Radosavljević, Jelena

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Authority KeyName Variants
orcid::0000-0002-6123-5474
  • Radosavljević, Jelena (34)
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
Ispitivanje strukture i funkcije biološki važnih makromolekula u fiziološkim i patološkim stanjima Serbian Academy of Sciences and Arts GA No. F-26.
Chemical biology for drugging undruggable targets (ChemBioDrug) (No. CZ.02.1.01/0.0/0.0/16_019/0000729) Czech Academy of Sciences [RVO 61388963, 68378050]
Czech Infrastructure for Integrative Structural Biology (LM2015043 CIISB for CMS BIOCEV funded by MEYS CR) Czech Science Foundation [15-19018S]
European Academy for Allergy and Clinical Immunology European Academy for Allergy and Clinical Immunology, COST Action [FA1005]
Modeling and Numerical Simulations of Complex Many-Body Systems Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200168 (University of Belgrade, Faculty of Chemistry)
CAPSIDO – Developement of the assays for detection of SARS Cov-2 virus capsid proteins in biological fluids of COVID19 patients Medical Research Council Grant [MR/R009066/1]
Medical Research Council Grants MR/K000179/1 and MR/R009066/1 Medical Research Council [MR/K000179/1]
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". Belgian Special Research Fund BOF StG No. 01N01718.
COST Action [928] COST Action [928, FA1005]
EAACI FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics
Advanced technologies for monitoring and environmental protection from chemical pollutants and radiation burden Developing technological processes for nonstandard copper concentrates processing with the aim to decrease pollutants emission
MEST, MEST-CT-2005-020924

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  - http://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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4330",
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.
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. Virology journal. 2021;557:15-22
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" Virology journal, 557 (2021):15-22,
https://doi.org/10.1016/j.virol.2021.01.004 .
4
1
1

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  - http://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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4331",
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.
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. Virology journal. 2021;557:15-22
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" Virology journal, 557 (2021):15-22,
https://doi.org/10.1016/j.virol.2021.01.004 .
4
1

Comparison of air pollution in the working environment during in site treatment of infectious medical waste by convertor and autoclave sterilization

Martinović, Biljana; Jelić, Ivana V.; Rikalović, Milena G.; Šljivić-Ivanović, Marija Z.; Radosavljević, Jelena; Kostić, Aleksandar Ž.; Adžemovic, Mesud

(Parlar Scientific Publications, 2020)

TY  - JOUR
AU  - Martinović, Biljana
AU  - Jelić, Ivana V.
AU  - Rikalović, Milena G.
AU  - Šljivić-Ivanović, Marija Z.
AU  - Radosavljević, Jelena
AU  - Kostić, Aleksandar Ž.
AU  - Adžemovic, Mesud
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4208
AB  - The aim of the present study is the comparison of ambient pollution in working environment during infectious medical waste treatment in two relevant health care institutions in the Republic of Serbia - The Blood Transfusion Institute of Serbia and The Clinical Centre of Serbia by different sterilization methods (sterilizer-convertor and autoclave, respectively). Monitoring and analysis of the following chemical compounds were performed in both institutions: water vapor, carbon dioxide, carbon monoxide, hydrochloric acid, methane, ethane, propane, hexane, formaldehyde, benzene, toluene, m-xylene, phenol, acrolein, ethanol, ethyl acetate, ethylamine, ethylene oxide, methanol, dimethyl disulphide, dimethyl sulphide, ethyl mercaptan, methyl mercaptan, freon 11 (trichlorofluoromethane), carbonyl sulphide and hydrogen chloride. The determination of vapor-phase concentrations was done by extractive Fourier transform infrared spectroscopy. Monitoring of ambient pollution during infectious medical waste sterilization has shown that mercaptans, acrolein, formaldehyde, dimethyl sulphide, and ethylene oxide are emitted in both health institutions, in concentrations which are not permitted by regulations, while increased concentrations of hydrogen chloride and phenol were found in the Clinical Centre of Serbia. A comparison of ambient pollution with two different sterilization methods has shown that higher concentrations of pollutants are emitted at higher temperatures. Considering the fact that mentioned compounds exhibit high toxicity, hence represent the risk to air quality in working and living environment, i.e. represents a risk to human health it is necessary to revise and improve the existing treatment methods.
PB  - Parlar Scientific Publications
T2  - Fresenius Environmental Bulletin
T1  - Comparison of air pollution in the working environment during in site treatment of infectious medical waste by convertor and autoclave sterilization
VL  - 29
IS  - 4
SP  - 2160
EP  - 2165
ER  - 
@article{
author = "Martinović, Biljana and Jelić, Ivana V. and Rikalović, Milena G. and Šljivić-Ivanović, Marija Z. and Radosavljević, Jelena and Kostić, Aleksandar Ž. and Adžemovic, Mesud",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4208",
abstract = "The aim of the present study is the comparison of ambient pollution in working environment during infectious medical waste treatment in two relevant health care institutions in the Republic of Serbia - The Blood Transfusion Institute of Serbia and The Clinical Centre of Serbia by different sterilization methods (sterilizer-convertor and autoclave, respectively). Monitoring and analysis of the following chemical compounds were performed in both institutions: water vapor, carbon dioxide, carbon monoxide, hydrochloric acid, methane, ethane, propane, hexane, formaldehyde, benzene, toluene, m-xylene, phenol, acrolein, ethanol, ethyl acetate, ethylamine, ethylene oxide, methanol, dimethyl disulphide, dimethyl sulphide, ethyl mercaptan, methyl mercaptan, freon 11 (trichlorofluoromethane), carbonyl sulphide and hydrogen chloride. The determination of vapor-phase concentrations was done by extractive Fourier transform infrared spectroscopy. Monitoring of ambient pollution during infectious medical waste sterilization has shown that mercaptans, acrolein, formaldehyde, dimethyl sulphide, and ethylene oxide are emitted in both health institutions, in concentrations which are not permitted by regulations, while increased concentrations of hydrogen chloride and phenol were found in the Clinical Centre of Serbia. A comparison of ambient pollution with two different sterilization methods has shown that higher concentrations of pollutants are emitted at higher temperatures. Considering the fact that mentioned compounds exhibit high toxicity, hence represent the risk to air quality in working and living environment, i.e. represents a risk to human health it is necessary to revise and improve the existing treatment methods.",
publisher = "Parlar Scientific Publications",
journal = "Fresenius Environmental Bulletin",
title = "Comparison of air pollution in the working environment during in site treatment of infectious medical waste by convertor and autoclave sterilization",
volume = "29",
number = "4",
pages = "2160-2165"
}
Martinović, B., Jelić, I. V., Rikalović, M. G., Šljivić-Ivanović, M. Z., Radosavljević, J., Kostić, A. Ž.,& Adžemovic, M. (2020). Comparison of air pollution in the working environment during in site treatment of infectious medical waste by convertor and autoclave sterilization.
Fresenius Environmental Bulletin
Parlar Scientific Publications., 29(4), 2160-2165.
Martinović B, Jelić IV, Rikalović MG, Šljivić-Ivanović MZ, Radosavljević J, Kostić AŽ, Adžemovic M. Comparison of air pollution in the working environment during in site treatment of infectious medical waste by convertor and autoclave sterilization. Fresenius Environmental Bulletin. 2020;29(4):2160-2165
Martinović Biljana, Jelić Ivana V., Rikalović Milena G., Šljivić-Ivanović Marija Z., Radosavljević Jelena, Kostić Aleksandar Ž., Adžemovic Mesud, "Comparison of air pollution in the working environment during in site treatment of infectious medical waste by convertor and autoclave sterilization" Fresenius Environmental Bulletin, 29, no. 4 (2020):2160-2165
1

Thermal Processing of Peanut Grains Impairs Their Mimicked Gastrointestinal Digestion While Downstream Defatting Treatments Affect Digestomic Profiles

Prodić, Ivana; Smiljanić, Katarina; Simović, Ana; Radosavljević, Jelena; Ćirković-Veličković, Tanja

