić, Ljiljana; Dević, Marija; Ćujić, Danica; Vasović, Tamara; Simović, Ana; Radomirović, Mirjana Ž.; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - JOUR
AU  - Đukić, Teodora
AU  - Mladenović, Maja
AU  - Stanić-Vučinić, Dragana
AU  - Radosavljević, Jelena
AU  - Smiljanić, Katarina
AU  - Sabljić, Ljiljana
AU  - Dević, Marija
AU  - Ćujić, Danica
AU  - Vasović, Tamara
AU  - Simović, Ana
AU  - Radomirović, Mirjana Ž.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4330
AB  - Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production.

SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified and characterized biochemically and immunologically.

Purified rfNP has secondary structure of full-length recombinant N protein, with high percentage of disordered structure (34.2%) and of β-sheet (40.7%). rfNP was tested in immunoblot using sera of COVID-19 convalescent patients. ELISA was optimized with sera of RT-PCR confirmed positive symptomatic patients and healthy individuals. IgG detection sensitivity was 96% (47/50) and specificity 97% (67/68), while IgM detection was slightly lower (94% and 96.5%, respectively).

Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection.
PB  - Elsevier
T2  - Virology journal
T1  - Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2
VL  - 557
SP  - 15
EP  - 22
DO  - 10.1016/j.virol.2021.01.004
ER  - 
@article{
author = "Đukić, Teodora and Mladenović, Maja and Stanić-Vučinić, Dragana and Radosavljević, Jelena and Smiljanić, Katarina and Sabljić, Ljiljana and Dević, Marija and Ćujić, Danica and Vasović, Tamara and Simović, Ana and Radomirović, Mirjana Ž. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production.

SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified and characterized biochemically and immunologically.

Purified rfNP has secondary structure of full-length recombinant N protein, with high percentage of disordered structure (34.2%) and of β-sheet (40.7%). rfNP was tested in immunoblot using sera of COVID-19 convalescent patients. ELISA was optimized with sera of RT-PCR confirmed positive symptomatic patients and healthy individuals. IgG detection sensitivity was 96% (47/50) and specificity 97% (67/68), while IgM detection was slightly lower (94% and 96.5%, respectively).

Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection.",
publisher = "Elsevier",
journal = "Virology journal",
title = "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2",
volume = "557",
pages = "15-22",
doi = "10.1016/j.virol.2021.01.004"
}
Đukić, T., Mladenović, M., Stanić-Vučinić, D., Radosavljević, J., Smiljanić, K., Sabljić, L., Dević, M., Ćujić, D., Vasović, T., Simović, A., Radomirović, M. Ž.,& Ćirković-Veličković, T.. (2021). Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2. in Virology journal
Elsevier., 557, 15-22.
https://doi.org/10.1016/j.virol.2021.01.004
Đukić T, Mladenović M, Stanić-Vučinić D, Radosavljević J, Smiljanić K, Sabljić L, Dević M, Ćujić D, Vasović T, Simović A, Radomirović MŽ, Ćirković-Veličković T. Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2. in Virology journal. 2021;557:15-22.
doi:10.1016/j.virol.2021.01.004 .
Đukić, Teodora, Mladenović, Maja, Stanić-Vučinić, Dragana, Radosavljević, Jelena, Smiljanić, Katarina, Sabljić, Ljiljana, Dević, Marija, Ćujić, Danica, Vasović, Tamara, Simović, Ana, Radomirović, Mirjana Ž., Ćirković-Veličković, Tanja, "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2" in Virology journal, 557 (2021):15-22,
https://doi.org/10.1016/j.virol.2021.01.004 . .
5
8
2
2

Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2

Đukić, Teodora; Mladenović, Maja; Stanić-Vučinić, Dragana; Radosavljević, Jelena; Smiljanić, Katarina; Sabljić, Ljiljana; Dević, Marija; Ćujić, Danica; Vasović, Tamara; Simović, Ana; Radomirović, Mirjana Ž.; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - JOUR
AU  - Đukić, Teodora
AU  - Mladenović, Maja
AU  - Stanić-Vučinić, Dragana
AU  - Radosavljević, Jelena
AU  - Smiljanić, Katarina
AU  - Sabljić, Ljiljana
AU  - Dević, Marija
AU  - Ćujić, Danica
AU  - Vasović, Tamara
AU  - Simović, Ana
AU  - Radomirović, Mirjana Ž.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4331
AB  - Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production.SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified and characterized biochemically and immunologically.Purified rfNP has secondary structure of full-length recombinant N protein, with high percentage of disordered structure (34.2%) and of β-sheet (40.7%). rfNP was tested in immunoblot using sera of COVID-19 convalescent patients. ELISA was optimized with sera of RT-PCR confirmed positive symptomatic patients and healthy individuals. IgG detection sensitivity was 96% (47/50) and specificity 97% (67/68), while IgM detection was slightly lower (94% and 96.5%, respectively).Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection.
PB  - Elsevier
T2  - Virology journal
T1  - Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2
VL  - 557
SP  - 15
EP  - 22
DO  - 10.1016/j.virol.2021.01.004
ER  - 
@article{
author = "Đukić, Teodora and Mladenović, Maja and Stanić-Vučinić, Dragana and Radosavljević, Jelena and Smiljanić, Katarina and Sabljić, Ljiljana and Dević, Marija and Ćujić, Danica and Vasović, Tamara and Simović, Ana and Radomirović, Mirjana Ž. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production.SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified and characterized biochemically and immunologically.Purified rfNP has secondary structure of full-length recombinant N protein, with high percentage of disordered structure (34.2%) and of β-sheet (40.7%). rfNP was tested in immunoblot using sera of COVID-19 convalescent patients. ELISA was optimized with sera of RT-PCR confirmed positive symptomatic patients and healthy individuals. IgG detection sensitivity was 96% (47/50) and specificity 97% (67/68), while IgM detection was slightly lower (94% and 96.5%, respectively).Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection.",
publisher = "Elsevier",
journal = "Virology journal",
title = "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2",
volume = "557",
pages = "15-22",
doi = "10.1016/j.virol.2021.01.004"
}
Đukić, T., Mladenović, M., Stanić-Vučinić, D., Radosavljević, J., Smiljanić, K., Sabljić, L., Dević, M., Ćujić, D., Vasović, T., Simović, A., Radomirović, M. Ž.,& Ćirković-Veličković, T.. (2021). Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2. in Virology journal
Elsevier., 557, 15-22.
https://doi.org/10.1016/j.virol.2021.01.004
Đukić T, Mladenović M, Stanić-Vučinić D, Radosavljević J, Smiljanić K, Sabljić L, Dević M, Ćujić D, Vasović T, Simović A, Radomirović MŽ, Ćirković-Veličković T. Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2. in Virology journal. 2021;557:15-22.
doi:10.1016/j.virol.2021.01.004 .
Đukić, Teodora, Mladenović, Maja, Stanić-Vučinić, Dragana, Radosavljević, Jelena, Smiljanić, Katarina, Sabljić, Ljiljana, Dević, Marija, Ćujić, Danica, Vasović, Tamara, Simović, Ana, Radomirović, Mirjana Ž., Ćirković-Veličković, Tanja, "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2" in Virology journal, 557 (2021):15-22,
https://doi.org/10.1016/j.virol.2021.01.004 . .
5
8
2
5

Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying

Peruško, Marija; Ghnimi, Sami; Simović, Ana; Stevanović, Nikola R.; Radomirović, Mirjana Ž.; Gharsallaoui, Adem; Smiljanić, Katarina; Van Haute, Sam; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - JOUR
AU  - Peruško, Marija
AU  - Ghnimi, Sami
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Radomirović, Mirjana Ž.
AU  - Gharsallaoui, Adem
AU  - Smiljanić, Katarina
AU  - Van Haute, Sam
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4332
AB  - Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.
PB  - Elsevier
T2  - LWT
T1  - Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying
VL  - 143
SP  - 111091
DO  - 10.1016/j.lwt.2021.111091
ER  - 
@article{
author = "Peruško, Marija and Ghnimi, Sami and Simović, Ana and Stevanović, Nikola R. and Radomirović, Mirjana Ž. and Gharsallaoui, Adem and Smiljanić, Katarina and Van Haute, Sam and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.",
publisher = "Elsevier",
journal = "LWT",
title = "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying",
volume = "143",
pages = "111091",
doi = "10.1016/j.lwt.2021.111091"
}
Peruško, M., Ghnimi, S., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Gharsallaoui, A., Smiljanić, K., Van Haute, S., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT
Elsevier., 143, 111091.
https://doi.org/10.1016/j.lwt.2021.111091
Peruško M, Ghnimi S, Simović A, Stevanović NR, Radomirović MŽ, Gharsallaoui A, Smiljanić K, Van Haute S, Stanić-Vučinić D, Ćirković-Veličković T. Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT. 2021;143:111091.
doi:10.1016/j.lwt.2021.111091 .
Peruško, Marija, Ghnimi, Sami, Simović, Ana, Stevanović, Nikola R., Radomirović, Mirjana Ž., Gharsallaoui, Adem, Smiljanić, Katarina, Van Haute, Sam, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying" in LWT, 143 (2021):111091,
https://doi.org/10.1016/j.lwt.2021.111091 . .
1
2
2
2

Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying

Peruško, Marija; Ghnimi, Sami; Simović, Ana; Stevanović, Nikola R.; Radomirović, Mirjana Ž.; Gharsallaoui, Adem; Smiljanić, Katarina; Van Haute, Sam; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - JOUR
AU  - Peruško, Marija
AU  - Ghnimi, Sami
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Radomirović, Mirjana Ž.
AU  - Gharsallaoui, Adem
AU  - Smiljanić, Katarina
AU  - Van Haute, Sam
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4333
AB  - Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.
PB  - Elsevier
T2  - LWT
T1  - Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying
VL  - 143
SP  - 111091
DO  - 10.1016/j.lwt.2021.111091
ER  - 
@article{
author = "Peruško, Marija and Ghnimi, Sami and Simović, Ana and Stevanović, Nikola R. and Radomirović, Mirjana Ž. and Gharsallaoui, Adem and Smiljanić, Katarina and Van Haute, Sam and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.",
publisher = "Elsevier",
journal = "LWT",
title = "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying",
volume = "143",
pages = "111091",
doi = "10.1016/j.lwt.2021.111091"
}
Peruško, M., Ghnimi, S., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Gharsallaoui, A., Smiljanić, K., Van Haute, S., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT
Elsevier., 143, 111091.
https://doi.org/10.1016/j.lwt.2021.111091
Peruško M, Ghnimi S, Simović A, Stevanović NR, Radomirović MŽ, Gharsallaoui A, Smiljanić K, Van Haute S, Stanić-Vučinić D, Ćirković-Veličković T. Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT. 2021;143:111091.
doi:10.1016/j.lwt.2021.111091 .
Peruško, Marija, Ghnimi, Sami, Simović, Ana, Stevanović, Nikola R., Radomirović, Mirjana Ž., Gharsallaoui, Adem, Smiljanić, Katarina, Van Haute, Sam, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying" in LWT, 143 (2021):111091,
https://doi.org/10.1016/j.lwt.2021.111091 . .
1
2
2
2

Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.

Peruško, Marija; Ghnimi, Sami; Simović, Ana; Stevanović, Nikola R.; Radomirović, Mirjana Ž.; Gharsallaoui, Adem; Smiljanić, Katarina; Van Haute, Sam; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - DATA
AU  - Peruško, Marija
AU  - Ghnimi, Sami
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Radomirović, Mirjana Ž.
AU  - Gharsallaoui, Adem
AU  - Smiljanić, Katarina
AU  - Van Haute, Sam
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4334
PB  - Elsevier
T2  - LWT
T1  - Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.
ER  - 
@misc{
author = "Peruško, Marija and Ghnimi, Sami and Simović, Ana and Stevanović, Nikola R. and Radomirović, Mirjana Ž. and Gharsallaoui, Adem and Smiljanić, Katarina and Van Haute, Sam and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
publisher = "Elsevier",
journal = "LWT",
title = "Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091."
}
Peruško, M., Ghnimi, S., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Gharsallaoui, A., Smiljanić, K., Van Haute, S., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.. in LWT
Elsevier..
Peruško M, Ghnimi S, Simović A, Stevanović NR, Radomirović MŽ, Gharsallaoui A, Smiljanić K, Van Haute S, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.. in LWT. 2021;..
Peruško, Marija, Ghnimi, Sami, Simović, Ana, Stevanović, Nikola R., Radomirović, Mirjana Ž., Gharsallaoui, Adem, Smiljanić, Katarina, Van Haute, Sam, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091." in LWT (2021).

Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability

Gligorijević, Nikola; Stanić-Vučinić, Dragana; Radomirović, Mirjana; Stojadinović, Marija M.; Khulal, Urmila; Nedić, Olgica; Ćirković-Veličković, Tanja

(MDPI, 2021)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana
AU  - Stojadinović, Marija M.
AU  - Khulal, Urmila
AU  - Nedić, Olgica
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://www.mdpi.com/1420-3049/26/10/2834
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4552
AB  - Resveratrol is a phytoalexin produced by many plants as a defense mechanism against stress-inducing conditions. The richest dietary sources of resveratrol are berries and grapes, their juices and wines. Good bioavailability of resveratrol is not reflected in its high biological activity in vivo because of resveratrol isomerization and its poor solubility in aqueous solutions. Proteins, cyclodextrins and nanomaterials have been explored as innovative delivery vehicles for resveratrol to overcome this limitation. Numerous in vitro and in vivo studies demonstrated beneficial effects of resveratrol in cardiovascular diseases (CVD). Main beneficial effects of resveratrol intake are cardioprotective, anti-hypertensive, vasodilatory, anti-diabetic, and improvement of lipid status. As resveratrol can alleviate the numerous factors associated with CVD, it has potential as a functional supplement to reduce COVID-19 illness severity in patients displaying poor prognosis due to cardio-vascular complications. Resveratrol was shown to mitigate the major pathways involved in the pathogenesis of SARS-CoV-2 including regulation of the renin-angiotensin system and expression of angiotensin-converting enzyme 2, stimulation of immune system and downregulation of pro-inflammatory cytokine release. Therefore, several studies already have anticipated potential implementation of resveratrol in COVID-19 treatment. Regular intake of a resveratrol rich diet, or resveratrol-based complementary medicaments, may contribute to a healthier cardio-vascular system, prevention and control of CVD, including COVID-19 disease related complications of CVD.
PB  - MDPI
T2  - Molecules
T1  - Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability
VL  - 26
IS  - 10
SP  - 2834
DO  - 10.3390/molecules26102834
ER  - 
@article{
author = "Gligorijević, Nikola and Stanić-Vučinić, Dragana and Radomirović, Mirjana and Stojadinović, Marija M. and Khulal, Urmila and Nedić, Olgica and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Resveratrol is a phytoalexin produced by many plants as a defense mechanism against stress-inducing conditions. The richest dietary sources of resveratrol are berries and grapes, their juices and wines. Good bioavailability of resveratrol is not reflected in its high biological activity in vivo because of resveratrol isomerization and its poor solubility in aqueous solutions. Proteins, cyclodextrins and nanomaterials have been explored as innovative delivery vehicles for resveratrol to overcome this limitation. Numerous in vitro and in vivo studies demonstrated beneficial effects of resveratrol in cardiovascular diseases (CVD). Main beneficial effects of resveratrol intake are cardioprotective, anti-hypertensive, vasodilatory, anti-diabetic, and improvement of lipid status. As resveratrol can alleviate the numerous factors associated with CVD, it has potential as a functional supplement to reduce COVID-19 illness severity in patients displaying poor prognosis due to cardio-vascular complications. Resveratrol was shown to mitigate the major pathways involved in the pathogenesis of SARS-CoV-2 including regulation of the renin-angiotensin system and expression of angiotensin-converting enzyme 2, stimulation of immune system and downregulation of pro-inflammatory cytokine release. Therefore, several studies already have anticipated potential implementation of resveratrol in COVID-19 treatment. Regular intake of a resveratrol rich diet, or resveratrol-based complementary medicaments, may contribute to a healthier cardio-vascular system, prevention and control of CVD, including COVID-19 disease related complications of CVD.",
publisher = "MDPI",
journal = "Molecules",
title = "Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability",
volume = "26",
number = "10",
pages = "2834",
doi = "10.3390/molecules26102834"
}
Gligorijević, N., Stanić-Vučinić, D., Radomirović, M., Stojadinović, M. M., Khulal, U., Nedić, O.,& Ćirković-Veličković, T.. (2021). Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability. in Molecules
MDPI., 26(10), 2834.
https://doi.org/10.3390/molecules26102834
Gligorijević N, Stanić-Vučinić D, Radomirović M, Stojadinović MM, Khulal U, Nedić O, Ćirković-Veličković T. Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability. in Molecules. 2021;26(10):2834.
doi:10.3390/molecules26102834 .
Gligorijević, Nikola, Stanić-Vučinić, Dragana, Radomirović, Mirjana, Stojadinović, Marija M., Khulal, Urmila, Nedić, Olgica, Ćirković-Veličković, Tanja, "Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability" in Molecules, 26, no. 10 (2021):2834,
https://doi.org/10.3390/molecules26102834 . .
1
6
1
2

The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c

Stanić-Vučinić, Dragana; Nikolić, Stefan; Vlajić, Katarina; Radomirović, Mirjana Ž.; Mihailović, Jelena; Ćirković-Veličković, Tanja; Grgurić-Šipka, Sanja

(Springer, 2020)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Vlajić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić-Šipka, Sanja
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3859
AB  - The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.
PB  - Springer
T2  - Journal of Biological Inorganic Chemistry
T1  - The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c
VL  - 25
IS  - 2
SP  - 253
EP  - 265
DO  - 10.1007/s00775-020-01758-3
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Nikolić, Stefan and Vlajić, Katarina and Radomirović, Mirjana Ž. and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić-Šipka, Sanja",
year = "2020",
abstract = "The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.",
publisher = "Springer",
journal = "Journal of Biological Inorganic Chemistry",
title = "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c",
volume = "25",
number = "2",
pages = "253-265",
doi = "10.1007/s00775-020-01758-3"
}
Stanić-Vučinić, D., Nikolić, S., Vlajić, K., Radomirović, M. Ž., Mihailović, J., Ćirković-Veličković, T.,& Grgurić-Šipka, S.. (2020). The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. in Journal of Biological Inorganic Chemistry
Springer., 25(2), 253-265.
https://doi.org/10.1007/s00775-020-01758-3
Stanić-Vučinić D, Nikolić S, Vlajić K, Radomirović MŽ, Mihailović J, Ćirković-Veličković T, Grgurić-Šipka S. The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. in Journal of Biological Inorganic Chemistry. 2020;25(2):253-265.
doi:10.1007/s00775-020-01758-3 .
Stanić-Vučinić, Dragana, Nikolić, Stefan, Vlajić, Katarina, Radomirović, Mirjana Ž., Mihailović, Jelena, Ćirković-Veličković, Tanja, Grgurić-Šipka, Sanja, "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c" in Journal of Biological Inorganic Chemistry, 25, no. 2 (2020):253-265,
https://doi.org/10.1007/s00775-020-01758-3 . .
3
3
3

Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3

Stanić-Vučinić, Dragana; Nikolić, Stefan; Vlajić, Katarina; Radomirović, Mirjana Ž.; Mihailović, Jelena; Ćirković-Veličković, Tanja; Grgurić-Šipka, Sanja

(Springer, 2020)

