Molecular properties and modifications of some respiratory and nutritional allergens

Link to this page

info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172024/RS//

Molecular properties and modifications of some respiratory and nutritional allergens (en)
Молекуларне особине и модификације неких респираторних и нутритивних алергена (sr)
Molekularne osobine i modifikacije nekih respiratornih i nutritivnih alergena (sr_RS)
Authors

Publications

Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?

Costa, Joana; Bavaro, Simona Lucia; Benedé, Sara; Diaz-Perales, Araceli; Bueno-Diaz, Cristina; Gelencser, Eva; Klueber, Julia; Larré, Colette; Lozano-Ojalvo, Daniel; Lupi, Roberta; Mafra, Isabel; Mazzucchelli, Gabriel; Molina, Elena; Monaci, Linda; Martín-Pedraza, Laura; Piras, Cristian; Rodrigues, Pedro M.; Roncada, Paola; Schrama, Denise; Ćirković-Veličković, Tanja; Verhoeckx, Kitty; Villa, Caterina; Kuehn, Annette; Hoffmann-Sommergruber, Karin; Holzhauser, Thomas

(Springer, 2022)

TY  - JOUR
AU  - Costa, Joana
AU  - Bavaro, Simona Lucia
AU  - Benedé, Sara
AU  - Diaz-Perales, Araceli
AU  - Bueno-Diaz, Cristina
AU  - Gelencser, Eva
AU  - Klueber, Julia
AU  - Larré, Colette
AU  - Lozano-Ojalvo, Daniel
AU  - Lupi, Roberta
AU  - Mafra, Isabel
AU  - Mazzucchelli, Gabriel
AU  - Molina, Elena
AU  - Monaci, Linda
AU  - Martín-Pedraza, Laura
AU  - Piras, Cristian
AU  - Rodrigues, Pedro M.
AU  - Roncada, Paola
AU  - Schrama, Denise
AU  - Ćirković-Veličković, Tanja
AU  - Verhoeckx, Kitty
AU  - Villa, Caterina
AU  - Kuehn, Annette
AU  - Hoffmann-Sommergruber, Karin
AU  - Holzhauser, Thomas
PY  - 2022
UR  - https://doi.org/10.1007/s12016-020-08810-9
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4981
AB  - This review searched for published evidence that could explain how different physicochemical properties impact on the allergenicity of food proteins and if their effects would follow specific patterns among distinct protein families. Owing to the amount and complexity of the collected information, this literature overview was divided in two articles, the current one dedicated to protein families of plant allergens and a second one focused on animal allergens. Our extensive analysis of the available literature revealed that physicochemical characteristics had consistent effects on protein allergenicity for allergens belonging to the same protein family. For example, protein aggregation contributes to increased allergenicity of 2S albumins, while for legumins and cereal prolamins, the same phenomenon leads to a reduction. Molecular stability, related to structural resistance to heat and proteolysis, was identified as the most common feature promoting plant protein allergenicity, although it fails to explain the potency of some unstable allergens (e.g. pollen-related food allergens). Furthermore, data on physicochemical characteristics translating into clinical effects are limited, mainly because most studies are focused on in vitro IgE binding. Clinical data assessing how these parameters affect the development and clinical manifestation of allergies is minimal, with only few reports evaluating the sensitising capacity of modified proteins (addressing different physicochemical properties) in murine allergy models. In vivo testing of modified pure proteins by SPT or DBPCFC is scarce. At this stage, a systematic approach to link the physicochemical properties with clinical plant allergenicity in real-life scenarios is still missing.
PB  - Springer
T2  - Clinical Reviews in Allergy & Immunology
T1  - Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?
VL  - 62
IS  - 1
SP  - 37
EP  - 63
DO  - 10.1007/s12016-020-08810-9
ER  - 
@article{
author = "Costa, Joana and Bavaro, Simona Lucia and Benedé, Sara and Diaz-Perales, Araceli and Bueno-Diaz, Cristina and Gelencser, Eva and Klueber, Julia and Larré, Colette and Lozano-Ojalvo, Daniel and Lupi, Roberta and Mafra, Isabel and Mazzucchelli, Gabriel and Molina, Elena and Monaci, Linda and Martín-Pedraza, Laura and Piras, Cristian and Rodrigues, Pedro M. and Roncada, Paola and Schrama, Denise and Ćirković-Veličković, Tanja and Verhoeckx, Kitty and Villa, Caterina and Kuehn, Annette and Hoffmann-Sommergruber, Karin and Holzhauser, Thomas",
year = "2022",
abstract = "This review searched for published evidence that could explain how different physicochemical properties impact on the allergenicity of food proteins and if their effects would follow specific patterns among distinct protein families. Owing to the amount and complexity of the collected information, this literature overview was divided in two articles, the current one dedicated to protein families of plant allergens and a second one focused on animal allergens. Our extensive analysis of the available literature revealed that physicochemical characteristics had consistent effects on protein allergenicity for allergens belonging to the same protein family. For example, protein aggregation contributes to increased allergenicity of 2S albumins, while for legumins and cereal prolamins, the same phenomenon leads to a reduction. Molecular stability, related to structural resistance to heat and proteolysis, was identified as the most common feature promoting plant protein allergenicity, although it fails to explain the potency of some unstable allergens (e.g. pollen-related food allergens). Furthermore, data on physicochemical characteristics translating into clinical effects are limited, mainly because most studies are focused on in vitro IgE binding. Clinical data assessing how these parameters affect the development and clinical manifestation of allergies is minimal, with only few reports evaluating the sensitising capacity of modified proteins (addressing different physicochemical properties) in murine allergy models. In vivo testing of modified pure proteins by SPT or DBPCFC is scarce. At this stage, a systematic approach to link the physicochemical properties with clinical plant allergenicity in real-life scenarios is still missing.",
publisher = "Springer",
journal = "Clinical Reviews in Allergy & Immunology",
title = "Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?",
volume = "62",
number = "1",
pages = "37-63",
doi = "10.1007/s12016-020-08810-9"
}
Costa, J., Bavaro, S. L., Benedé, S., Diaz-Perales, A., Bueno-Diaz, C., Gelencser, E., Klueber, J., Larré, C., Lozano-Ojalvo, D., Lupi, R., Mafra, I., Mazzucchelli, G., Molina, E., Monaci, L., Martín-Pedraza, L., Piras, C., Rodrigues, P. M., Roncada, P., Schrama, D., Ćirković-Veličković, T., Verhoeckx, K., Villa, C., Kuehn, A., Hoffmann-Sommergruber, K.,& Holzhauser, T.. (2022). Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?. in Clinical Reviews in Allergy & Immunology
Springer., 62(1), 37-63.
https://doi.org/10.1007/s12016-020-08810-9
Costa J, Bavaro SL, Benedé S, Diaz-Perales A, Bueno-Diaz C, Gelencser E, Klueber J, Larré C, Lozano-Ojalvo D, Lupi R, Mafra I, Mazzucchelli G, Molina E, Monaci L, Martín-Pedraza L, Piras C, Rodrigues PM, Roncada P, Schrama D, Ćirković-Veličković T, Verhoeckx K, Villa C, Kuehn A, Hoffmann-Sommergruber K, Holzhauser T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?. in Clinical Reviews in Allergy & Immunology. 2022;62(1):37-63.
doi:10.1007/s12016-020-08810-9 .
Costa, Joana, Bavaro, Simona Lucia, Benedé, Sara, Diaz-Perales, Araceli, Bueno-Diaz, Cristina, Gelencser, Eva, Klueber, Julia, Larré, Colette, Lozano-Ojalvo, Daniel, Lupi, Roberta, Mafra, Isabel, Mazzucchelli, Gabriel, Molina, Elena, Monaci, Linda, Martín-Pedraza, Laura, Piras, Cristian, Rodrigues, Pedro M., Roncada, Paola, Schrama, Denise, Ćirković-Veličković, Tanja, Verhoeckx, Kitty, Villa, Caterina, Kuehn, Annette, Hoffmann-Sommergruber, Karin, Holzhauser, Thomas, "Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?" in Clinical Reviews in Allergy & Immunology, 62, no. 1 (2022):37-63,
https://doi.org/10.1007/s12016-020-08810-9 . .
9
56
30
48

Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk

Stanić-Vučinić, Dragana; Stojadinović, Marija M.; Radomirović, Mirjana Ž.; Simović, Ana; Radibratović, Milica; Ćirković-Veličković, Tanja

(Bentham Science, 2022)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Radomirović, Mirjana Ž.
AU  - Simović, Ana
AU  - Radibratović, Milica
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4884
AB  - Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.
PB  - Bentham Science
T2  - Current Analytical Chemistry
T1  - Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk
VL  - 18
IS  - 3
SP  - 341
EP  - 359
DO  - 10.2174/1573411017666210108092338
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4884
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Radomirović, Mirjana Ž. and Simović, Ana and Radibratović, Milica and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.",
publisher = "Bentham Science",
journal = "Current Analytical Chemistry",
title = "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk",
volume = "18",
number = "3",
pages = "341-359",
doi = "10.2174/1573411017666210108092338",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4884"
}
Stanić-Vučinić, D., Stojadinović, M. M., Radomirović, M. Ž., Simović, A., Radibratović, M.,& Ćirković-Veličković, T.. (2022). Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry
Bentham Science., 18(3), 341-359.
https://doi.org/10.2174/1573411017666210108092338
https://hdl.handle.net/21.15107/rcub_cherry_4884
Stanić-Vučinić D, Stojadinović MM, Radomirović MŽ, Simović A, Radibratović M, Ćirković-Veličković T. Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry. 2022;18(3):341-359.
doi:10.2174/1573411017666210108092338
https://hdl.handle.net/21.15107/rcub_cherry_4884 .
Stanić-Vučinić, Dragana, Stojadinović, Marija M., Radomirović, Mirjana Ž., Simović, Ana, Radibratović, Milica, Ćirković-Veličković, Tanja, "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk" in Current Analytical Chemistry, 18, no. 3 (2022):341-359,
https://doi.org/10.2174/1573411017666210108092338 .,
https://hdl.handle.net/21.15107/rcub_cherry_4884 .
2
1
1

Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk

Radosavljević, Jelena; Stanić-Vučinić, Dragana; Stojadinović, Marija M.; Radomirović, Mirjana Ž.; Simović, Ana; Radibratović, Milica; Ćirković-Veličković, Tanja

(Bentham Science, 2022)