(MDPI, 2019)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Simović, Ana
AU  - Radosavljević, Jelena
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3682
AB  - Resistance to digestion by digestive proteases represents a critical property of many food allergens. Recently, a harmonized INFOGEST protocol was proposed for solid food digestion. The protocol proposes digestion conditions suitable for all kinds of solid and liquid foods. However, peanuts, as a lipid-rich food, represent a challenge for downstream analyses of the digestome. This is particularly reflected in the methodological difficulties in analyzing proteins and peptides in the presence of lipids. Therefore, the removal of the lipids seems to be a prerequisite for the downstream analysis of digestomes of lipid-rich foods. Here, we aimed to compare the digestomes of raw and thermally treated (boiled and roasted) peanuts, resulting from the INFOGEST digestion protocol for solid food, upon defatting the digests in two different manners. The most reproducible results of peanut digests were obtained in downstream analyses on TCA/acetone defatting. Unfortunately, defatting, even with an optimized TCA/acetone procedure, leads to the loss of proteins and peptides. The results of our study reveal that different thermal treatments of peanuts affect protein extraction and gastric/gastrointestinal digestion. Roasting of peanuts seems to enhance the extraction of proteins during intestinal digestion to a notable extent. The increased intestinal digestion is a consequence of the delayed extraction of thermally treated peanut proteins, which are poorly soluble in acidic gastric digestion juice but are easily extracted when the pH of the media is raised as in the subsequent intestinal phase of the digestion. Thermal processing of peanuts impaired the gastrointestinal digestion of the peanut proteins, especially in the case of roasted samples
PB  - MDPI
T2  - Foods
T1  - Thermal Processing of Peanut Grains Impairs Their Mimicked Gastrointestinal Digestion While Downstream Defatting Treatments Affect Digestomic Profiles
VL  - 8
IS  - 10
SP  - 1
EP  - 18
DO  - https://doi.org/10.3390/foods8100463
ER  - 
@article{
author = "Prodić, Ivana and Smiljanić, Katarina and Simović, Ana and Radosavljević, Jelena and Ćirković-Veličković, Tanja",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3682",
abstract = "Resistance to digestion by digestive proteases represents a critical property of many food allergens. Recently, a harmonized INFOGEST protocol was proposed for solid food digestion. The protocol proposes digestion conditions suitable for all kinds of solid and liquid foods. However, peanuts, as a lipid-rich food, represent a challenge for downstream analyses of the digestome. This is particularly reflected in the methodological difficulties in analyzing proteins and peptides in the presence of lipids. Therefore, the removal of the lipids seems to be a prerequisite for the downstream analysis of digestomes of lipid-rich foods. Here, we aimed to compare the digestomes of raw and thermally treated (boiled and roasted) peanuts, resulting from the INFOGEST digestion protocol for solid food, upon defatting the digests in two different manners. The most reproducible results of peanut digests were obtained in downstream analyses on TCA/acetone defatting. Unfortunately, defatting, even with an optimized TCA/acetone procedure, leads to the loss of proteins and peptides. The results of our study reveal that different thermal treatments of peanuts affect protein extraction and gastric/gastrointestinal digestion. Roasting of peanuts seems to enhance the extraction of proteins during intestinal digestion to a notable extent. The increased intestinal digestion is a consequence of the delayed extraction of thermally treated peanut proteins, which are poorly soluble in acidic gastric digestion juice but are easily extracted when the pH of the media is raised as in the subsequent intestinal phase of the digestion. Thermal processing of peanuts impaired the gastrointestinal digestion of the peanut proteins, especially in the case of roasted samples",
publisher = "MDPI",
journal = "Foods",
title = "Thermal Processing of Peanut Grains Impairs Their Mimicked Gastrointestinal Digestion While Downstream Defatting Treatments Affect Digestomic Profiles",
volume = "8",
number = "10",
pages = "1-18",
doi = "https://doi.org/10.3390/foods8100463"
}
Prodić, I., Smiljanić, K., Simović, A., Radosavljević, J.,& Ćirković-Veličković, T. (2019). Thermal Processing of Peanut Grains Impairs Their Mimicked Gastrointestinal Digestion While Downstream Defatting Treatments Affect Digestomic Profiles.
Foods
MDPI., 8(10), 1-18.
https://doi.org/https://doi.org/10.3390/foods8100463
Prodić I, Smiljanić K, Simović A, Radosavljević J, Ćirković-Veličković T. Thermal Processing of Peanut Grains Impairs Their Mimicked Gastrointestinal Digestion While Downstream Defatting Treatments Affect Digestomic Profiles. Foods. 2019;8(10):1-18
Prodić Ivana, Smiljanić Katarina, Simović Ana, Radosavljević Jelena, Ćirković-Veličković Tanja, "Thermal Processing of Peanut Grains Impairs Their Mimicked Gastrointestinal Digestion While Downstream Defatting Treatments Affect Digestomic Profiles" Foods, 8, no. 10 (2019):1-18,
https://doi.org/https://doi.org/10.3390/foods8100463 .
1

Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2

Pompach, Petr; Viola, Cristina M.; Radosavljević, Jelena; Lin, Jingjing; Jiráček, Jirˇí; Brzozowski, Andrzej M.; Selicharová, Irena

(Frontiers Media S.A., 2019)

TY  - JOUR
AU  - Pompach, Petr
AU  - Viola, Cristina M.
AU  - Radosavljević, Jelena
AU  - Lin, Jingjing
AU  - Jiráček, Jirˇí
AU  - Brzozowski, Andrzej M.
AU  - Selicharová, Irena
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3719
AB  - Structural details of changes accompanying interaction between insulin-related hormones and their binding partners are often enigmatic. Here, cross-linking/mass spectrometry could complement structural techniques and reveal details of these protein-protein interfaces. We used such approach to clarify missing structural description of the interface in human insulin-like growth factor (IGF-1): Drosophila melanogaster imaginal morphogenesis protein-late 2 protein (Imp-L2) complex which we studied previously by X-ray crystallography. We crosslinked these proteins by heterobifunctional cross-linker sulfosuccinimidyl 4,4′-azidopentanoate (Sulfo-SDA) for the subsequent mass spectrometry (MS) analysis. The MS analysis revealed IGF-1:Imp-L2 interactions which were not resolved in the crystal structure of this assembly, and they converged with X-ray results, indicating the importance of the IGF-1 N-terminus interaction with the C-terminal (185–242) part of the Imp-L2 for stability of this complex. Here, we also showed the advantage and reliability of MS approach in solving details of protein-protein interactions that are too flexible for solid state structural methods.
PB  - Frontiers Media S.A.
T2  - Frontiers in Endocrinology
T1  - Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2
VL  - 10
DO  - 10.3389/fendo.2019.00695
ER  - 
@article{
author = "Pompach, Petr and Viola, Cristina M. and Radosavljević, Jelena and Lin, Jingjing and Jiráček, Jirˇí and Brzozowski, Andrzej M. and Selicharová, Irena",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3719",
abstract = "Structural details of changes accompanying interaction between insulin-related hormones and their binding partners are often enigmatic. Here, cross-linking/mass spectrometry could complement structural techniques and reveal details of these protein-protein interfaces. We used such approach to clarify missing structural description of the interface in human insulin-like growth factor (IGF-1): Drosophila melanogaster imaginal morphogenesis protein-late 2 protein (Imp-L2) complex which we studied previously by X-ray crystallography. We crosslinked these proteins by heterobifunctional cross-linker sulfosuccinimidyl 4,4′-azidopentanoate (Sulfo-SDA) for the subsequent mass spectrometry (MS) analysis. The MS analysis revealed IGF-1:Imp-L2 interactions which were not resolved in the crystal structure of this assembly, and they converged with X-ray results, indicating the importance of the IGF-1 N-terminus interaction with the C-terminal (185–242) part of the Imp-L2 for stability of this complex. Here, we also showed the advantage and reliability of MS approach in solving details of protein-protein interactions that are too flexible for solid state structural methods.",
publisher = "Frontiers Media S.A.",
journal = "Frontiers in Endocrinology",
title = "Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2",
volume = "10",
doi = "10.3389/fendo.2019.00695"
}
Pompach, P., Viola, C. M., Radosavljević, J., Lin, J., Jiráček, J., Brzozowski, A. M.,& Selicharová, I. (2019). Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2.
Frontiers in Endocrinology
Frontiers Media S.A.., 10.
https://doi.org/10.3389/fendo.2019.00695
Pompach P, Viola CM, Radosavljević J, Lin J, Jiráček J, Brzozowski AM, Selicharová I. Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2. Frontiers in Endocrinology. 2019;10
Pompach Petr, Viola Cristina M., Radosavljević Jelena, Lin Jingjing, Jiráček Jirˇí, Brzozowski Andrzej M., Selicharová Irena, "Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2" Frontiers in Endocrinology, 10 (2019),
https://doi.org/10.3389/fendo.2019.00695 .
6
1
1

Supplementary data for the article: Pompach, P.; Viola, C. M.; Radosavljević, J.; Lin, J.; Jiráček, J.; Brzozowski, A. M.; Selicharová, I. Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2. Frontiers in Endocrinology 2019, 10. https://doi.org/10.3389/fendo.2019.00695

Pompach, Petr; Viola, Cristina M.; Radosavljević, Jelena; Lin, Jingjing; Jiráček, Jirˇí; Brzozowski, Andrzej M.; Selicharová, Irena

(Frontiers Media S.A., 2019)

TY  - BOOK
AU  - Pompach, Petr
AU  - Viola, Cristina M.
AU  - Radosavljević, Jelena
AU  - Lin, Jingjing
AU  - Jiráček, Jirˇí
AU  - Brzozowski, Andrzej M.
AU  - Selicharová, Irena
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3720
PB  - Frontiers Media S.A.
T2  - Frontiers in Endocrinology
T1  - Supplementary data for the article: Pompach, P.; Viola, C. M.; Radosavljević, J.; Lin, J.; Jiráček, J.; Brzozowski, A. M.; Selicharová, I. Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2. Frontiers in Endocrinology 2019, 10. https://doi.org/10.3389/fendo.2019.00695
ER  - 
@book{
author = "Pompach, Petr and Viola, Cristina M. and Radosavljević, Jelena and Lin, Jingjing and Jiráček, Jirˇí and Brzozowski, Andrzej M. and Selicharová, Irena",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3720",
publisher = "Frontiers Media S.A.",
journal = "Frontiers in Endocrinology",
title = "Supplementary data for the article: Pompach, P.; Viola, C. M.; Radosavljević, J.; Lin, J.; Jiráček, J.; Brzozowski, A. M.; Selicharová, I. Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2. Frontiers in Endocrinology 2019, 10. https://doi.org/10.3389/fendo.2019.00695"
}
Pompach, P., Viola, C. M., Radosavljević, J., Lin, J., Jiráček, J., Brzozowski, A. M.,& Selicharová, I. (2019). Supplementary data for the article: Pompach, P.; Viola, C. M.; Radosavljević, J.; Lin, J.; Jiráček, J.; Brzozowski, A. M.; Selicharová, I. Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2. Frontiers in Endocrinology 2019, 10. https://doi.org/10.3389/fendo.2019.00695.
Frontiers in Endocrinology
Frontiers Media S.A...
Pompach P, Viola CM, Radosavljević J, Lin J, Jiráček J, Brzozowski AM, Selicharová I. Supplementary data for the article: Pompach, P.; Viola, C. M.; Radosavljević, J.; Lin, J.; Jiráček, J.; Brzozowski, A. M.; Selicharová, I. Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2. Frontiers in Endocrinology 2019, 10. https://doi.org/10.3389/fendo.2019.00695. Frontiers in Endocrinology. 2019;
Pompach Petr, Viola Cristina M., Radosavljević Jelena, Lin Jingjing, Jiráček Jirˇí, Brzozowski Andrzej M., Selicharová Irena, "Supplementary data for the article: Pompach, P.; Viola, C. M.; Radosavljević, J.; Lin, J.; Jiráček, J.; Brzozowski, A. M.; Selicharová, I. Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2. Frontiers in Endocrinology 2019, 10. https://doi.org/10.3389/fendo.2019.00695" Frontiers in Endocrinology (2019)

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  - http://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
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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3224",
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"
}
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.
Clinical and Experimental Allergy
Wiley, Hoboken., 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 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. Clinical and Experimental Allergy. 2018;48(6):731-740
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" Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 .
3
21
18
19

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  - BOOK
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  - http://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  - 
@book{
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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3225",
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.
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. 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" Clinical and Experimental Allergy (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  - http://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
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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2155",
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"
}
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.
Clinical and Experimental Allergy
Wiley, Hoboken., 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 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. Clinical and Experimental Allergy. 2018;48(6):731-740
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" Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 .
3
21
18
19