TY  - DATA
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Vlajić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić-Šipka, Sanja
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3863
PB  - Springer
T2  - Journal of Biological Inorganic Chemistry
T1  - Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3
ER  - 
@misc{
author = "Stanić-Vučinić, Dragana and Nikolić, Stefan and Vlajić, Katarina and Radomirović, Mirjana Ž. and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić-Šipka, Sanja",
year = "2020",
publisher = "Springer",
journal = "Journal of Biological Inorganic Chemistry",
title = "Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3"
}
Stanić-Vučinić, D., Nikolić, S., Vlajić, K., Radomirović, M. Ž., Mihailović, J., Ćirković-Veličković, T.,& Grgurić-Šipka, S.. (2020). Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3. in Journal of Biological Inorganic Chemistry
Springer..
Stanić-Vučinić D, Nikolić S, Vlajić K, Radomirović MŽ, Mihailović J, Ćirković-Veličković T, Grgurić-Šipka S. Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3. in Journal of Biological Inorganic Chemistry. 2020;..
Stanić-Vučinić, Dragana, Nikolić, Stefan, Vlajić, Katarina, Radomirović, Mirjana Ž., Mihailović, Jelena, Ćirković-Veličković, Tanja, Grgurić-Šipka, Sanja, "Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3" in Journal of Biological Inorganic Chemistry (2020).

The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c

Stanić-Vučinić, Dragana; Nikolić, Stefan; Vlajić, Katarina; Radomirović, Mirjana Ž.; Mihailović, Jelena; Ćirković-Veličković, Tanja; Grgurić-Šipka, Sanja

(Springer, 2020)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Vlajić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić-Šipka, Sanja
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3942
AB  - The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.
PB  - Springer
T2  - Journal of Biological Inorganic Chemistry
T1  - The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c
VL  - 25
IS  - 2
SP  - 253
EP  - 265
DO  - 10.1007/s00775-020-01758-3
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Nikolić, Stefan and Vlajić, Katarina and Radomirović, Mirjana Ž. and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić-Šipka, Sanja",
year = "2020",
abstract = "The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.",
publisher = "Springer",
journal = "Journal of Biological Inorganic Chemistry",
title = "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c",
volume = "25",
number = "2",
pages = "253-265",
doi = "10.1007/s00775-020-01758-3"
}
Stanić-Vučinić, D., Nikolić, S., Vlajić, K., Radomirović, M. Ž., Mihailović, J., Ćirković-Veličković, T.,& Grgurić-Šipka, S.. (2020). The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. in Journal of Biological Inorganic Chemistry
Springer., 25(2), 253-265.
https://doi.org/10.1007/s00775-020-01758-3
Stanić-Vučinić D, Nikolić S, Vlajić K, Radomirović MŽ, Mihailović J, Ćirković-Veličković T, Grgurić-Šipka S. The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. in Journal of Biological Inorganic Chemistry. 2020;25(2):253-265.
doi:10.1007/s00775-020-01758-3 .
Stanić-Vučinić, Dragana, Nikolić, Stefan, Vlajić, Katarina, Radomirović, Mirjana Ž., Mihailović, Jelena, Ćirković-Veličković, Tanja, Grgurić-Šipka, Sanja, "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c" in Journal of Biological Inorganic Chemistry, 25, no. 2 (2020):253-265,
https://doi.org/10.1007/s00775-020-01758-3 . .
3
3
3

Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study

Radibratović, Milica; Al-Hanish, Ayah; Minić, Simeon L.; Radomirović, Mirjana Ž.; Milčić, Miloš K.; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier, 2019)

TY  - JOUR
AU  - Radibratović, Milica
AU  - Al-Hanish, Ayah
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3733
AB  - α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. 

EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.
PB  - Elsevier
T2  - Food Chemistry
T1  - Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study
VL  - 278
SP  - 388
EP  - 395
DO  - 10.1016/j.foodchem.2018.11.038
ER  - 
@article{
author = "Radibratović, Milica and Al-Hanish, Ayah and Minić, Simeon L. and Radomirović, Mirjana Ž. and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. 

EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study",
volume = "278",
pages = "388-395",
doi = "10.1016/j.foodchem.2018.11.038"
}
Radibratović, M., Al-Hanish, A., Minić, S. L., Radomirović, M. Ž., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2019). Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. in Food Chemistry
Elsevier., 278, 388-395.
https://doi.org/10.1016/j.foodchem.2018.11.038
Radibratović M, Al-Hanish A, Minić SL, Radomirović MŽ, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. in Food Chemistry. 2019;278:388-395.
doi:10.1016/j.foodchem.2018.11.038 .
Radibratović, Milica, Al-Hanish, Ayah, Minić, Simeon L., Radomirović, Mirjana Ž., Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study" in Food Chemistry, 278 (2019):388-395,
https://doi.org/10.1016/j.foodchem.2018.11.038 . .
5
4
5

Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.; Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099. https://doi.org/10.1016/j.foodchem.2017.07.066

Minić, Simeon L.; Stanić-Vučinić, Dragana; Radomirović, Mirjana Ž.; Radibratović, Milica; Milčić, Miloš K.; Nikolić, Milan; Ćirković-Veličković, Tanja

(Elsevier, 2018)

TY  - DATA
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana Ž.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3139
PB  - Elsevier
T2  - Food Chemistry
T1  - Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066
ER  - 
@misc{
author = "Minić, Simeon L. and Stanić-Vučinić, Dragana and Radomirović, Mirjana Ž. and Radibratović, Milica and Milčić, Miloš K. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2018",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066"
}
Minić, S. L., Stanić-Vučinić, D., Radomirović, M. Ž., Radibratović, M., Milčić, M. K., Nikolić, M.,& Ćirković-Veličković, T.. (2018). Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066. in Food Chemistry
Elsevier..
Minić SL, Stanić-Vučinić D, Radomirović MŽ, Radibratović M, Milčić MK, Nikolić M, Ćirković-Veličković T. Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066. in Food Chemistry. 2018;..
Minić, Simeon L., Stanić-Vučinić, Dragana, Radomirović, Mirjana Ž., Radibratović, Milica, Milčić, Miloš K., Nikolić, Milan, Ćirković-Veličković, Tanja, "Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066" in Food Chemistry (2018).

Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions

Minić, Simeon L.; Radomirović, Mirjana Ž.; Savković, Nina; Radibratović, Milica; Mihailović-Vesić, Jelena; Vasović, Tamara; Nikolić, Milan; Milčić, Miloš K.; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2018)

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Savković, Nina
AU  - Radibratović, Milica
AU  - Mihailović-Vesić, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3186
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
UR  - Kon_3528
ER  - 
@article{
author = "Minić, Simeon L. and Radomirović, Mirjana Ž. and Savković, Nina and Radibratović, Milica and Mihailović-Vesić, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš K. 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",
url = "Kon_3528"
}
Minić, S. L., Radomirović, M. Ž., Savković, N., Radibratović, M., Mihailović-Vesić, J., Vasović, T., Nikolić, M., Milčić, M. K., 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
Kon_3528
Minić SL, Radomirović MŽ, Savković N, Radibratović M, Mihailović-Vesić J, Vasović T, Nikolić M, Milčić MK, 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
Kon_3528 .
Minić, Simeon L., Radomirović, Mirjana Ž., Savković, Nina, Radibratović, Milica, Mihailović-Vesić, Jelena, Vasović, Tamara, Nikolić, Milan, Milčić, Miloš K., 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 .,
Kon_3528 .
1
3
2
3

Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138

Minić, Simeon L.; Radomirović, Mirjana Ž.; Savković, Nina; Radibratović, Milica; Mihailović-Vesić, Jelena; Vasović, Tamara; Nikolić, Milan; Milčić, Miloš K.; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2018)

TY  - DATA
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Savković, Nina
AU  - Radibratović, Milica
AU  - Mihailović-Vesić, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3187
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138
ER  - 
@misc{
author = "Minić, Simeon L. and Radomirović, Mirjana Ž. and Savković, Nina and Radibratović, Milica and Mihailović-Vesić, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138"
}
Minić, S. L., Radomirović, M. Ž., Savković, N., Radibratović, M., Mihailović-Vesić, J., Vasović, T., Nikolić, M., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2018). Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138. in Food Chemistry
Elsevier Sci Ltd, Oxford..
Minić SL, Radomirović MŽ, Savković N, Radibratović M, Mihailović-Vesić J, Vasović T, Nikolić M, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138. in Food Chemistry. 2018;..
Minić, Simeon L., Radomirović, Mirjana Ž., Savković, Nina, Radibratović, Milica, Mihailović-Vesić, Jelena, Vasović, Tamara, Nikolić, Milan, Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138" in Food Chemistry (2018).

Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović-Vesić, Jelena; Radibratović, Milica; Radosavljević, Jelena; Burazer, Lidija M.; Milčić, Miloš K.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2155
AB  - BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
VL  - 48
IS  - 6
SP  - 731
EP  - 740
DO  - 10.1111/cea.13113
UR  - Kon_3486
ER  - 
@article{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
volume = "48",
number = "6",
pages = "731-740",
doi = "10.1111/cea.13113",
url = "Kon_3486"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T.. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy
Wiley, Hoboken., 48(6), 731-740.
https://doi.org/10.1111/cea.13113
Kon_3486
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, Ćirković-Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy. 2018;48(6):731-740.
doi:10.1111/cea.13113
Kon_3486 .
Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Mihailović-Vesić, Jelena, Radibratović, Milica, Radosavljević, Jelena, Burazer, Lidija M., Milčić, Miloš K., Smiljanić, Katarina, van Hage, Marianne, Ćirković-Veličković, Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" in Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 .,
Kon_3486 .
3
23
20
19

Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović-Vesić, Jelena; Radibratović, Milica; Radosavljević, Jelena; Burazer, Lidija M.; Milčić, Miloš K.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3224
AB  - BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
VL  - 48
IS  - 6
SP  - 731
EP  - 740
DO  - 10.1111/cea.13113
UR  - Kon_3486
ER  - 
@article{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
volume = "48",
number = "6",
pages = "731-740",
doi = "10.1111/cea.13113",
url = "Kon_3486"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T.. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy
Wiley, Hoboken., 48(6), 731-740.
https://doi.org/10.1111/cea.13113
Kon_3486
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, Ćirković-Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy. 2018;48(6):731-740.
doi:10.1111/cea.13113
Kon_3486 .
Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Mihailović-Vesić, Jelena, Radibratović, Milica, Radosavljević, Jelena, Burazer, Lidija M., Milčić, Miloš K., Smiljanić, Katarina, van Hage, Marianne, Ćirković-Veličković, Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" in Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 .,
Kon_3486 .
3
23
20
20

Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović-Vesić, Jelena; Radibratović, Milica; Radosavljević, Jelena; Burazer, Lidija M.; Milčić, Miloš K.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - DATA
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3225
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113
ER  - 
@misc{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T.. (2018). Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113. in Clinical and Experimental Allergy
Wiley, Hoboken..
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, Ćirković-Veličković T. Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113. in Clinical and Experimental Allergy. 2018;..
Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Mihailović-Vesić, Jelena, Radibratović, Milica, Radosavljević, Jelena, Burazer, Lidija M., Milčić, Miloš K., Smiljanić, Katarina, van Hage, Marianne, Ćirković-Veličković, Tanja, "Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113" in Clinical and Experimental Allergy (2018).

Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects

Radomirović, Mirjana Ž.; Minić, Simeon L.; Savković, Nina; Vasović, T.; Nikolić, Milan; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Minić, Simeon L.
AU  - Savković, Nina
AU  - Vasović, T.
AU  - Nikolić, Milan
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2175
PB  - Wiley, Hoboken
C3  - FEBS OPEN BIO
T1  - Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects
VL  - 8
SP  - 97
EP  - 97
UR  - Kon_3506
ER  - 
@conference{
author = "Radomirović, Mirjana Ž. and Minić, Simeon L. and Savković, Nina and Vasović, T. and Nikolić, Milan and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
publisher = "Wiley, Hoboken",
journal = "FEBS OPEN BIO",
title = "Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects",
volume = "8",
pages = "97-97",
url = "Kon_3506"
}
Radomirović, M. Ž., Minić, S. L., Savković, N., Vasović, T., Nikolić, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2018). Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects. in FEBS OPEN BIO
Wiley, Hoboken., 8, 97-97.
Kon_3506
Radomirović MŽ, Minić SL, Savković N, Vasović T, Nikolić M, Stanić-Vučinić D, Ćirković-Veličković T. Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects. in FEBS OPEN BIO. 2018;8:97-97.
Kon_3506 .
Radomirović, Mirjana Ž., Minić, Simeon L., Savković, Nina, Vasović, T., Nikolić, Milan, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects" in FEBS OPEN BIO, 8 (2018):97-97,
Kon_3506 .

Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions

Minić, Simeon L.; Radomirović, Mirjana Ž.; Savković, Nina; Radibratović, Milica; Mihailović-Vesić, Jelena; Vasović, Tamara; Nikolić, Milan; Milčić, Miloš K.; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2018)

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Savković, Nina
AU  - Radibratović, Milica
AU  - Mihailović-Vesić, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2197
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
UR  - Kon_3528
ER  - 
@article{
author = "Minić, Simeon L. and Radomirović, Mirjana Ž. and Savković, Nina and Radibratović, Milica and Mihailović-Vesić, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš K. 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",
url = "Kon_3528"
}
Minić, S. L., Radomirović, M. Ž., Savković, N., Radibratović, M., Mihailović-Vesić, J., Vasović, T., Nikolić, M., Milčić, M. K., 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
Kon_3528
Minić SL, Radomirović MŽ, Savković N, Radibratović M, Mihailović-Vesić J, Vasović T, Nikolić M, Milčić MK, 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
Kon_3528 .
Minić, Simeon L., Radomirović, Mirjana Ž., Savković, Nina, Radibratović, Milica, Mihailović-Vesić, Jelena, Vasović, Tamara, Nikolić, Milan, Milčić, Miloš K., 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 .,
Kon_3528 .
1
3
2
3

Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin

Minić, Simeon L.; Stanić-Vučinić, Dragana; Radomirović, Mirjana Ž.; Radibratović, Milica; Milčić, Miloš K.; Nikolić, Milan; Ćirković-Veličković, Tanja

(Elsevier, 2018)

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana Ž.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2515
AB  - Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (K-a = 2 x 10(6) M-1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin. (C) 2017 Elsevier Ltd. All rights reserved.
PB  - Elsevier
T2  - Food Chemistry
T1  - Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin
VL  - 239
SP  - 1090
EP  - 1099
DO  - 10.1016/j.foodchem.2017.07.066
UR  - Kon_3331
ER  - 
@article{
author = "Minić, Simeon L. and Stanić-Vučinić, Dragana and Radomirović, Mirjana Ž. and Radibratović, Milica and Milčić, Miloš K. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (K-a = 2 x 10(6) M-1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin. (C) 2017 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin",
volume = "239",
pages = "1090-1099",
doi = "10.1016/j.foodchem.2017.07.066",
url = "Kon_3331"
}
Minić, S. L., Stanić-Vučinić, D., Radomirović, M. Ž., Radibratović, M., Milčić, M. K., Nikolić, M.,& Ćirković-Veličković, T.. (2018). Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. in Food Chemistry
Elsevier., 239, 1090-1099.
https://doi.org/10.1016/j.foodchem.2017.07.066
Kon_3331
Minić SL, Stanić-Vučinić D, Radomirović MŽ, Radibratović M, Milčić MK, Nikolić M, Ćirković-Veličković T. Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. in Food Chemistry. 2018;239:1090-1099.
doi:10.1016/j.foodchem.2017.07.066
Kon_3331 .
Minić, Simeon L., Stanić-Vučinić, Dragana, Radomirović, Mirjana Ž., Radibratović, Milica, Milčić, Miloš K., Nikolić, Milan, Ćirković-Veličković, Tanja, "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin" in Food Chemistry, 239 (2018):1090-1099,
https://doi.org/10.1016/j.foodchem.2017.07.066 .,
Kon_3331 .
19
19
19

Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341

Peruško, Marija; van Roest, Manon; Stanić-Vučinić, Dragana; Simons, Peter J.; Pieters, Raymond; Ćirković-Veličković, Tanja; Smit, Joost

(Wiley, Hoboken, 2018)

TY  - DATA
AU  - Peruško, Marija
AU  - van Roest, Manon
AU  - Stanić-Vučinić, Dragana
AU  - Simons, Peter J.
AU  - Pieters, Raymond
AU  - Ćirković-Veličković, Tanja
AU  - Smit, Joost
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3205
PB  - Wiley, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341
ER  - 
@misc{
author = "Peruško, Marija and van Roest, Manon and Stanić-Vučinić, Dragana and Simons, Peter J. and Pieters, Raymond and Ćirković-Veličković, Tanja and Smit, Joost",
year = "2018",
publisher = "Wiley, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341"
}
Peruško, M., van Roest, M., Stanić-Vučinić, D., Simons, P. J., Pieters, R., Ćirković-Veličković, T.,& Smit, J.. (2018). Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341. in Molecular Nutrition and Food Research
Wiley, Hoboken..
Peruško M, van Roest M, Stanić-Vučinić D, Simons PJ, Pieters R, Ćirković-Veličković T, Smit J. Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341. in Molecular Nutrition and Food Research. 2018;..
Peruško, Marija, van Roest, Manon, Stanić-Vučinić, Dragana, Simons, Peter J., Pieters, Raymond, Ćirković-Veličković, Tanja, Smit, Joost, "Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341" in Molecular Nutrition and Food Research (2018).

Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation

Peruško, Marija; van Roest, Manon; Stanić-Vučinić, Dragana; Simons, Peter J.; Pieters, Raymond; Ćirković-Veličković, Tanja; Smit, Joost

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Peruško, Marija
AU  - van Roest, Manon
AU  - Stanić-Vučinić, Dragana
AU  - Simons, Peter J.
AU  - Pieters, Raymond
AU  - Ćirković-Veličković, Tanja
AU  - Smit, Joost
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2212
AB  - Scope: During food processing, the Maillard reaction (MR) may occur, resulting in the formation of glycated proteins. Glycated proteins are of particular importance in food allergies because glycation may influence interactions with the immune system. This study compared native and extensively glycated milk allergen beta-lactoglobulin (BLG), in their interactions with cells crucially involved in allergy. Methods and results: BLG was glycated in MR and characterized. Native and glycated BLG were tested in experiments of epithelial transport, uptake and degradation by DCs, T-cell cytokine responses, and basophil cell degranulation using ELISA and flow cytometry. Glycation of BLG induced partial unfolding and reduced its intestinal epithelial transfer over a Caco-2 monolayer. Uptake of glycated BLG by bone marrow-derived dendritic cells (BMDC) was increased, although both BLG forms entered BMDC via the same mechanism, receptor-mediated endocytosis. Once inside the BMDC, glycated BLG was degraded faster, which might have led to observed lower cytokine production in BMDC/CD4(+) T-cells coculture. Finally, glycated BLG was less efficient in induction of degranulation of BLG-specific IgE sensitized basophil cells. Conclusions: This study suggests that glycation of BLG by MR significantly alters its fate in processes involved in immunogenicity and allergenicity, pointing out the importance of food processing in food allergy.
PB  - Wiley, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation
VL  - 62
IS  - 17
DO  - 10.1002/mnfr.201800341
UR  - Kon_3543
ER  - 
@article{
author = "Peruško, Marija and van Roest, Manon and Stanić-Vučinić, Dragana and Simons, Peter J. and Pieters, Raymond and Ćirković-Veličković, Tanja and Smit, Joost",
year = "2018",
abstract = "Scope: During food processing, the Maillard reaction (MR) may occur, resulting in the formation of glycated proteins. Glycated proteins are of particular importance in food allergies because glycation may influence interactions with the immune system. This study compared native and extensively glycated milk allergen beta-lactoglobulin (BLG), in their interactions with cells crucially involved in allergy. Methods and results: BLG was glycated in MR and characterized. Native and glycated BLG were tested in experiments of epithelial transport, uptake and degradation by DCs, T-cell cytokine responses, and basophil cell degranulation using ELISA and flow cytometry. Glycation of BLG induced partial unfolding and reduced its intestinal epithelial transfer over a Caco-2 monolayer. Uptake of glycated BLG by bone marrow-derived dendritic cells (BMDC) was increased, although both BLG forms entered BMDC via the same mechanism, receptor-mediated endocytosis. Once inside the BMDC, glycated BLG was degraded faster, which might have led to observed lower cytokine production in BMDC/CD4(+) T-cells coculture. Finally, glycated BLG was less efficient in induction of degranulation of BLG-specific IgE sensitized basophil cells. Conclusions: This study suggests that glycation of BLG by MR significantly alters its fate in processes involved in immunogenicity and allergenicity, pointing out the importance of food processing in food allergy.",
publisher = "Wiley, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation",
volume = "62",
number = "17",
doi = "10.1002/mnfr.201800341",
url = "Kon_3543"
}
Peruško, M., van Roest, M., Stanić-Vučinić, D., Simons, P. J., Pieters, R., Ćirković-Veličković, T.,& Smit, J.. (2018). Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. in Molecular Nutrition and Food Research
Wiley, Hoboken., 62(17).
https://doi.org/10.1002/mnfr.201800341
Kon_3543
Peruško M, van Roest M, Stanić-Vučinić D, Simons PJ, Pieters R, Ćirković-Veličković T, Smit J. Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. in Molecular Nutrition and Food Research. 2018;62(17).
doi:10.1002/mnfr.201800341
Kon_3543 .
Peruško, Marija, van Roest, Manon, Stanić-Vučinić, Dragana, Simons, Peter J., Pieters, Raymond, Ćirković-Veličković, Tanja, Smit, Joost, "Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation" in Molecular Nutrition and Food Research, 62, no. 17 (2018),
https://doi.org/10.1002/mnfr.201800341 .,
Kon_3543 .
1
18
15
15