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Radomirović, Mirjana Ž.
AU  - Simović, Ana
AU  - Radibratović, Milica
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4883
AB  - Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.
PB  - Bentham Science
T2  - Current Analytical Chemistry
T1  - Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk
VL  - 18
IS  - 3
SP  - 341
EP  - 359
DO  - 10.2174/1573411017666210108092338
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4883
ER  - 
@article{
author = "Radosavljević, Jelena and Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Radomirović, Mirjana Ž. and Simović, Ana and Radibratović, Milica and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.",
publisher = "Bentham Science",
journal = "Current Analytical Chemistry",
title = "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk",
volume = "18",
number = "3",
pages = "341-359",
doi = "10.2174/1573411017666210108092338",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4883"
}
Radosavljević, J., Stanić-Vučinić, D., Stojadinović, M. M., Radomirović, M. Ž., Simović, A., Radibratović, M.,& Ćirković-Veličković, T.. (2022). Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry
Bentham Science., 18(3), 341-359.
https://doi.org/10.2174/1573411017666210108092338
https://hdl.handle.net/21.15107/rcub_cherry_4883
Radosavljević J, Stanić-Vučinić D, Stojadinović MM, Radomirović MŽ, Simović A, Radibratović M, Ćirković-Veličković T. Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry. 2022;18(3):341-359.
doi:10.2174/1573411017666210108092338
https://hdl.handle.net/21.15107/rcub_cherry_4883 .
Radosavljević, Jelena, Stanić-Vučinić, Dragana, Stojadinović, Marija M., Radomirović, Mirjana Ž., Simović, Ana, Radibratović, Milica, Ćirković-Veličković, Tanja, "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk" in Current Analytical Chemistry, 18, no. 3 (2022):341-359,
https://doi.org/10.2174/1573411017666210108092338 .,
https://hdl.handle.net/21.15107/rcub_cherry_4883 .
2
1
1

Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.

Costa, Joana; Bavaro, Simona Lucia; Benedé, Sara; Diaz-Perales, Araceli; Bueno-Diaz, Cristina; Gelencser, Eva; Klueber, Julia; Larré, Colette; Lozano-Ojalvo, Daniel; Lupi, Roberta; Mafra, Isabel; Mazzucchelli, Gabriel; Molina, Elena; Monaci, Linda; Martín-Pedraza, Laura; Piras, Cristian; Rodrigues, Pedro M.; Roncada, Paola; Schrama, Denise; Ćirković-Veličković, Tanja; Verhoeckx, Kitty; Villa, Caterina; Kuehn, Annette; Hoffmann-Sommergruber, Karin; Holzhauser, Thomas

(Springer, 2022)

TY  - DATA
AU  - Costa, Joana
AU  - Bavaro, Simona Lucia
AU  - Benedé, Sara
AU  - Diaz-Perales, Araceli
AU  - Bueno-Diaz, Cristina
AU  - Gelencser, Eva
AU  - Klueber, Julia
AU  - Larré, Colette
AU  - Lozano-Ojalvo, Daniel
AU  - Lupi, Roberta
AU  - Mafra, Isabel
AU  - Mazzucchelli, Gabriel
AU  - Molina, Elena
AU  - Monaci, Linda
AU  - Martín-Pedraza, Laura
AU  - Piras, Cristian
AU  - Rodrigues, Pedro M.
AU  - Roncada, Paola
AU  - Schrama, Denise
AU  - Ćirković-Veličković, Tanja
AU  - Verhoeckx, Kitty
AU  - Villa, Caterina
AU  - Kuehn, Annette
AU  - Hoffmann-Sommergruber, Karin
AU  - Holzhauser, Thomas
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4982
PB  - Springer
T2  - Clinical Reviews in Allergy & Immunology
T1  - Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4982
ER  - 
@misc{
author = "Costa, Joana and Bavaro, Simona Lucia and Benedé, Sara and Diaz-Perales, Araceli and Bueno-Diaz, Cristina and Gelencser, Eva and Klueber, Julia and Larré, Colette and Lozano-Ojalvo, Daniel and Lupi, Roberta and Mafra, Isabel and Mazzucchelli, Gabriel and Molina, Elena and Monaci, Linda and Martín-Pedraza, Laura and Piras, Cristian and Rodrigues, Pedro M. and Roncada, Paola and Schrama, Denise and Ćirković-Veličković, Tanja and Verhoeckx, Kitty and Villa, Caterina and Kuehn, Annette and Hoffmann-Sommergruber, Karin and Holzhauser, Thomas",
year = "2022",
publisher = "Springer",
journal = "Clinical Reviews in Allergy & Immunology",
title = "Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4982"
}
Costa, J., Bavaro, S. L., Benedé, S., Diaz-Perales, A., Bueno-Diaz, C., Gelencser, E., Klueber, J., Larré, C., Lozano-Ojalvo, D., Lupi, R., Mafra, I., Mazzucchelli, G., Molina, E., Monaci, L., Martín-Pedraza, L., Piras, C., Rodrigues, P. M., Roncada, P., Schrama, D., Ćirković-Veličković, T., Verhoeckx, K., Villa, C., Kuehn, A., Hoffmann-Sommergruber, K.,& Holzhauser, T.. (2022). Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.. in Clinical Reviews in Allergy & Immunology
Springer..
https://hdl.handle.net/21.15107/rcub_cherry_4982
Costa J, Bavaro SL, Benedé S, Diaz-Perales A, Bueno-Diaz C, Gelencser E, Klueber J, Larré C, Lozano-Ojalvo D, Lupi R, Mafra I, Mazzucchelli G, Molina E, Monaci L, Martín-Pedraza L, Piras C, Rodrigues PM, Roncada P, Schrama D, Ćirković-Veličković T, Verhoeckx K, Villa C, Kuehn A, Hoffmann-Sommergruber K, Holzhauser T. Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.. in Clinical Reviews in Allergy & Immunology. 2022;.
https://hdl.handle.net/21.15107/rcub_cherry_4982 .
Costa, Joana, Bavaro, Simona Lucia, Benedé, Sara, Diaz-Perales, Araceli, Bueno-Diaz, Cristina, Gelencser, Eva, Klueber, Julia, Larré, Colette, Lozano-Ojalvo, Daniel, Lupi, Roberta, Mafra, Isabel, Mazzucchelli, Gabriel, Molina, Elena, Monaci, Linda, Martín-Pedraza, Laura, Piras, Cristian, Rodrigues, Pedro M., Roncada, Paola, Schrama, Denise, Ćirković-Veličković, Tanja, Verhoeckx, Kitty, Villa, Caterina, Kuehn, Annette, Hoffmann-Sommergruber, Karin, Holzhauser, Thomas, "Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9." in Clinical Reviews in Allergy & Immunology (2022),
https://hdl.handle.net/21.15107/rcub_cherry_4982 .