Converting Insulin-like Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the Introduction of an Evolutionarily Divergent Mutation

Machackova, Katerina; Chrudinova, Martina; Radosavljević, Jelena; Potalitsyn, Paulo; Krizkova, Kvetoslava; Fabry, Milan; Selicharova, Irena; Collinsova, Michaela; Brzozowski, Andrzej M.; Zakova, Lenka; Jiracek, Jiri

(Amer Chemical Soc, Washington, 2018)

TY  - JOUR
AU  - Machackova, Katerina
AU  - Chrudinova, Martina
AU  - Radosavljević, Jelena
AU  - Potalitsyn, Paulo
AU  - Krizkova, Kvetoslava
AU  - Fabry, Milan
AU  - Selicharova, Irena
AU  - Collinsova, Michaela
AU  - Brzozowski, Andrzej M.
AU  - Zakova, Lenka
AU  - Jiracek, Jiri
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2135
AB  - Insulin-like growth factors 1 and 2 (IGF-1 and -2, respectively) are protein hormones involved not only in normal growth and development but also in life span regulation and cancer. They exert their functions mainly through the IGF-1R or by binding to isoform A of the insulin receptor (IR-A). The development of IGF-1 and IGF-2 antagonists is of great clinical interest. Mutations of A4 and A8 sites of human insulin lead to disproportionate effects on hormone IR binding and activation. Here, we systematically modified IGF-1 sites 45, 46, and 49 and IGF-2 sites 45 and 48, which correspond, or are close, to insulin sites A4 and A8. The IGF-1R and IR-A binding and autophosphorylation potencies of these analogues were characterized. They retained the main IGF-1R-related properties, but the hormones with His49 in IGF-1 and His48 in IGF-2 showed significantly higher affinities for IR-A and for IR-B, being the strongest IGF-1- and IGF-2-like binders of these receptors ever reported. All analogues activated IR-A and IGF-1R without major discrepancies in their binding affinities. This study revealed that IR-A and IGF-1R contain specific sites, likely parts of their so-called sites 2', which can interact differently with specifically modified IGF analogues. Moreover, a clear importance of IGF-2 site 44 for effective hormone folding was also observed. These findings may facilitate novel and rational engineering of new hormone analogues for IR-A and IGF-1R studies and for potential medical applications.
PB  - Amer Chemical Soc, Washington
T2  - Biochemistry
T1  - Converting Insulin-like Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the Introduction of an Evolutionarily Divergent Mutation
VL  - 57
IS  - 16
SP  - 2373
EP  - 2382
DO  - 10.1021/acs.biochem.7b01260
ER  - 
@article{
author = "Machackova, Katerina and Chrudinova, Martina and Radosavljević, Jelena and Potalitsyn, Paulo and Krizkova, Kvetoslava and Fabry, Milan and Selicharova, Irena and Collinsova, Michaela and Brzozowski, Andrzej M. and Zakova, Lenka and Jiracek, Jiri",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2135",
abstract = "Insulin-like growth factors 1 and 2 (IGF-1 and -2, respectively) are protein hormones involved not only in normal growth and development but also in life span regulation and cancer. They exert their functions mainly through the IGF-1R or by binding to isoform A of the insulin receptor (IR-A). The development of IGF-1 and IGF-2 antagonists is of great clinical interest. Mutations of A4 and A8 sites of human insulin lead to disproportionate effects on hormone IR binding and activation. Here, we systematically modified IGF-1 sites 45, 46, and 49 and IGF-2 sites 45 and 48, which correspond, or are close, to insulin sites A4 and A8. The IGF-1R and IR-A binding and autophosphorylation potencies of these analogues were characterized. They retained the main IGF-1R-related properties, but the hormones with His49 in IGF-1 and His48 in IGF-2 showed significantly higher affinities for IR-A and for IR-B, being the strongest IGF-1- and IGF-2-like binders of these receptors ever reported. All analogues activated IR-A and IGF-1R without major discrepancies in their binding affinities. This study revealed that IR-A and IGF-1R contain specific sites, likely parts of their so-called sites 2', which can interact differently with specifically modified IGF analogues. Moreover, a clear importance of IGF-2 site 44 for effective hormone folding was also observed. These findings may facilitate novel and rational engineering of new hormone analogues for IR-A and IGF-1R studies and for potential medical applications.",
publisher = "Amer Chemical Soc, Washington",
journal = "Biochemistry",
title = "Converting Insulin-like Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the Introduction of an Evolutionarily Divergent Mutation",
volume = "57",
number = "16",
pages = "2373-2382",
doi = "10.1021/acs.biochem.7b01260"
}
Machackova, K., Chrudinova, M., Radosavljević, J., Potalitsyn, P., Krizkova, K., Fabry, M., Selicharova, I., Collinsova, M., Brzozowski, A. M., Zakova, L.,& Jiracek, J. (2018). Converting Insulin-like Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the Introduction of an Evolutionarily Divergent Mutation.
Biochemistry
Amer Chemical Soc, Washington., 57(16), 2373-2382.
https://doi.org/10.1021/acs.biochem.7b01260
Machackova K, Chrudinova M, Radosavljević J, Potalitsyn P, Krizkova K, Fabry M, Selicharova I, Collinsova M, Brzozowski AM, Zakova L, Jiracek J. Converting Insulin-like Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the Introduction of an Evolutionarily Divergent Mutation. Biochemistry. 2018;57(16):2373-2382
Machackova Katerina, Chrudinova Martina, Radosavljević Jelena, Potalitsyn Paulo, Krizkova Kvetoslava, Fabry Milan, Selicharova Irena, Collinsova Michaela, Brzozowski Andrzej M., Zakova Lenka, Jiracek Jiri, "Converting Insulin-like Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the Introduction of an Evolutionarily Divergent Mutation" Biochemistry, 57, no. 16 (2018):2373-2382,
https://doi.org/10.1021/acs.biochem.7b01260 .
3
9
6
7

Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes

Radosavljević, Jelena; Apostolović, Danijela; Mihailović-Vesić, Jelena; Atanasković-Marković, Marina; Burazer, Lidija M.; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - CONF
AU  - Radosavljević, Jelena
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija M.
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2176
PB  - Wiley, Hoboken
C3  - FEBS OPEN BIO
T1  - Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes
VL  - 8
SP  - 257
EP  - 257
ER  - 
@conference{
author = "Radosavljević, Jelena and Apostolović, Danijela and Mihailović-Vesić, Jelena and Atanasković-Marković, Marina and Burazer, Lidija M. and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2176",
publisher = "Wiley, Hoboken",
journal = "FEBS OPEN BIO",
title = "Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes",
volume = "8",
pages = "257-257"
}
Radosavljević, J., Apostolović, D., Mihailović-Vesić, J., Atanasković-Marković, M., Burazer, L. M., van Hage, M.,& Ćirković-Veličković, T. (2018). Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes.
FEBS OPEN BIO
Wiley, Hoboken., 8, 257-257.
Radosavljević J, Apostolović D, Mihailović-Vesić J, Atanasković-Marković M, Burazer LM, van Hage M, Ćirković-Veličković T. Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes. FEBS OPEN BIO. 2018;8:257-257
Radosavljević Jelena, Apostolović Danijela, Mihailović-Vesić Jelena, Atanasković-Marković Marina, Burazer Lidija M., van Hage Marianne, Ćirković-Veličković Tanja, "Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes" FEBS OPEN BIO, 8 (2018):257-257

Supplementary material for the article: Macháčková, K.; Chrudinová, M.; Radosavljević, J.; Potalitsyn, P.; Křížková, K.; Fábry, M.; Selicharová, I.; Collinsová, M.; Brzozowski, A. M.; Žáková, L.; et al. Converting Insulin-like Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the Introduction of an Evolutionarily Divergent Mutation. Biochemistry 2018, 57 (16), 2373– 2382. https://doi.org/10.1021/acs.biochem.7b01260

Machackova, Katerina; Chrudinova, Martina; Radosavljević, Jelena; Potalitsyn, Paulo; Krizkova, Kvetoslava; Fabry, Milan; Selicharova, Irena; Collinsova, Michaela; Brzozowski, Andrzej M.; Zakova, Lenka; Jiracek, Jiri

(Amer Chemical Soc, Washington, 2018)