Supplementary data for the article: Cirkovic Velickovic, T. D.; Stanic-Vucinic, D. J. The Role of Dietary Phenolic Compounds in Protein Digestion and Processing Technologies to Improve Their Antinutritive Properties. Comprehensive Reviews in Food Science and Food Safety 2018, 17 (1), 82–103. https://doi.org/10.1111/1541-4337.12320

Ćirković-Veličković, Tanja; Stanić-Vučinić, Dragana

(Wiley, Hoboken, 2018)

TY  - DATA
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3309
PB  - Wiley, Hoboken
T2  - Comprehensive Reviews in Food Science and Food Safety
T1  - Supplementary data for the article: Cirkovic Velickovic, T. D.; Stanic-Vucinic, D. J. The Role of Dietary Phenolic Compounds in Protein Digestion and Processing Technologies to Improve Their Antinutritive Properties. Comprehensive Reviews in Food Science and Food Safety 2018, 17 (1), 82–103. https://doi.org/10.1111/1541-4337.12320
ER  - 
@misc{
author = "Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2018",
publisher = "Wiley, Hoboken",
journal = "Comprehensive Reviews in Food Science and Food Safety",
title = "Supplementary data for the article: Cirkovic Velickovic, T. D.; Stanic-Vucinic, D. J. The Role of Dietary Phenolic Compounds in Protein Digestion and Processing Technologies to Improve Their Antinutritive Properties. Comprehensive Reviews in Food Science and Food Safety 2018, 17 (1), 82–103. https://doi.org/10.1111/1541-4337.12320"
}
Ćirković-Veličković, T.,& Stanić-Vučinić, D.. (2018). Supplementary data for the article: Cirkovic Velickovic, T. D.; Stanic-Vucinic, D. J. The Role of Dietary Phenolic Compounds in Protein Digestion and Processing Technologies to Improve Their Antinutritive Properties. Comprehensive Reviews in Food Science and Food Safety 2018, 17 (1), 82–103. https://doi.org/10.1111/1541-4337.12320. in Comprehensive Reviews in Food Science and Food Safety
Wiley, Hoboken..
Ćirković-Veličković T, Stanić-Vučinić D. Supplementary data for the article: Cirkovic Velickovic, T. D.; Stanic-Vucinic, D. J. The Role of Dietary Phenolic Compounds in Protein Digestion and Processing Technologies to Improve Their Antinutritive Properties. Comprehensive Reviews in Food Science and Food Safety 2018, 17 (1), 82–103. https://doi.org/10.1111/1541-4337.12320. in Comprehensive Reviews in Food Science and Food Safety. 2018;..
Ćirković-Veličković, Tanja, Stanić-Vučinić, Dragana, "Supplementary data for the article: Cirkovic Velickovic, T. D.; Stanic-Vucinic, D. J. The Role of Dietary Phenolic Compounds in Protein Digestion and Processing Technologies to Improve Their Antinutritive Properties. Comprehensive Reviews in Food Science and Food Safety 2018, 17 (1), 82–103. https://doi.org/10.1111/1541-4337.12320" in Comprehensive Reviews in Food Science and Food Safety (2018).

The Role of Dietary Phenolic Compounds in Protein Digestion and Processing Technologies to Improve Their Antinutritive Properties