Drying methodology effect on the phenolic content, antioxidant activity of Myrtus communis L. leaves ethanol extracts and soybean oil oxidative stability

Snoussi, Ahmed; Essaidi, Ismahen; Ben Haj Koubaier, Hayet; Zrelli, Houda; Alsafari, Ibrahim; Tešić, Živoslav Lj.; Mihailovic, Jelena; Khan, Muhummadh; El Omri, Abdelfatteh; Ćirković-Veličković, Tanja; Bouzouita, Nabiha

(Springer Nature, 2021)

TY  - JOUR
AU  - Snoussi, Ahmed
AU  - Essaidi, Ismahen
AU  - Ben Haj Koubaier, Hayet
AU  - Zrelli, Houda
AU  - Alsafari, Ibrahim
AU  - Tešić, Živoslav Lj.
AU  - Mihailovic, Jelena
AU  - Khan, Muhummadh
AU  - El Omri, Abdelfatteh
AU  - Ćirković-Veličković, Tanja
AU  - Bouzouita, Nabiha
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4441
AB  - In this study, different drying methodologies (convective air, oven and microwave) of Myrtus communis L. (M. communis L.) leaves were conducted to investigate their effects on the levels of phenolic compounds, antioxidant capacity of ethanolic extracts (EEs) as well as the soybean oil oxidative stability. Drying methodology significantly influenced the extractability of phenolic compounds. Microwave drying led to an increase in the amounts of total phenols, flavonoids and proanthocyanidins followed by oven drying at 70 °C. Higher temperature of drying (100 and 120 °C) led to a significant reduction of their amounts (p < 0.05). An ultra-performance liquid chromatography method combined with high resolution mass spectroscopic detection was used to analyze the phenolic fraction of extracts. Higher amounts of the identified compounds were observed when leaves were heat treated. Furthermore, the evaluation of the antioxidant activity showed that the studied extracts possess in general high antioxidant capacities, significantly dependent on the employed drying methodology. The incorporation of the different extracts at 200 ppm in soybean oil showed that its oxidative stability was significantly improved. Extracts from leaves treated with microwave (EE_MW) and at 70 °C (EE_70) have better effect than BHT. The results of the present study suggest that microwave drying could be useful to enhance the extractability of phenolic compounds and the antioxidant capacity of M. communis L. leaf extract.
PB  - Springer Nature
T2  - BMC Chemistry
T2  - BMC ChemistryBMC Chemistry
T1  - Drying methodology effect on the phenolic content, antioxidant activity of Myrtus communis L. leaves ethanol extracts and soybean oil oxidative stability
VL  - 15
IS  - 1
SP  - 31
DO  - 10.1186/s13065-021-00753-2
ER  - 
@article{
author = "Snoussi, Ahmed and Essaidi, Ismahen and Ben Haj Koubaier, Hayet and Zrelli, Houda and Alsafari, Ibrahim and Tešić, Živoslav Lj. and Mihailovic, Jelena and Khan, Muhummadh and El Omri, Abdelfatteh and Ćirković-Veličković, Tanja and Bouzouita, Nabiha",
year = "2021",
abstract = "In this study, different drying methodologies (convective air, oven and microwave) of Myrtus communis L. (M. communis L.) leaves were conducted to investigate their effects on the levels of phenolic compounds, antioxidant capacity of ethanolic extracts (EEs) as well as the soybean oil oxidative stability. Drying methodology significantly influenced the extractability of phenolic compounds. Microwave drying led to an increase in the amounts of total phenols, flavonoids and proanthocyanidins followed by oven drying at 70 °C. Higher temperature of drying (100 and 120 °C) led to a significant reduction of their amounts (p < 0.05). An ultra-performance liquid chromatography method combined with high resolution mass spectroscopic detection was used to analyze the phenolic fraction of extracts. Higher amounts of the identified compounds were observed when leaves were heat treated. Furthermore, the evaluation of the antioxidant activity showed that the studied extracts possess in general high antioxidant capacities, significantly dependent on the employed drying methodology. The incorporation of the different extracts at 200 ppm in soybean oil showed that its oxidative stability was significantly improved. Extracts from leaves treated with microwave (EE_MW) and at 70 °C (EE_70) have better effect than BHT. The results of the present study suggest that microwave drying could be useful to enhance the extractability of phenolic compounds and the antioxidant capacity of M. communis L. leaf extract.",
publisher = "Springer Nature",
journal = "BMC Chemistry, BMC ChemistryBMC Chemistry",
title = "Drying methodology effect on the phenolic content, antioxidant activity of Myrtus communis L. leaves ethanol extracts and soybean oil oxidative stability",
volume = "15",
number = "1",
pages = "31",
doi = "10.1186/s13065-021-00753-2"
}
Snoussi, A., Essaidi, I., Ben Haj Koubaier, H., Zrelli, H., Alsafari, I., Tešić, Ž. Lj., Mihailovic, J., Khan, M., El Omri, A., Ćirković-Veličković, T.,& Bouzouita, N.. (2021). Drying methodology effect on the phenolic content, antioxidant activity of Myrtus communis L. leaves ethanol extracts and soybean oil oxidative stability. in BMC Chemistry
Springer Nature., 15(1), 31.
https://doi.org/10.1186/s13065-021-00753-2
Snoussi A, Essaidi I, Ben Haj Koubaier H, Zrelli H, Alsafari I, Tešić ŽL, Mihailovic J, Khan M, El Omri A, Ćirković-Veličković T, Bouzouita N. Drying methodology effect on the phenolic content, antioxidant activity of Myrtus communis L. leaves ethanol extracts and soybean oil oxidative stability. in BMC Chemistry. 2021;15(1):31.
doi:10.1186/s13065-021-00753-2 .
Snoussi, Ahmed, Essaidi, Ismahen, Ben Haj Koubaier, Hayet, Zrelli, Houda, Alsafari, Ibrahim, Tešić, Živoslav Lj., Mihailovic, Jelena, Khan, Muhummadh, El Omri, Abdelfatteh, Ćirković-Veličković, Tanja, Bouzouita, Nabiha, "Drying methodology effect on the phenolic content, antioxidant activity of Myrtus communis L. leaves ethanol extracts and soybean oil oxidative stability" in BMC Chemistry, 15, no. 1 (2021):31,
https://doi.org/10.1186/s13065-021-00753-2 . .
3
1
3

Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis

Moons, Jens; de Azambuja, Francisco; Mihailović, Jelena; Kozma, Karoly; Smiljanić, Katarina; Amiri, Mehran; Ćirković-Veličković, Tanja; Nyman, May; Parac-Vogt, Tatjana

(Wiley, 2020)

TY  - JOUR
AU  - Moons, Jens
AU  - de Azambuja, Francisco
AU  - Mihailović, Jelena
AU  - Kozma, Karoly
AU  - Smiljanić, Katarina
AU  - Amiri, Mehran
AU  - Ćirković-Veličković, Tanja
AU  - Nyman, May
AU  - Parac-Vogt, Tatjana
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3917
AB  - The selective hydrolysis of proteins by non‐enzymatic catalysis is difficult to achieve, yet it is crucial for applications in biotechnology and proteomics. Herein, we report that discrete hafnium metal‐oxo cluster [Hf18O10(OH)26(SO4)13⋅(H2O)33] (Hf18), which is centred by the same hexamer motif found in many MOFs, acts as a heterogeneous catalyst for the efficient hydrolysis of horse heart myoglobin (HHM) in low buffer concentrations. Among 154 amino acids present in the sequence of HHM, strictly selective cleavage at only 6 solvent accessible aspartate residues was observed. Mechanistic experiments suggest that the hydrolytic activity is likely derived from the actuation of HfIV Lewis acidic sites and the Brønsted acidic surface of Hf18. X‐ray scattering and ESI‐MS revealed that Hf18 is completely insoluble in these conditions, confirming the HHM hydrolysis is caused by a heterogeneous reaction of the solid Hf18 cluster, and not from smaller, soluble Hf species that could leach into solution.
PB  - Wiley
T2  - Angewandte Chemie (International Edition)
T1  - Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis
VL  - 59
IS  - 17
SP  - 1
EP  - 9
DO  - 10.1002/anie.202001036
ER  - 
@article{
author = "Moons, Jens and de Azambuja, Francisco and Mihailović, Jelena and Kozma, Karoly and Smiljanić, Katarina and Amiri, Mehran and Ćirković-Veličković, Tanja and Nyman, May and Parac-Vogt, Tatjana",
year = "2020",
abstract = "The selective hydrolysis of proteins by non‐enzymatic catalysis is difficult to achieve, yet it is crucial for applications in biotechnology and proteomics. Herein, we report that discrete hafnium metal‐oxo cluster [Hf18O10(OH)26(SO4)13⋅(H2O)33] (Hf18), which is centred by the same hexamer motif found in many MOFs, acts as a heterogeneous catalyst for the efficient hydrolysis of horse heart myoglobin (HHM) in low buffer concentrations. Among 154 amino acids present in the sequence of HHM, strictly selective cleavage at only 6 solvent accessible aspartate residues was observed. Mechanistic experiments suggest that the hydrolytic activity is likely derived from the actuation of HfIV Lewis acidic sites and the Brønsted acidic surface of Hf18. X‐ray scattering and ESI‐MS revealed that Hf18 is completely insoluble in these conditions, confirming the HHM hydrolysis is caused by a heterogeneous reaction of the solid Hf18 cluster, and not from smaller, soluble Hf species that could leach into solution.",
publisher = "Wiley",
journal = "Angewandte Chemie (International Edition)",
title = "Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis",
volume = "59",
number = "17",
pages = "1-9",
doi = "10.1002/anie.202001036"
}
Moons, J., de Azambuja, F., Mihailović, J., Kozma, K., Smiljanić, K., Amiri, M., Ćirković-Veličković, T., Nyman, M.,& Parac-Vogt, T.. (2020). Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis. in Angewandte Chemie (International Edition)
Wiley., 59(17), 1-9.
https://doi.org/10.1002/anie.202001036
Moons J, de Azambuja F, Mihailović J, Kozma K, Smiljanić K, Amiri M, Ćirković-Veličković T, Nyman M, Parac-Vogt T. Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis. in Angewandte Chemie (International Edition). 2020;59(17):1-9.
doi:10.1002/anie.202001036 .
Moons, Jens, de Azambuja, Francisco, Mihailović, Jelena, Kozma, Karoly, Smiljanić, Katarina, Amiri, Mehran, Ćirković-Veličković, Tanja, Nyman, May, Parac-Vogt, Tatjana, "Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis" in Angewandte Chemie (International Edition), 59, no. 17 (2020):1-9,
https://doi.org/10.1002/anie.202001036 . .
22
23
15
19

Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis

Moons, Jens; de Azambuja, Francisco; Mihailović, Jelena; Kozma, Karoly; Smiljanić, Katarina; Amiri, Mehran; Ćirković-Veličković, Tanja; Nyman, May; Parac-Vogt, Tatjana

(Wiley, 2020)

TY  - JOUR
AU  - Moons, Jens
AU  - de Azambuja, Francisco
AU  - Mihailović, Jelena
AU  - Kozma, Karoly
AU  - Smiljanić, Katarina
AU  - Amiri, Mehran
AU  - Ćirković-Veličković, Tanja
AU  - Nyman, May
AU  - Parac-Vogt, Tatjana
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4850
AB  - The selective hydrolysis of proteins by non‐enzymatic catalysis is difficult to achieve, yet it is crucial for applications in biotechnology and proteomics. Herein, we report that discrete hafnium metal‐oxo cluster [Hf18O10(OH)26(SO4)13⋅(H2O)33] (Hf18), which is centred by the same hexamer motif found in many MOFs, acts as a heterogeneous catalyst for the efficient hydrolysis of horse heart myoglobin (HHM) in low buffer concentrations. Among 154 amino acids present in the sequence of HHM, strictly selective cleavage at only 6 solvent accessible aspartate residues was observed. Mechanistic experiments suggest that the hydrolytic activity is likely derived from the actuation of HfIV Lewis acidic sites and the Brønsted acidic surface of Hf18. X‐ray scattering and ESI‐MS revealed that Hf18 is completely insoluble in these conditions, confirming the HHM hydrolysis is caused by a heterogeneous reaction of the solid Hf18 cluster, and not from smaller, soluble Hf species that could leach into solution.
PB  - Wiley
T2  - Angewandte Chemie (International Edition)
T1  - Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis
VL  - 59
IS  - 17
SP  - 1
EP  - 9
DO  - 10.1002/anie.202001036
ER  - 
@article{
author = "Moons, Jens and de Azambuja, Francisco and Mihailović, Jelena and Kozma, Karoly and Smiljanić, Katarina and Amiri, Mehran and Ćirković-Veličković, Tanja and Nyman, May and Parac-Vogt, Tatjana",
year = "2020",
abstract = "The selective hydrolysis of proteins by non‐enzymatic catalysis is difficult to achieve, yet it is crucial for applications in biotechnology and proteomics. Herein, we report that discrete hafnium metal‐oxo cluster [Hf18O10(OH)26(SO4)13⋅(H2O)33] (Hf18), which is centred by the same hexamer motif found in many MOFs, acts as a heterogeneous catalyst for the efficient hydrolysis of horse heart myoglobin (HHM) in low buffer concentrations. Among 154 amino acids present in the sequence of HHM, strictly selective cleavage at only 6 solvent accessible aspartate residues was observed. Mechanistic experiments suggest that the hydrolytic activity is likely derived from the actuation of HfIV Lewis acidic sites and the Brønsted acidic surface of Hf18. X‐ray scattering and ESI‐MS revealed that Hf18 is completely insoluble in these conditions, confirming the HHM hydrolysis is caused by a heterogeneous reaction of the solid Hf18 cluster, and not from smaller, soluble Hf species that could leach into solution.",
publisher = "Wiley",
journal = "Angewandte Chemie (International Edition)",
title = "Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis",
volume = "59",
number = "17",
pages = "1-9",
doi = "10.1002/anie.202001036"
}
Moons, J., de Azambuja, F., Mihailović, J., Kozma, K., Smiljanić, K., Amiri, M., Ćirković-Veličković, T., Nyman, M.,& Parac-Vogt, T.. (2020). Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis. in Angewandte Chemie (International Edition)
Wiley., 59(17), 1-9.
https://doi.org/10.1002/anie.202001036
Moons J, de Azambuja F, Mihailović J, Kozma K, Smiljanić K, Amiri M, Ćirković-Veličković T, Nyman M, Parac-Vogt T. Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis. in Angewandte Chemie (International Edition). 2020;59(17):1-9.
doi:10.1002/anie.202001036 .
Moons, Jens, de Azambuja, Francisco, Mihailović, Jelena, Kozma, Karoly, Smiljanić, Katarina, Amiri, Mehran, Ćirković-Veličković, Tanja, Nyman, May, Parac-Vogt, Tatjana, "Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis" in Angewandte Chemie (International Edition), 59, no. 17 (2020):1-9,
https://doi.org/10.1002/anie.202001036 . .
22
23
15
20

Supplementary data for the article: Moons, J.; de Azambuja, F.; Mihailović, J.; Kozma, K.; Smiljanić, K.; Amiri, M.; Ćirković-Veličković, T.; Nyman, M.; Parac-Vogt, T. Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis. Angewandte Chemie (International Edition) 2020, 59 (17), 1–9. https://doi.org/10.1002/anie.202001036.