TY  - BOOK
AU  - Machackova, Katerina
AU  - Chrudinova, Martina
AU  - Radosavljević, Jelena
AU  - Potalitsyn, Paulo
AU  - Krizkova, Kvetoslava
AU  - Fabry, Milan
AU  - Selicharova, Irena
AU  - Collinsova, Michaela
AU  - Brzozowski, Andrzej M.
AU  - Zakova, Lenka
AU  - Jiracek, Jiri
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3185
PB  - Amer Chemical Soc, Washington
T2  - Biochemistry
T1  - Supplementary material for the article: Macháčková, K.; Chrudinová, M.; Radosavljević, J.; Potalitsyn, P.; Křížková, K.; Fábry, M.;  Selicharová, I.; Collinsová, M.; Brzozowski, A. M.; Žáková, L.; et al. Converting Insulin-like  Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the  Introduction of an Evolutionarily Divergent Mutation. Biochemistry 2018, 57 (16), 2373– 2382. https://doi.org/10.1021/acs.biochem.7b01260
ER  - 
@book{
author = "Machackova, Katerina and Chrudinova, Martina and Radosavljević, Jelena and Potalitsyn, Paulo and Krizkova, Kvetoslava and Fabry, Milan and Selicharova, Irena and Collinsova, Michaela and Brzozowski, Andrzej M. and Zakova, Lenka and Jiracek, Jiri",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3185",
publisher = "Amer Chemical Soc, Washington",
journal = "Biochemistry",
title = "Supplementary material for the article: Macháčková, K.; Chrudinová, M.; Radosavljević, J.; Potalitsyn, P.; Křížková, K.; Fábry, M.;  Selicharová, I.; Collinsová, M.; Brzozowski, A. M.; Žáková, L.; et al. Converting Insulin-like  Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the  Introduction of an Evolutionarily Divergent Mutation. Biochemistry 2018, 57 (16), 2373– 2382. https://doi.org/10.1021/acs.biochem.7b01260"
}
Machackova, K., Chrudinova, M., Radosavljević, J., Potalitsyn, P., Krizkova, K., Fabry, M., Selicharova, I., Collinsova, M., Brzozowski, A. M., Zakova, L.,& Jiracek, J. (2018). Supplementary material for the article: Macháčková, K.; Chrudinová, M.; Radosavljević, J.; Potalitsyn, P.; Křížková, K.; Fábry, M.;  Selicharová, I.; Collinsová, M.; Brzozowski, A. M.; Žáková, L.; et al. Converting Insulin-like  Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the  Introduction of an Evolutionarily Divergent Mutation. Biochemistry 2018, 57 (16), 2373– 2382. https://doi.org/10.1021/acs.biochem.7b01260.
Biochemistry
Amer Chemical Soc, Washington..
Machackova K, Chrudinova M, Radosavljević J, Potalitsyn P, Krizkova K, Fabry M, Selicharova I, Collinsova M, Brzozowski AM, Zakova L, Jiracek J. Supplementary material for the article: Macháčková, K.; Chrudinová, M.; Radosavljević, J.; Potalitsyn, P.; Křížková, K.; Fábry, M.;  Selicharová, I.; Collinsová, M.; Brzozowski, A. M.; Žáková, L.; et al. Converting Insulin-like  Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the  Introduction of an Evolutionarily Divergent Mutation. Biochemistry 2018, 57 (16), 2373– 2382. https://doi.org/10.1021/acs.biochem.7b01260. Biochemistry. 2018;
Machackova Katerina, Chrudinova Martina, Radosavljević Jelena, Potalitsyn Paulo, Krizkova Kvetoslava, Fabry Milan, Selicharova Irena, Collinsova Michaela, Brzozowski Andrzej M., Zakova Lenka, Jiracek Jiri, "Supplementary material for the article: Macháčková, K.; Chrudinová, M.; Radosavljević, J.; Potalitsyn, P.; Křížková, K.; Fábry, M.;  Selicharová, I.; Collinsová, M.; Brzozowski, A. M.; Žáková, L.; et al. Converting Insulin-like  Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the  Introduction of an Evolutionarily Divergent Mutation. Biochemistry 2018, 57 (16), 2373– 2382. https://doi.org/10.1021/acs.biochem.7b01260" Biochemistry (2018)

Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249

Apostolović, Danijela; Stanić-Vučinić, Dragana; de Jongh, Harmen H. J.; de Jong, Govardus A. H.; Mihailović-Vesić, Jelena; Radosavljević, Jelena; Radibratović, Milica; Nordlee, Julie A.; Baumert, Joseph L.; Milčić, Miloš K.; Taylor, Steve L.; Clua, Nuria Garrido; Ćirković-Veličković, Tanja; Koppelman, Stef J.

(Nature Publishing Group, London, 2016)

TY  - BOOK
AU  - Apostolović, Danijela
AU  - Stanić-Vučinić, Dragana
AU  - de Jongh, Harmen H. J.
AU  - de Jong, Govardus A. H.
AU  - Mihailović-Vesić, Jelena
AU  - Radosavljević, Jelena
AU  - Radibratović, Milica
AU  - Nordlee, Julie A.
AU  - Baumert, Joseph L.
AU  - Milčić, Miloš K.
AU  - Taylor, Steve L.
AU  - Clua, Nuria Garrido
AU  - Ćirković-Veličković, Tanja
AU  - Koppelman, Stef J.
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3415
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249
ER  - 
@book{
author = "Apostolović, Danijela and Stanić-Vučinić, Dragana and de Jongh, Harmen H. J. and de Jong, Govardus A. H. and Mihailović-Vesić, Jelena and Radosavljević, Jelena and Radibratović, Milica and Nordlee, Julie A. and Baumert, Joseph L. and Milčić, Miloš K. and Taylor, Steve L. and Clua, Nuria Garrido and Ćirković-Veličković, Tanja and Koppelman, Stef J.",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3415",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249"
}
Apostolović, D., Stanić-Vučinić, D., de Jongh, H. H. J., de Jong, G. A. H., Mihailović-Vesić, J., Radosavljević, J., Radibratović, M., Nordlee, J. A., Baumert, J. L., Milčić, M. K., Taylor, S. L., Clua, N. G., Ćirković-Veličković, T.,& Koppelman, S. J. (2016). Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249.
Scientific Reports
Nature Publishing Group, London..
Apostolović D, Stanić-Vučinić D, de Jongh HHJ, de Jong GAH, Mihailović-Vesić J, Radosavljević J, Radibratović M, Nordlee JA, Baumert JL, Milčić MK, Taylor SL, Clua NG, Ćirković-Veličković T, Koppelman SJ. Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249. Scientific Reports. 2016;
Apostolović Danijela, Stanić-Vučinić Dragana, de Jongh Harmen H. J., de Jong Govardus A. H., Mihailović-Vesić Jelena, Radosavljević Jelena, Radibratović Milica, Nordlee Julie A., Baumert Joseph L., Milčić Miloš K., Taylor Steve L., Clua Nuria Garrido, Ćirković-Veličković Tanja, Koppelman Stef J., "Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249" Scientific Reports (2016)

Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a

Mihajlović-Lalić, Ljiljana; Radosavljević, Jelena; Nordlund, Emilia; Krstić-Ristivojević, Maja; Bohn, Torsten; Smit, Joost; Buchert, Johanna; Ćirković-Veličković, Tanja

(Royal Soc Chemistry, Cambridge, 2016)

TY  - BOOK
AU  - Mihajlović-Lalić, Ljiljana
AU  - Radosavljević, Jelena
AU  - Nordlund, Emilia
AU  - Krstić-Ristivojević, Maja
AU  - Bohn, Torsten
AU  - Smit, Joost
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3591
PB  - Royal Soc Chemistry, Cambridge
T2  - Food and Function
T1  - Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a
ER  - 
@book{
author = "Mihajlović-Lalić, Ljiljana and Radosavljević, Jelena and Nordlund, Emilia and Krstić-Ristivojević, Maja and Bohn, Torsten and Smit, Joost and Buchert, Johanna and Ćirković-Veličković, Tanja",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3591",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Food and Function",
title = "Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a"
}
Mihajlović-Lalić, L., Radosavljević, J., Nordlund, E., Krstić-Ristivojević, M., Bohn, T., Smit, J., Buchert, J.,& Ćirković-Veličković, T. (2016). Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a.
Food and Function
Royal Soc Chemistry, Cambridge..
Mihajlović-Lalić L, Radosavljević J, Nordlund E, Krstić-Ristivojević M, Bohn T, Smit J, Buchert J, Ćirković-Veličković T. Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a. Food and Function. 2016;
Mihajlović-Lalić Ljiljana, Radosavljević Jelena, Nordlund Emilia, Krstić-Ristivojević Maja, Bohn Torsten, Smit Joost, Buchert Johanna, Ćirković-Veličković Tanja, "Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a" Food and Function (2016)

Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity

Apostolović, Danijela; Stanić-Vučinić, Dragana; de Jongh, Harmen H. J.; de Jong, Govardus A. H.; Mihailović-Vesić, Jelena; Radosavljević, Jelena; Radibratović, Milica; Nordlee, Julie A.; Baumert, Joseph L.; Milčić, Miloš K.; Taylor, Steve L.; Clua, Nuria Garrido; Ćirković-Veličković, Tanja; Koppelman, Stef J.

(Nature Publishing Group, London, 2016)

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Stanić-Vučinić, Dragana
AU  - de Jongh, Harmen H. J.
AU  - de Jong, Govardus A. H.
AU  - Mihailović-Vesić, Jelena
AU  - Radosavljević, Jelena
AU  - Radibratović, Milica
AU  - Nordlee, Julie A.
AU  - Baumert, Joseph L.
AU  - Milčić, Miloš K.
AU  - Taylor, Steve L.
AU  - Clua, Nuria Garrido
AU  - Ćirković-Veličković, Tanja
AU  - Koppelman, Stef J.
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2273
AB  - Conglutins represent the major peanut allergens and are renowned for their resistance to gastrointestinal digestion. Our aim was to characterize the digestion-resistant peptides (DRPs) of conglutins by biochemical and biophysical methods followed by a molecular dynamics simulation in order to better understand the molecular basis of food protein allergenicity. We have mapped proteolysis sites at the N- and C-termini and at a limited internal segment, while other potential proteolysis sites remained unaffected. Molecular dynamics simulation showed that proteolysis only occurred in the vibrant regions of the proteins. DRPs appeared to be conformationally stable as intact conglutins. Also, the overall secondary structure and IgE-binding potency of DRPs was comparable to that of intact conglutins. The stability of conglutins toward gastro-intestinal digestion, combined with the conformational stability of the resulting DRPs provide conditions for optimal exposure to the intestinal immune system, providing an explanation for the extraordinary allergenicity of peanut conglutins.
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity
VL  - 6
DO  - 10.1038/srep29249
ER  - 
@article{
author = "Apostolović, Danijela and Stanić-Vučinić, Dragana and de Jongh, Harmen H. J. and de Jong, Govardus A. H. and Mihailović-Vesić, Jelena and Radosavljević, Jelena and Radibratović, Milica and Nordlee, Julie A. and Baumert, Joseph L. and Milčić, Miloš K. and Taylor, Steve L. and Clua, Nuria Garrido and Ćirković-Veličković, Tanja and Koppelman, Stef J.",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2273",
abstract = "Conglutins represent the major peanut allergens and are renowned for their resistance to gastrointestinal digestion. Our aim was to characterize the digestion-resistant peptides (DRPs) of conglutins by biochemical and biophysical methods followed by a molecular dynamics simulation in order to better understand the molecular basis of food protein allergenicity. We have mapped proteolysis sites at the N- and C-termini and at a limited internal segment, while other potential proteolysis sites remained unaffected. Molecular dynamics simulation showed that proteolysis only occurred in the vibrant regions of the proteins. DRPs appeared to be conformationally stable as intact conglutins. Also, the overall secondary structure and IgE-binding potency of DRPs was comparable to that of intact conglutins. The stability of conglutins toward gastro-intestinal digestion, combined with the conformational stability of the resulting DRPs provide conditions for optimal exposure to the intestinal immune system, providing an explanation for the extraordinary allergenicity of peanut conglutins.",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity",
volume = "6",
doi = "10.1038/srep29249"
}
Apostolović, D., Stanić-Vučinić, D., de Jongh, H. H. J., de Jong, G. A. H., Mihailović-Vesić, J., Radosavljević, J., Radibratović, M., Nordlee, J. A., Baumert, J. L., Milčić, M. K., Taylor, S. L., Clua, N. G., Ćirković-Veličković, T.,& Koppelman, S. J. (2016). Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity.
Scientific Reports
Nature Publishing Group, London., 6.
https://doi.org/10.1038/srep29249
Apostolović D, Stanić-Vučinić D, de Jongh HHJ, de Jong GAH, Mihailović-Vesić J, Radosavljević J, Radibratović M, Nordlee JA, Baumert JL, Milčić MK, Taylor SL, Clua NG, Ćirković-Veličković T, Koppelman SJ. Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity. Scientific Reports. 2016;6
Apostolović Danijela, Stanić-Vučinić Dragana, de Jongh Harmen H. J., de Jong Govardus A. H., Mihailović-Vesić Jelena, Radosavljević Jelena, Radibratović Milica, Nordlee Julie A., Baumert Joseph L., Milčić Miloš K., Taylor Steve L., Clua Nuria Garrido, Ćirković-Veličković Tanja, Koppelman Stef J., "Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity" Scientific Reports, 6 (2016),
https://doi.org/10.1038/srep29249 .
9
43
39
41