Ćirković-Veličković, Tanja; Stanić-Vučinić, Dragana

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2074
AB  - Digestion is the key step for delivering nutrients and bioactive substances to the body. The way different food components interact with each other and with digestive enzymes can modify the digestion process and affect human health. Understanding how food components interact during digestion is essential for the rational design of functional food products. Plant polyphenols have gained much attention for the bioactive roles they play in the human body. However, their strong beneficial effects on human health have also been associated with a negative impact on the digestion process. Due to the generally low absorption of phenolic compounds after food intake, most of the consumed polyphenols remain in the gastrointestinal tract, where they then can exert inhibitory effects on enzymes involved in the degradation of saccharides, lipids, and proteins. While the inhibitory effects of phenolics on the digestion of energy-rich food components (saccharides and lipids) may be regarded as beneficial, primarily in weight-control diets, their inhibitory effects on the digestion of proteins are not desirable for the reason of reduced utilization of amino acids. The effect of polyphenols on protein digestion is reviewed in this article, with an emphasis on food processing methods to improve the antinutritive properties of polyphenols.
PB  - Wiley, Hoboken
T2  - Comprehensive Reviews in Food Science and Food Safety
T1  - The Role of Dietary Phenolic Compounds in Protein Digestion and Processing Technologies to Improve Their Antinutritive Properties
VL  - 17
IS  - 1
SP  - 82
EP  - 103
DO  - 10.1111/1541-4337.12320
UR  - Kon_3405
ER  - 
@article{
author = "Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2018",
abstract = "Digestion is the key step for delivering nutrients and bioactive substances to the body. The way different food components interact with each other and with digestive enzymes can modify the digestion process and affect human health. Understanding how food components interact during digestion is essential for the rational design of functional food products. Plant polyphenols have gained much attention for the bioactive roles they play in the human body. However, their strong beneficial effects on human health have also been associated with a negative impact on the digestion process. Due to the generally low absorption of phenolic compounds after food intake, most of the consumed polyphenols remain in the gastrointestinal tract, where they then can exert inhibitory effects on enzymes involved in the degradation of saccharides, lipids, and proteins. While the inhibitory effects of phenolics on the digestion of energy-rich food components (saccharides and lipids) may be regarded as beneficial, primarily in weight-control diets, their inhibitory effects on the digestion of proteins are not desirable for the reason of reduced utilization of amino acids. The effect of polyphenols on protein digestion is reviewed in this article, with an emphasis on food processing methods to improve the antinutritive properties of polyphenols.",
publisher = "Wiley, Hoboken",
journal = "Comprehensive Reviews in Food Science and Food Safety",
title = "The Role of Dietary Phenolic Compounds in Protein Digestion and Processing Technologies to Improve Their Antinutritive Properties",
volume = "17",
number = "1",
pages = "82-103",
doi = "10.1111/1541-4337.12320",
url = "Kon_3405"
}
Ćirković-Veličković, T.,& Stanić-Vučinić, D.. (2018). The Role of Dietary Phenolic Compounds in Protein Digestion and Processing Technologies to Improve Their Antinutritive Properties. in Comprehensive Reviews in Food Science and Food Safety
Wiley, Hoboken., 17(1), 82-103.
https://doi.org/10.1111/1541-4337.12320
Kon_3405
Ćirković-Veličković T, Stanić-Vučinić D. The Role of Dietary Phenolic Compounds in Protein Digestion and Processing Technologies to Improve Their Antinutritive Properties. in Comprehensive Reviews in Food Science and Food Safety. 2018;17(1):82-103.
doi:10.1111/1541-4337.12320
Kon_3405 .
Ćirković-Veličković, Tanja, Stanić-Vučinić, Dragana, "The Role of Dietary Phenolic Compounds in Protein Digestion and Processing Technologies to Improve Their Antinutritive Properties" in Comprehensive Reviews in Food Science and Food Safety, 17, no. 1 (2018):82-103,
https://doi.org/10.1111/1541-4337.12320 .,
Kon_3405 .
14
86
64
75

Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin

Minić, Simeon L.; Stanić-Vučinić, Dragana; Radomirović, Mirjana Ž.; Radibratović, Milica; Milčić, Miloš K.; Nikolić, Milan; Ćirković-Veličković, Tanja

(Elsevier, 2017)

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana Ž.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3035
AB  - Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (Ka = 2 × 106 M−1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin.
PB  - Elsevier
T2  - Food Chemistry
T1  - Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin
VL  - 239
SP  - 1090
EP  - 1099
DO  - 10.1016/j.foodchem.2017.07.066
ER  - 
@article{
author = "Minić, Simeon L. and Stanić-Vučinić, Dragana and Radomirović, Mirjana Ž. and Radibratović, Milica and Milčić, Miloš K. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2017",
abstract = "Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (Ka = 2 × 106 M−1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin",
volume = "239",
pages = "1090-1099",
doi = "10.1016/j.foodchem.2017.07.066"
}
Minić, S. L., Stanić-Vučinić, D., Radomirović, M. Ž., Radibratović, M., Milčić, M. K., Nikolić, M.,& Ćirković-Veličković, T.. (2017). Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. in Food Chemistry
Elsevier., 239, 1090-1099.
https://doi.org/10.1016/j.foodchem.2017.07.066
Minić SL, Stanić-Vučinić D, Radomirović MŽ, Radibratović M, Milčić MK, Nikolić M, Ćirković-Veličković T. Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. in Food Chemistry. 2017;239:1090-1099.
doi:10.1016/j.foodchem.2017.07.066 .
Minić, Simeon L., Stanić-Vučinić, Dragana, Radomirović, Mirjana Ž., Radibratović, Milica, Milčić, Miloš K., Nikolić, Milan, Ćirković-Veličković, Tanja, "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin" in Food Chemistry, 239 (2017):1090-1099,
https://doi.org/10.1016/j.foodchem.2017.07.066 . .
19
19

Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin

Minić, Simeon L.; Radomirović, Mirjana Ž.; Radibratović, Milica; Milčić, Miloš K.; Stanić-Vučinić, Dragana; Nikolić, Milan; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2017)

TY  - CONF
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2408
AB  - Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (Ka = 2 × 106 M−1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin.
PB  - Wiley, Hoboken
C3  - FEBS Journal / Federation of European of Biochemical Societies
T1  - Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin
VL  - 284
SP  - 189
EP  - 190
DO  - 10.1016/j.foodchem.2017.07.066
UR  - Kon_3224
ER  - 
@conference{
author = "Minić, Simeon L. and Radomirović, Mirjana Ž. and Radibratović, Milica and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2017",
abstract = "Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (Ka = 2 × 106 M−1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin.",
publisher = "Wiley, Hoboken",
journal = "FEBS Journal / Federation of European of Biochemical Societies",
title = "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin",
volume = "284",
pages = "189-190",
doi = "10.1016/j.foodchem.2017.07.066",
url = "Kon_3224"
}
Minić, S. L., Radomirović, M. Ž., Radibratović, M., Milčić, M. K., Stanić-Vučinić, D., Nikolić, M.,& Ćirković-Veličković, T.. (2017). Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. in FEBS Journal / Federation of European of Biochemical Societies
Wiley, Hoboken., 284, 189-190.
https://doi.org/10.1016/j.foodchem.2017.07.066
Kon_3224
Minić SL, Radomirović MŽ, Radibratović M, Milčić MK, Stanić-Vučinić D, Nikolić M, Ćirković-Veličković T. Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. in FEBS Journal / Federation of European of Biochemical Societies. 2017;284:189-190.
doi:10.1016/j.foodchem.2017.07.066
Kon_3224 .
Minić, Simeon L., Radomirović, Mirjana Ž., Radibratović, Milica, Milčić, Miloš K., Stanić-Vučinić, Dragana, Nikolić, Milan, Ćirković-Veličković, Tanja, "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin" in FEBS Journal / Federation of European of Biochemical Societies, 284 (2017):189-190,
https://doi.org/10.1016/j.foodchem.2017.07.066 .,
Kon_3224 .
19
19