Moons, Jens; de Azambuja, Francisco; Mihailović, Jelena; Kozma, Karoly; Smiljanić, Katarina; Amiri, Mehran; Ćirković-Veličković, Tanja; Nyman, May; Parac-Vogt, Tatjana

(Wiley, 2020)

TY  - DATA
AU  - Moons, Jens
AU  - de Azambuja, Francisco
AU  - Mihailović, Jelena
AU  - Kozma, Karoly
AU  - Smiljanić, Katarina
AU  - Amiri, Mehran
AU  - Ćirković-Veličković, Tanja
AU  - Nyman, May
AU  - Parac-Vogt, Tatjana
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4851
PB  - Wiley
T2  - Angewandte Chemie (International Edition)
T1  - Supplementary data for the article: Moons, J.; de Azambuja, F.; Mihailović, J.; Kozma, K.; Smiljanić, K.; Amiri, M.; Ćirković-Veličković, T.; Nyman, M.; Parac-Vogt, T. Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis. Angewandte Chemie (International Edition) 2020, 59 (17), 1–9. https://doi.org/10.1002/anie.202001036.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4851
ER  - 
@misc{
author = "Moons, Jens and de Azambuja, Francisco and Mihailović, Jelena and Kozma, Karoly and Smiljanić, Katarina and Amiri, Mehran and Ćirković-Veličković, Tanja and Nyman, May and Parac-Vogt, Tatjana",
year = "2020",
publisher = "Wiley",
journal = "Angewandte Chemie (International Edition)",
title = "Supplementary data for the article: Moons, J.; de Azambuja, F.; Mihailović, J.; Kozma, K.; Smiljanić, K.; Amiri, M.; Ćirković-Veličković, T.; Nyman, M.; Parac-Vogt, T. Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis. Angewandte Chemie (International Edition) 2020, 59 (17), 1–9. https://doi.org/10.1002/anie.202001036.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4851"
}
Moons, J., de Azambuja, F., Mihailović, J., Kozma, K., Smiljanić, K., Amiri, M., Ćirković-Veličković, T., Nyman, M.,& Parac-Vogt, T.. (2020). Supplementary data for the article: Moons, J.; de Azambuja, F.; Mihailović, J.; Kozma, K.; Smiljanić, K.; Amiri, M.; Ćirković-Veličković, T.; Nyman, M.; Parac-Vogt, T. Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis. Angewandte Chemie (International Edition) 2020, 59 (17), 1–9. https://doi.org/10.1002/anie.202001036.. in Angewandte Chemie (International Edition)
Wiley..
https://hdl.handle.net/21.15107/rcub_cherry_4851
Moons J, de Azambuja F, Mihailović J, Kozma K, Smiljanić K, Amiri M, Ćirković-Veličković T, Nyman M, Parac-Vogt T. Supplementary data for the article: Moons, J.; de Azambuja, F.; Mihailović, J.; Kozma, K.; Smiljanić, K.; Amiri, M.; Ćirković-Veličković, T.; Nyman, M.; Parac-Vogt, T. Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis. Angewandte Chemie (International Edition) 2020, 59 (17), 1–9. https://doi.org/10.1002/anie.202001036.. in Angewandte Chemie (International Edition). 2020;.
https://hdl.handle.net/21.15107/rcub_cherry_4851 .
Moons, Jens, de Azambuja, Francisco, Mihailović, Jelena, Kozma, Karoly, Smiljanić, Katarina, Amiri, Mehran, Ćirković-Veličković, Tanja, Nyman, May, Parac-Vogt, Tatjana, "Supplementary data for the article: Moons, J.; de Azambuja, F.; Mihailović, J.; Kozma, K.; Smiljanić, K.; Amiri, M.; Ćirković-Veličković, T.; Nyman, M.; Parac-Vogt, T. Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis. Angewandte Chemie (International Edition) 2020, 59 (17), 1–9. https://doi.org/10.1002/anie.202001036." in Angewandte Chemie (International Edition) (2020),
https://hdl.handle.net/21.15107/rcub_cherry_4851 .

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

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

(Springer, 2020)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Vlajić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić-Šipka, Sanja
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3859
AB  - The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.
PB  - Springer
T2  - Journal of Biological Inorganic Chemistry
T1  - The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c
VL  - 25
IS  - 2
SP  - 253
EP  - 265
DO  - 10.1007/s00775-020-01758-3
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Nikolić, Stefan and Vlajić, Katarina and Radomirović, Mirjana Ž. and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić-Šipka, Sanja",
year = "2020",
abstract = "The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.",
publisher = "Springer",
journal = "Journal of Biological Inorganic Chemistry",
title = "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c",
volume = "25",
number = "2",
pages = "253-265",
doi = "10.1007/s00775-020-01758-3"
}
Stanić-Vučinić, D., Nikolić, S., Vlajić, K., Radomirović, M. Ž., Mihailović, J., Ćirković-Veličković, T.,& Grgurić-Šipka, S.. (2020). The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. in Journal of Biological Inorganic Chemistry
Springer., 25(2), 253-265.
https://doi.org/10.1007/s00775-020-01758-3
Stanić-Vučinić D, Nikolić S, Vlajić K, Radomirović MŽ, Mihailović J, Ćirković-Veličković T, Grgurić-Šipka S. The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. in Journal of Biological Inorganic Chemistry. 2020;25(2):253-265.
doi:10.1007/s00775-020-01758-3 .
Stanić-Vučinić, Dragana, Nikolić, Stefan, Vlajić, Katarina, Radomirović, Mirjana Ž., Mihailović, Jelena, Ćirković-Veličković, Tanja, Grgurić-Šipka, Sanja, "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c" in Journal of Biological Inorganic Chemistry, 25, no. 2 (2020):253-265,
https://doi.org/10.1007/s00775-020-01758-3 . .
6
3
6