Peanut allergens

Radosavljević, Jelena

(2016)

TY  - CHAP
AU  - Radosavljević, Jelena
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/308
AB  - Allergic reactions to peanuts are a major cause of food-induced anaphylaxis, both in children and adults. It is estimated that approximately 1% of the world’s population developed allergy to peanuts and the prevalence is exhibiting an increasing trend. Sensitization by peanut proteins is suspected to develop directly by ingestion of food containing peanuts or processed peanut proteins or through skin, using cosmetic products containing peanut oil and some peanut proteins. In this chapter, biochemical properties of major peanut allergens (Ara h 1, Ara h 2, Ara h 3 and Ara h 6) are thoroughly reviewed with emphasis on structural similarity to proteins from other sources which is frequently resulting in cross-reactivity. Recently reported peanut proteins are briefly described (Ara h 7-17). Methodologies for detecting minute amounts of peanuts in different sources will be improved by further advancement of knowledge on peanut allergens. Hopefully, the potential threat to peanut-allergic persons produced by contamination of food by trace amounts of peanuts and their proteins will be diminished. © 2017 by Nova Science Publishers, Inc. All rights reserved.
T1  - Peanut allergens
SP  - 31
EP  - 62
ER  - 
@article{
author = "Radosavljević, Jelena",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/308",
abstract = "Allergic reactions to peanuts are a major cause of food-induced anaphylaxis, both in children and adults. It is estimated that approximately 1% of the world’s population developed allergy to peanuts and the prevalence is exhibiting an increasing trend. Sensitization by peanut proteins is suspected to develop directly by ingestion of food containing peanuts or processed peanut proteins or through skin, using cosmetic products containing peanut oil and some peanut proteins. In this chapter, biochemical properties of major peanut allergens (Ara h 1, Ara h 2, Ara h 3 and Ara h 6) are thoroughly reviewed with emphasis on structural similarity to proteins from other sources which is frequently resulting in cross-reactivity. Recently reported peanut proteins are briefly described (Ara h 7-17). Methodologies for detecting minute amounts of peanuts in different sources will be improved by further advancement of knowledge on peanut allergens. Hopefully, the potential threat to peanut-allergic persons produced by contamination of food by trace amounts of peanuts and their proteins will be diminished. © 2017 by Nova Science Publishers, Inc. All rights reserved.",
title = "Peanut allergens",
pages = "31-62"
}
Radosavljević, J. (2016). Peanut allergens.
, 31-62.
Radosavljević J. Peanut allergens. 2016;:31-62
Radosavljević Jelena, "Peanut allergens" (2016):31-62

Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase

Mihajlović-Lalić, Ljiljana; Radosavljević, Jelena; Nordlund, Emilia; Krstić-Ristivojević, Maja; Bohn, Torsten; Smit, Joost; Buchert, Johanna; Ćirković-Veličković, Tanja

(Royal Soc Chemistry, Cambridge, 2016)

TY  - JOUR
AU  - Mihajlović-Lalić, Ljiljana
AU  - Radosavljević, Jelena
AU  - Nordlund, Emilia
AU  - Krstić-Ristivojević, Maja
AU  - Bohn, Torsten
AU  - Smit, Joost
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2254
AB  - Food texture can be improved by enzyme-mediated covalent cross-linking of different food components, such as proteins and carbohydrates. Cross-linking changes the biological and immunological properties of proteins and may change the sensitizing potential of food allergens. In this study we applied a microbial polyphenol oxidase, laccase, to cross-link peanut proteins. The size and morphology of the obtained cross-linked proteins were analyzed by electrophoresis and electron microscopy. Structural changes in proteins were analyzed by CD spectroscopy and by using specific antibodies to major peanut allergens. The bioavailability of peanut proteins was analyzed using a Caco-2 epithelial cell model. The in vivo sensitizing potential of laccase-treated peanut proteins was analyzed using a mouse model of food allergy. Finally, peanut polyphenols were analyzed by UHPLC-MS/MS, before and after the enzymatic reaction with laccase. Laccase treatment of peanut proteins yielded a covalently cross-linked material, with the modified tertiary structure of peanut proteins, improved bioavailability of Ara h 2 (by 70 fold, p  lt  0.05) and modulated allergic immune response in vivo. The modulation of the immune response was related to the increased production of IgG2a antibodies 11 fold (p  lt  0.05) and reduced IL-13 secretion in in vitro cultured splenocytes 7 fold (p  lt  0.05). Analysis of the peanut polyphenol content and profile by HPLC-MS/MS revealed that laccase treatment depleted the peanut extract of polyphenol compounds leaving mostly isorhamnetin derivatives and procyanidin dimer B-type in detectable amounts. Treatment of complex food extracts rich in polyphenols with laccase results in both protein cross-linking and modification of polyphenol compounds. These extensively cross-linked proteins have unchanged potency to induce allergic sensitization in vivo, but certain immunomodulatory changes were observed.
PB  - Royal Soc Chemistry, Cambridge
T2  - Food and Function
T1  - Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase
VL  - 7
IS  - 5
SP  - 2357
EP  - 2366
DO  - 10.1039/c5fo01325a
ER  - 
@article{
author = "Mihajlović-Lalić, Ljiljana and Radosavljević, Jelena and Nordlund, Emilia and Krstić-Ristivojević, Maja and Bohn, Torsten and Smit, Joost and Buchert, Johanna and Ćirković-Veličković, Tanja",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2254",
abstract = "Food texture can be improved by enzyme-mediated covalent cross-linking of different food components, such as proteins and carbohydrates. Cross-linking changes the biological and immunological properties of proteins and may change the sensitizing potential of food allergens. In this study we applied a microbial polyphenol oxidase, laccase, to cross-link peanut proteins. The size and morphology of the obtained cross-linked proteins were analyzed by electrophoresis and electron microscopy. Structural changes in proteins were analyzed by CD spectroscopy and by using specific antibodies to major peanut allergens. The bioavailability of peanut proteins was analyzed using a Caco-2 epithelial cell model. The in vivo sensitizing potential of laccase-treated peanut proteins was analyzed using a mouse model of food allergy. Finally, peanut polyphenols were analyzed by UHPLC-MS/MS, before and after the enzymatic reaction with laccase. Laccase treatment of peanut proteins yielded a covalently cross-linked material, with the modified tertiary structure of peanut proteins, improved bioavailability of Ara h 2 (by 70 fold, p  lt  0.05) and modulated allergic immune response in vivo. The modulation of the immune response was related to the increased production of IgG2a antibodies 11 fold (p  lt  0.05) and reduced IL-13 secretion in in vitro cultured splenocytes 7 fold (p  lt  0.05). Analysis of the peanut polyphenol content and profile by HPLC-MS/MS revealed that laccase treatment depleted the peanut extract of polyphenol compounds leaving mostly isorhamnetin derivatives and procyanidin dimer B-type in detectable amounts. Treatment of complex food extracts rich in polyphenols with laccase results in both protein cross-linking and modification of polyphenol compounds. These extensively cross-linked proteins have unchanged potency to induce allergic sensitization in vivo, but certain immunomodulatory changes were observed.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Food and Function",
title = "Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase",
volume = "7",
number = "5",
pages = "2357-2366",
doi = "10.1039/c5fo01325a"
}
Mihajlović-Lalić, L., Radosavljević, J., Nordlund, E., Krstić-Ristivojević, M., Bohn, T., Smit, J., Buchert, J.,& Ćirković-Veličković, T. (2016). Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase.
Food and Function
Royal Soc Chemistry, Cambridge., 7(5), 2357-2366.
https://doi.org/10.1039/c5fo01325a
Mihajlović-Lalić L, Radosavljević J, Nordlund E, Krstić-Ristivojević M, Bohn T, Smit J, Buchert J, Ćirković-Veličković T. Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase. Food and Function. 2016;7(5):2357-2366
Mihajlović-Lalić Ljiljana, Radosavljević Jelena, Nordlund Emilia, Krstić-Ristivojević Maja, Bohn Torsten, Smit Joost, Buchert Johanna, Ćirković-Veličković Tanja, "Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase" Food and Function, 7, no. 5 (2016):2357-2366,
https://doi.org/10.1039/c5fo01325a .
2
8
4
7

Toxicity of Bacillus thuringiensis (L.) Cry proteins against summer fruit tortrix (Adoxophyes orana - Fischer von Rosslerstamm)

Radosavljević, Jelena; Naimov, Samir

(Academic Press Inc Elsevier Science, San Diego, 2016)

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Naimov, Samir
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2282
AB  - The activity of seven Cry1, one Cry9 and one hybrid Cry1 protoxins against neonate larvae of summer fruit tortrix (Adoxophyes orana - Fischer von Rosslerstamm) has been investigated. Cry1Ia is identified as the most toxic protein, followed by Cry1Aa and Cry1Ac. Cry1Ca, Cry1Cb, Cry1Da and Cry1Fa were less active, while SN19 (Cry1 hybrid protein with domain composition 1Ba/1Ia/1Ba) and Cry9Aa exhibited negligible toxicity against A. orana. In vitro trypsin-activated Cry1Ac is still less active than Cry1Ia pro toxin, suggesting that toxicity of Cry1Ia is most probably due to more complex differences in further downstream processing, toxin-receptor interactions and pore formation in A. orana's midgut epithelium. (C) 2016 Elsevier Inc. All rights reserved.
PB  - Academic Press Inc Elsevier Science, San Diego
T2  - Journal of Invertebrate Pathology
T1  - Toxicity of Bacillus thuringiensis (L.) Cry proteins against summer fruit tortrix (Adoxophyes orana - Fischer von Rosslerstamm)
VL  - 138
SP  - 63
EP  - 65
DO  - 10.1016/j.jip.2016.06.004
ER  - 
@article{
author = "Radosavljević, Jelena and Naimov, Samir",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2282",
abstract = "The activity of seven Cry1, one Cry9 and one hybrid Cry1 protoxins against neonate larvae of summer fruit tortrix (Adoxophyes orana - Fischer von Rosslerstamm) has been investigated. Cry1Ia is identified as the most toxic protein, followed by Cry1Aa and Cry1Ac. Cry1Ca, Cry1Cb, Cry1Da and Cry1Fa were less active, while SN19 (Cry1 hybrid protein with domain composition 1Ba/1Ia/1Ba) and Cry9Aa exhibited negligible toxicity against A. orana. In vitro trypsin-activated Cry1Ac is still less active than Cry1Ia pro toxin, suggesting that toxicity of Cry1Ia is most probably due to more complex differences in further downstream processing, toxin-receptor interactions and pore formation in A. orana's midgut epithelium. (C) 2016 Elsevier Inc. All rights reserved.",
publisher = "Academic Press Inc Elsevier Science, San Diego",
journal = "Journal of Invertebrate Pathology",
title = "Toxicity of Bacillus thuringiensis (L.) Cry proteins against summer fruit tortrix (Adoxophyes orana - Fischer von Rosslerstamm)",
volume = "138",
pages = "63-65",
doi = "10.1016/j.jip.2016.06.004"
}
Radosavljević, J.,& Naimov, S. (2016). Toxicity of Bacillus thuringiensis (L.) Cry proteins against summer fruit tortrix (Adoxophyes orana - Fischer von Rosslerstamm).
Journal of Invertebrate Pathology
Academic Press Inc Elsevier Science, San Diego., 138, 63-65.
https://doi.org/10.1016/j.jip.2016.06.004
Radosavljević J, Naimov S. Toxicity of Bacillus thuringiensis (L.) Cry proteins against summer fruit tortrix (Adoxophyes orana - Fischer von Rosslerstamm). Journal of Invertebrate Pathology. 2016;138:63-65
Radosavljević Jelena, Naimov Samir, "Toxicity of Bacillus thuringiensis (L.) Cry proteins against summer fruit tortrix (Adoxophyes orana - Fischer von Rosslerstamm)" Journal of Invertebrate Pathology, 138 (2016):63-65,
https://doi.org/10.1016/j.jip.2016.06.004 .
1
1
1
1

Toxicity of Bacillus thuringiensis (L.) Cry proteins against summer fruit tortrix (Adoxophyes orana - Fischer von Rosslerstamm)

Radosavljević, Jelena; Naimov, Samir

(Academic Press Inc Elsevier Science, San Diego, 2016)

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Naimov, Samir
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3656
AB  - The activity of seven Cry1, one Cry9 and one hybrid Cry1 protoxins against neonate larvae of summer fruit tortrix (Adoxophyes orana - Fischer von Rosslerstamm) has been investigated. Cry1Ia is identified as the most toxic protein, followed by Cry1Aa and Cry1Ac. Cry1Ca, Cry1Cb, Cry1Da and Cry1Fa were less active, while SN19 (Cry1 hybrid protein with domain composition 1Ba/1Ia/1Ba) and Cry9Aa exhibited negligible toxicity against A. orana. In vitro trypsin-activated Cry1Ac is still less active than Cry1Ia pro toxin, suggesting that toxicity of Cry1Ia is most probably due to more complex differences in further downstream processing, toxin-receptor interactions and pore formation in A. orana's midgut epithelium. (C) 2016 Elsevier Inc. All rights reserved.
PB  - Academic Press Inc Elsevier Science, San Diego
T2  - Journal of Invertebrate Pathology
T1  - Toxicity of Bacillus thuringiensis (L.) Cry proteins against summer fruit tortrix (Adoxophyes orana - Fischer von Rosslerstamm)
VL  - 138
SP  - 63
EP  - 65
DO  - 10.1016/j.jip.2016.06.004
ER  - 
@article{
author = "Radosavljević, Jelena and Naimov, Samir",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3656",
abstract = "The activity of seven Cry1, one Cry9 and one hybrid Cry1 protoxins against neonate larvae of summer fruit tortrix (Adoxophyes orana - Fischer von Rosslerstamm) has been investigated. Cry1Ia is identified as the most toxic protein, followed by Cry1Aa and Cry1Ac. Cry1Ca, Cry1Cb, Cry1Da and Cry1Fa were less active, while SN19 (Cry1 hybrid protein with domain composition 1Ba/1Ia/1Ba) and Cry9Aa exhibited negligible toxicity against A. orana. In vitro trypsin-activated Cry1Ac is still less active than Cry1Ia pro toxin, suggesting that toxicity of Cry1Ia is most probably due to more complex differences in further downstream processing, toxin-receptor interactions and pore formation in A. orana's midgut epithelium. (C) 2016 Elsevier Inc. All rights reserved.",
publisher = "Academic Press Inc Elsevier Science, San Diego",
journal = "Journal of Invertebrate Pathology",
title = "Toxicity of Bacillus thuringiensis (L.) Cry proteins against summer fruit tortrix (Adoxophyes orana - Fischer von Rosslerstamm)",
volume = "138",
pages = "63-65",
doi = "10.1016/j.jip.2016.06.004"
}
Radosavljević, J.,& Naimov, S. (2016). Toxicity of Bacillus thuringiensis (L.) Cry proteins against summer fruit tortrix (Adoxophyes orana - Fischer von Rosslerstamm).
Journal of Invertebrate Pathology
Academic Press Inc Elsevier Science, San Diego., 138, 63-65.
https://doi.org/10.1016/j.jip.2016.06.004
Radosavljević J, Naimov S. Toxicity of Bacillus thuringiensis (L.) Cry proteins against summer fruit tortrix (Adoxophyes orana - Fischer von Rosslerstamm). Journal of Invertebrate Pathology. 2016;138:63-65
Radosavljević Jelena, Naimov Samir, "Toxicity of Bacillus thuringiensis (L.) Cry proteins against summer fruit tortrix (Adoxophyes orana - Fischer von Rosslerstamm)" Journal of Invertebrate Pathology, 138 (2016):63-65,
https://doi.org/10.1016/j.jip.2016.06.004 .
1
1
1
1

Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles

Mihajlovic, Luka; Radosavljević, Jelena; Burazer, Lidija M.; Smiljanić, Katarina; Ćirković-Veličković, Tanja

(Pergamon-Elsevier Science Ltd, Oxford, 2015)

TY  - JOUR
AU  - Mihajlovic, Luka
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1899
AB  - Phenolic composition of Ambrosia artemisiifolia L. pollen and sub-pollen particles (SPP) aqueous extracts was determined, using a novel extraction procedure. Total phenolic and flavonoid content was determined, as well as the antioxidative properties of the extract. Main components of water-soluble pollen phenolics are monoglycosides and malonyl-mono- and diglycosides of isorhamnetin, quercetin and kaempferol, while spermidine derivatives were identified as the dominant polyamides. SPP are similar in composition to pollen phenolics (predominant isorhamnetin and quercetin monoglycosides), but lacking small phenolic molecules ( lt 450 Da). Ethanol-based extraction protocol revealed one-third lower amount of total phenolics in SPP than in pollen. For the first time in any pollen species, SPP and pollen phenolic compositions were compared in detail, with an UHPLC/ESI-LTQ-Orbitrap-MS-MS approach, revealing the presence of spermidine derivatives in both SPP and pollen, not previously reported in Ambrosia species. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Phytochemistry
T1  - Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles
VL  - 109
SP  - 125
EP  - 132
DO  - 10.1016/j.phytochem.2014.10.022
ER  - 
@article{
author = "Mihajlovic, Luka and Radosavljević, Jelena and Burazer, Lidija M. and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2015",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1899",
abstract = "Phenolic composition of Ambrosia artemisiifolia L. pollen and sub-pollen particles (SPP) aqueous extracts was determined, using a novel extraction procedure. Total phenolic and flavonoid content was determined, as well as the antioxidative properties of the extract. Main components of water-soluble pollen phenolics are monoglycosides and malonyl-mono- and diglycosides of isorhamnetin, quercetin and kaempferol, while spermidine derivatives were identified as the dominant polyamides. SPP are similar in composition to pollen phenolics (predominant isorhamnetin and quercetin monoglycosides), but lacking small phenolic molecules ( lt 450 Da). Ethanol-based extraction protocol revealed one-third lower amount of total phenolics in SPP than in pollen. For the first time in any pollen species, SPP and pollen phenolic compositions were compared in detail, with an UHPLC/ESI-LTQ-Orbitrap-MS-MS approach, revealing the presence of spermidine derivatives in both SPP and pollen, not previously reported in Ambrosia species. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Phytochemistry",
title = "Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles",
volume = "109",
pages = "125-132",
doi = "10.1016/j.phytochem.2014.10.022"
}
Mihajlovic, L., Radosavljević, J., Burazer, L. M., Smiljanić, K.,& Ćirković-Veličković, T. (2015). Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles.
Phytochemistry
Pergamon-Elsevier Science Ltd, Oxford., 109, 125-132.
https://doi.org/10.1016/j.phytochem.2014.10.022
Mihajlovic L, Radosavljević J, Burazer LM, Smiljanić K, Ćirković-Veličković T. Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles. Phytochemistry. 2015;109:125-132
Mihajlovic Luka, Radosavljević Jelena, Burazer Lidija M., Smiljanić Katarina, Ćirković-Veličković Tanja, "Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles" Phytochemistry, 109 (2015):125-132,
https://doi.org/10.1016/j.phytochem.2014.10.022 .
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Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy

Radosavljević, Jelena; Nordlund, Emilia; Mihajlovic, Luka; Krstić-Ristivojević, Maja; Bohn, Torsten; Buchert, Johanna; Ćirković-Veličković, Tanja; Smit, Joost

(Wiley-Blackwell, Hoboken, 2014)

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Nordlund, Emilia
AU  - Mihajlovic, Luka
AU  - Krstić-Ristivojević, Maja
AU  - Bohn, Torsten
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
AU  - Smit, Joost
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1510
AB  - ScopeThe cross-linking of proteins by enzymes to form high-molecular-weight protein, aggregates can be used to tailor the technological or physiological functionality of food products. Aggregation of dietary proteins by food processing may promote allergic sensitization, but the effects of enzymatic cross-linking of dietary proteins on the allergenic potential of food are not known. In this study, the bioavailability and the sensitizing or tolerizing potential of peanut proteins (PE) cross-linked with microbial tyrosinase from Trichoderma reesei and mushroom tyrosinase from Agaricus bisporus, were investigated. Methods and resultsThe impact of cross-linking of PE on the in vitro bioavailability of fluorescein isothiocyanate-labeled peanut proteins was tested in a Caco-2 cell monolayer and by competitive ELISA. The in vivo allergenicity or capacity to induce oral tolerance in mice were measured by serum levels of PE-specific antibodies and T cell cytokine production after exposure to PE and cross-linked PE. ConclusionEnzymatic processing of peanut proteins by the two tyrosinases increased the bioavailability of major peanut allergen Ara h 2, but did not significantly change the allergenic or tolerizing properties of peanut. Enzymatic treatment of peanut proteins yielded cross-linked proteins with preserved molecular and immunological features of peanut allergens.
PB  - Wiley-Blackwell, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy
VL  - 58
IS  - 3
SP  - 635
EP  - 646
DO  - 10.1002/mnfr.201300403
ER  - 
@article{
author = "Radosavljević, Jelena and Nordlund, Emilia and Mihajlovic, Luka and Krstić-Ristivojević, Maja and Bohn, Torsten and Buchert, Johanna and Ćirković-Veličković, Tanja and Smit, Joost",
year = "2014",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1510",
abstract = "ScopeThe cross-linking of proteins by enzymes to form high-molecular-weight protein, aggregates can be used to tailor the technological or physiological functionality of food products. Aggregation of dietary proteins by food processing may promote allergic sensitization, but the effects of enzymatic cross-linking of dietary proteins on the allergenic potential of food are not known. In this study, the bioavailability and the sensitizing or tolerizing potential of peanut proteins (PE) cross-linked with microbial tyrosinase from Trichoderma reesei and mushroom tyrosinase from Agaricus bisporus, were investigated. Methods and resultsThe impact of cross-linking of PE on the in vitro bioavailability of fluorescein isothiocyanate-labeled peanut proteins was tested in a Caco-2 cell monolayer and by competitive ELISA. The in vivo allergenicity or capacity to induce oral tolerance in mice were measured by serum levels of PE-specific antibodies and T cell cytokine production after exposure to PE and cross-linked PE. ConclusionEnzymatic processing of peanut proteins by the two tyrosinases increased the bioavailability of major peanut allergen Ara h 2, but did not significantly change the allergenic or tolerizing properties of peanut. Enzymatic treatment of peanut proteins yielded cross-linked proteins with preserved molecular and immunological features of peanut allergens.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy",
volume = "58",
number = "3",
pages = "635-646",
doi = "10.1002/mnfr.201300403"
}
Radosavljević, J., Nordlund, E., Mihajlovic, L., Krstić-Ristivojević, M., Bohn, T., Buchert, J., Ćirković-Veličković, T.,& Smit, J. (2014). Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy.
Molecular Nutrition and Food Research
Wiley-Blackwell, Hoboken., 58(3), 635-646.
https://doi.org/10.1002/mnfr.201300403
Radosavljević J, Nordlund E, Mihajlovic L, Krstić-Ristivojević M, Bohn T, Buchert J, Ćirković-Veličković T, Smit J. Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy. Molecular Nutrition and Food Research. 2014;58(3):635-646
Radosavljević Jelena, Nordlund Emilia, Mihajlovic Luka, Krstić-Ristivojević Maja, Bohn Torsten, Buchert Johanna, Ćirković-Veličković Tanja, Smit Joost, "Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy" Molecular Nutrition and Food Research, 58, no. 3 (2014):635-646,
https://doi.org/10.1002/mnfr.201300403 .
8
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24

Supplementary data for the article: Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Binding Affinity between Dietary Polyphenols and β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chemistry 2013, 136 (3–4), 1263–1271. https://doi.org/10.1016/j.foodchem.2012.09.040

Stojadinović, Marija M.; Radosavljević, Jelena; Ognjenović, Jana; Mihailović-Vesić, Jelena; Prodić, Ivana; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2013)

TY  - BOOK
AU  - Stojadinović, Marija M.
AU  - Radosavljević, Jelena
AU  - Ognjenović, Jana
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2905
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Supplementary data for the article: Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Binding Affinity between Dietary Polyphenols and β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chemistry 2013, 136 (3–4), 1263–1271. https://doi.org/10.1016/j.foodchem.2012.09.040
ER  - 
@book{
author = "Stojadinović, Marija M. and Radosavljević, Jelena and Ognjenović, Jana and Mihailović-Vesić, Jelena and Prodić, Ivana and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2013",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2905",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Supplementary data for the article: Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Binding Affinity between Dietary Polyphenols and β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chemistry 2013, 136 (3–4), 1263–1271. https://doi.org/10.1016/j.foodchem.2012.09.040"
}
Stojadinović, M. M., Radosavljević, J., Ognjenović, J., Mihailović-Vesić, J., Prodić, I., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2013). Supplementary data for the article: Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Binding Affinity between Dietary Polyphenols and β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chemistry 2013, 136 (3–4), 1263–1271. https://doi.org/10.1016/j.foodchem.2012.09.040.
Food Chemistry
Elsevier Sci Ltd, Oxford..
Stojadinović MM, Radosavljević J, Ognjenović J, Mihailović-Vesić J, Prodić I, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary data for the article: Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Binding Affinity between Dietary Polyphenols and β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chemistry 2013, 136 (3–4), 1263–1271. https://doi.org/10.1016/j.foodchem.2012.09.040. Food Chemistry. 2013;
Stojadinović Marija M., Radosavljević Jelena, Ognjenović Jana, Mihailović-Vesić Jelena, Prodić Ivana, Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Supplementary data for the article: Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Binding Affinity between Dietary Polyphenols and β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chemistry 2013, 136 (3–4), 1263–1271. https://doi.org/10.1016/j.foodchem.2012.09.040" Food Chemistry (2013)

Alergenost enzimski procesovanih nutritivnih alergena

Radosavljević, Jelena

(Универзитет у Београду, Хемијски факултет, 2013)

TY  - BOOK
AU  - Radosavljević, Jelena
PY  - 2013
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=3657
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:12461/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=45318671
UR  - http://nardus.mpn.gov.rs/123456789/6383
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2701
AB  - U cilju poboljšanja funkcionalnih karakteristika hrane sve se češćeupotrebljavaju enzimi. Prilikom modifikacije proteina hrane enzimima u ciljudobijanja poboljšanih svojstava neophodno je obratiti pažnju na mogućepromene u alergenosti novonastalih modifikata.U ovoj tezi ispitan je uticaj umrežavanja alergena kikirikija i mleka na njihovualergenost. Pokazano je da se tretmanima proteina kikirikija oksidativnimenzimima ne pojačava in vitro IgE reaktivnost alergena, niti ex vivo aktivacijabazofila. Umrežavanje kazeina, kao glavnog alergena mleka, pokazalo jeneznatno izmenjeno vezivanje IgE antitela, bez narušavanja funkcionalnogodgovora u smislu aktivacije bazofila.Rezultati dobijeni u in vitro studijama, kada je reč o potencijalnoj primenienzima u komercijalne svrhe, uzimaju se sa rezervom, s obzirom na složenostmehanizama alergijske senzitizacije i opasnosti koje uvođenje izmenjenihalergena može da prouzrokuje. Ispitivanja na životinjskim modelima alergija nahranu predstavljaju pouzdaniji pokazatelj efekata koje bi modifikovani alergenimogli da prouzrokuju. U slučaju proteina kikirikija umreženih tirozinazama, umišjem modelu alergije na kikiriki, nije došlo do pojačanja alergijskesenzitizacije i proteini su sačuvali sposobnost indukcije oralne tolerancije.Umrežavanje proteina kikirikija lakazom smanjuje alergijsku senzitizaciju,izaziva jači tolerogeni odgovor i potencijalno bi mogao da se koristi i zaimunoterapiju alergija na kikiriki...
AB  - Enzymes are increasingly exploited for improving functional characteristics offood. During the enzymatic modification of food, it is necessary to pay attentionto a possible change in allergenicity of obtained novel modificates.The influence of crosslinking of peanut and milk allergens on their allergenicityhas been investigated in this thesis. It has been shown that treatment of peanutproteins by oxidative enzymes does not enhance the in vitro IgE reactivity ofthese allergens, nor ex vivo activation of basophils. Crosslinking of casein,which is a major milk allergen, slightly altered binding of IgE antibodies,without disturbing the functional response in terms of the activation ofbasophils.Results of in vitro studies regarding the potential application of enzymes forcommercial purposes are not taken for granted, due to the complexity of themechanisms of allergic sensitization and the risk that the modified allergen mayintroduce. Results obtained from studies of animal models of food allergy morereliably reflect the effects caused by modified allergens. There was no increasein allergic senzitization with peanut proteins crosslinked by action of tyrosinasesin a mouse model of peanut allergy, and, also, induction of oral tolerance waspreserved. Crosslinking of peanut proteins by laccase reduced allergicsensitization, mounted more pronounced tolerogenic response and potentiallycould be used for immunotherapy of allergy to peanuts...
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Alergenost enzimski procesovanih nutritivnih alergena
T1  - Allergenicity of enzymatically processed nutritive allergens
ER  - 
@phdthesis{
author = "Radosavljević, Jelena",
year = "2013",
url = "http://eteze.bg.ac.rs/application/showtheses?thesesId=3657, https://fedorabg.bg.ac.rs/fedora/get/o:12461/bdef:Content/download, http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=45318671, http://nardus.mpn.gov.rs/123456789/6383, http://cherry.chem.bg.ac.rs/handle/123456789/2701",
abstract = "U cilju poboljšanja funkcionalnih karakteristika hrane sve se češćeupotrebljavaju enzimi. Prilikom modifikacije proteina hrane enzimima u ciljudobijanja poboljšanih svojstava neophodno je obratiti pažnju na mogućepromene u alergenosti novonastalih modifikata.U ovoj tezi ispitan je uticaj umrežavanja alergena kikirikija i mleka na njihovualergenost. Pokazano je da se tretmanima proteina kikirikija oksidativnimenzimima ne pojačava in vitro IgE reaktivnost alergena, niti ex vivo aktivacijabazofila. Umrežavanje kazeina, kao glavnog alergena mleka, pokazalo jeneznatno izmenjeno vezivanje IgE antitela, bez narušavanja funkcionalnogodgovora u smislu aktivacije bazofila.Rezultati dobijeni u in vitro studijama, kada je reč o potencijalnoj primenienzima u komercijalne svrhe, uzimaju se sa rezervom, s obzirom na složenostmehanizama alergijske senzitizacije i opasnosti koje uvođenje izmenjenihalergena može da prouzrokuje. Ispitivanja na životinjskim modelima alergija nahranu predstavljaju pouzdaniji pokazatelj efekata koje bi modifikovani alergenimogli da prouzrokuju. U slučaju proteina kikirikija umreženih tirozinazama, umišjem modelu alergije na kikiriki, nije došlo do pojačanja alergijskesenzitizacije i proteini su sačuvali sposobnost indukcije oralne tolerancije.Umrežavanje proteina kikirikija lakazom smanjuje alergijsku senzitizaciju,izaziva jači tolerogeni odgovor i potencijalno bi mogao da se koristi i zaimunoterapiju alergija na kikiriki..., Enzymes are increasingly exploited for improving functional characteristics offood. During the enzymatic modification of food, it is necessary to pay attentionto a possible change in allergenicity of obtained novel modificates.The influence of crosslinking of peanut and milk allergens on their allergenicityhas been investigated in this thesis. It has been shown that treatment of peanutproteins by oxidative enzymes does not enhance the in vitro IgE reactivity ofthese allergens, nor ex vivo activation of basophils. Crosslinking of casein,which is a major milk allergen, slightly altered binding of IgE antibodies,without disturbing the functional response in terms of the activation ofbasophils.Results of in vitro studies regarding the potential application of enzymes forcommercial purposes are not taken for granted, due to the complexity of themechanisms of allergic sensitization and the risk that the modified allergen mayintroduce. Results obtained from studies of animal models of food allergy morereliably reflect the effects caused by modified allergens. There was no increasein allergic senzitization with peanut proteins crosslinked by action of tyrosinasesin a mouse model of peanut allergy, and, also, induction of oral tolerance waspreserved. Crosslinking of peanut proteins by laccase reduced allergicsensitization, mounted more pronounced tolerogenic response and potentiallycould be used for immunotherapy of allergy to peanuts...",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Alergenost enzimski procesovanih nutritivnih alergena, Allergenicity of enzymatically processed nutritive allergens"
}
Radosavljević, J. (2013). Allergenicity of enzymatically processed nutritive allergens.
Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
Radosavljević J. Allergenicity of enzymatically processed nutritive allergens. Универзитет у Београду. 2013;
Radosavljević Jelena, "Allergenicity of enzymatically processed nutritive allergens" Универзитет у Београду (2013)

Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed

Stojadinović, Marija M.; Radosavljević, Jelena; Ognjenović, Jana; Mihailović-Vesić, Jelena; Prodić, Ivana; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2013)

TY  - JOUR
AU  - Stojadinović, Marija M.
AU  - Radosavljević, Jelena
AU  - Ognjenović, Jana
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1577
AB  - Non-covalent interactions between beta-lactoglobulin (BLG) and polyphenol extracts of teas, coffee and cocoa were studied by fluorescence and CD spectroscopy at pH values of the gastrointestinal tract (GIT). The biological implications of non-covalent binding of polyphenols to BLG were investigated by in vitro pepsin and pancreatin digestibility assay and ABTS radical scavenging activity of complexes formed. The polyphenol-BLG systems were stable at pH values of the GIT. The most profound effect of pH on binding affinity was observed for polyphenol extracts rich in phenolic acids. Stronger non-covalent interactions delayed pepsin and pancreatin digestion of BLG and induced beta-sheet to alpha-helix transition at neutral pH. All polyphenols tested protected protein secondary structure at an extremely acidic pH of 1.2. A positive correlation was found between the strength of protein-polyphenol interactions and (a) half time of protein decay in gastric conditions (R-2 = 0.85), (b) masking of total antioxidant capacity of protein-polyphenol complexes (R-2 = 0.95).
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed
VL  - 136
IS  - 3-4
SP  - 1263
EP  - 1271
DO  - 10.1016/j.foodchem.2012.09.040
ER  - 
@article{
author = "Stojadinović, Marija M. and Radosavljević, Jelena and Ognjenović, Jana and Mihailović-Vesić, Jelena and Prodić, Ivana and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2013",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1577",
abstract = "Non-covalent interactions between beta-lactoglobulin (BLG) and polyphenol extracts of teas, coffee and cocoa were studied by fluorescence and CD spectroscopy at pH values of the gastrointestinal tract (GIT). The biological implications of non-covalent binding of polyphenols to BLG were investigated by in vitro pepsin and pancreatin digestibility assay and ABTS radical scavenging activity of complexes formed. The polyphenol-BLG systems were stable at pH values of the GIT. The most profound effect of pH on binding affinity was observed for polyphenol extracts rich in phenolic acids. Stronger non-covalent interactions delayed pepsin and pancreatin digestion of BLG and induced beta-sheet to alpha-helix transition at neutral pH. All polyphenols tested protected protein secondary structure at an extremely acidic pH of 1.2. A positive correlation was found between the strength of protein-polyphenol interactions and (a) half time of protein decay in gastric conditions (R-2 = 0.85), (b) masking of total antioxidant capacity of protein-polyphenol complexes (R-2 = 0.95).",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed",
volume = "136",
number = "3-4",
pages = "1263-1271",
doi = "10.1016/j.foodchem.2012.09.040"
}
Stojadinović, M. M., Radosavljević, J., Ognjenović, J., Mihailović-Vesić, J., Prodić, I., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2013). Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed.
Food Chemistry
Elsevier Sci Ltd, Oxford., 136(3-4), 1263-1271.
https://doi.org/10.1016/j.foodchem.2012.09.040
Stojadinović MM, Radosavljević J, Ognjenović J, Mihailović-Vesić J, Prodić I, Stanić-Vučinić D, Ćirković-Veličković T. Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed. Food Chemistry. 2013;136(3-4):1263-1271
Stojadinović Marija M., Radosavljević Jelena, Ognjenović Jana, Mihailović-Vesić Jelena, Prodić Ivana, Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed" Food Chemistry, 136, no. 3-4 (2013):1263-1271,
https://doi.org/10.1016/j.foodchem.2012.09.040 .
122
106
124

Application of ion exchanger in the separation of whey proteins and lactin from milk whey

Stanić, Dragana; Radosavljević, Jelena; Stojadinović, Marija M.; Ćirković-Veličković, Tanja

(2012)

TY  - CHAP
AU  - Stanić, Dragana
AU  - Radosavljević, Jelena
AU  - Stojadinović, Marija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/289
AB  - Whey disposal represents a huge obstacle for dairy industry, being costly and problematic. On the other hand, it could be used as a starting material for isolation of some components that are valuable on the market. Whey processing is not an easy operation; it requires robust techniques of high volumetric throughput with minimal pretreatment of the starting material. For this purpose, ion exchangers can be used, due to their versatility, safety, and relative cheapness. Being a mixture of acidic and basic proteins, double-step ion exchange chromatography, involving both cation and anion exchangers, must be performed to obtain highly purified whey proteins. Development of new technologies, based on ion exchange, which can provide fast and efficient whey processing, provides maximal exploitation in environmentally safe way. In this chapter, the literature review on the usage of ion exchangers in the separation of lactin from bovine whey proteins and fractionation of bovine whey proteins will be given. © 2012 Springer Science+Business Media B.V. All rights are reserved.
T1  - Application of ion exchanger in the separation of whey proteins and lactin from milk whey
SP  - 35
EP  - 63
DO  - 10.1007/978-94-007-4026-6_2
ER  - 
@article{
author = "Stanić, Dragana and Radosavljević, Jelena and Stojadinović, Marija M. and Ćirković-Veličković, Tanja",
year = "2012",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/289",
abstract = "Whey disposal represents a huge obstacle for dairy industry, being costly and problematic. On the other hand, it could be used as a starting material for isolation of some components that are valuable on the market. Whey processing is not an easy operation; it requires robust techniques of high volumetric throughput with minimal pretreatment of the starting material. For this purpose, ion exchangers can be used, due to their versatility, safety, and relative cheapness. Being a mixture of acidic and basic proteins, double-step ion exchange chromatography, involving both cation and anion exchangers, must be performed to obtain highly purified whey proteins. Development of new technologies, based on ion exchange, which can provide fast and efficient whey processing, provides maximal exploitation in environmentally safe way. In this chapter, the literature review on the usage of ion exchangers in the separation of lactin from bovine whey proteins and fractionation of bovine whey proteins will be given. © 2012 Springer Science+Business Media B.V. All rights are reserved.",
title = "Application of ion exchanger in the separation of whey proteins and lactin from milk whey",
pages = "35-63",
doi = "10.1007/978-94-007-4026-6_2"
}
Stanić, D., Radosavljević, J., Stojadinović, M. M.,& Ćirković-Veličković, T. (2012). Application of ion exchanger in the separation of whey proteins and lactin from milk whey.
, 35-63.
https://doi.org/10.1007/978-94-007-4026-6_2
Stanić D, Radosavljević J, Stojadinović MM, Ćirković-Veličković T. Application of ion exchanger in the separation of whey proteins and lactin from milk whey. 2012;:35-63
Stanić Dragana, Radosavljević Jelena, Stojadinović Marija M., Ćirković-Veličković Tanja, "Application of ion exchanger in the separation of whey proteins and lactin from milk whey" (2012):35-63,
https://doi.org/10.1007/978-94-007-4026-6_2 .
1
1