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

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

(Springer, 2020)

TY  - DATA
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Vlajić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić-Šipka, Sanja
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3863
PB  - Springer
T2  - Journal of Biological Inorganic Chemistry
T1  - Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3863
ER  - 
@misc{
author = "Stanić-Vučinić, Dragana and Nikolić, Stefan and Vlajić, Katarina and Radomirović, Mirjana Ž. and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić-Šipka, Sanja",
year = "2020",
publisher = "Springer",
journal = "Journal of Biological Inorganic Chemistry",
title = "Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3863"
}
Stanić-Vučinić, D., Nikolić, S., Vlajić, K., Radomirović, M. Ž., Mihailović, J., Ćirković-Veličković, T.,& Grgurić-Šipka, S.. (2020). Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3. in Journal of Biological Inorganic Chemistry
Springer..
https://hdl.handle.net/21.15107/rcub_cherry_3863
Stanić-Vučinić D, Nikolić S, Vlajić K, Radomirović MŽ, Mihailović J, Ćirković-Veličković T, Grgurić-Šipka S. Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3. in Journal of Biological Inorganic Chemistry. 2020;.
https://hdl.handle.net/21.15107/rcub_cherry_3863 .
Stanić-Vučinić, Dragana, Nikolić, Stefan, Vlajić, Katarina, Radomirović, Mirjana Ž., Mihailović, Jelena, Ćirković-Veličković, Tanja, Grgurić-Šipka, Sanja, "Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3" in Journal of Biological Inorganic Chemistry (2020),
https://hdl.handle.net/21.15107/rcub_cherry_3863 .

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

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

(Springer, 2020)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Vlajić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić-Šipka, Sanja
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3942
AB  - The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.
PB  - Springer
T2  - Journal of Biological Inorganic Chemistry
T1  - The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c
VL  - 25
IS  - 2
SP  - 253
EP  - 265
DO  - 10.1007/s00775-020-01758-3
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Nikolić, Stefan and Vlajić, Katarina and Radomirović, Mirjana Ž. and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić-Šipka, Sanja",
year = "2020",
abstract = "The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.",
publisher = "Springer",
journal = "Journal of Biological Inorganic Chemistry",
title = "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c",
volume = "25",
number = "2",
pages = "253-265",
doi = "10.1007/s00775-020-01758-3"
}
Stanić-Vučinić, D., Nikolić, S., Vlajić, K., Radomirović, M. Ž., Mihailović, J., Ćirković-Veličković, T.,& Grgurić-Šipka, S.. (2020). The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. in Journal of Biological Inorganic Chemistry
Springer., 25(2), 253-265.
https://doi.org/10.1007/s00775-020-01758-3
Stanić-Vučinić D, Nikolić S, Vlajić K, Radomirović MŽ, Mihailović J, Ćirković-Veličković T, Grgurić-Šipka S. The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. in Journal of Biological Inorganic Chemistry. 2020;25(2):253-265.
doi:10.1007/s00775-020-01758-3 .
Stanić-Vučinić, Dragana, Nikolić, Stefan, Vlajić, Katarina, Radomirović, Mirjana Ž., Mihailović, Jelena, Ćirković-Veličković, Tanja, Grgurić-Šipka, Sanja, "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c" in Journal of Biological Inorganic Chemistry, 25, no. 2 (2020):253-265,
https://doi.org/10.1007/s00775-020-01758-3 . .
6
3
6

Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978

Apostolović, Danijela; Mihailović, Jelena; Commins, Scott P.; Wijnveld, Michiel; Kazimirova, Maria; Starkhammar, Maria; Stockinger, Hannes; Platts-Mills, Thomas A. E.; Ćirković-Veličković, Tanja; Hamsten, Carl; van Hage, Marianne

(Wiley, 2020)

TY  - DATA
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Commins, Scott P.
AU  - Wijnveld, Michiel
AU  - Kazimirova, Maria
AU  - Starkhammar, Maria
AU  - Stockinger, Hannes
AU  - Platts-Mills, Thomas A. E.
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3864
PB  - Wiley
T2  - Allergy: European Journal of Allergy and Clinical Immunology
T1  - Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3864
ER  - 
@misc{
author = "Apostolović, Danijela and Mihailović, Jelena and Commins, Scott P. and Wijnveld, Michiel and Kazimirova, Maria and Starkhammar, Maria and Stockinger, Hannes and Platts-Mills, Thomas A. E. and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2020",
publisher = "Wiley",
journal = "Allergy: European Journal of Allergy and Clinical Immunology",
title = "Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3864"
}
Apostolović, D., Mihailović, J., Commins, S. P., Wijnveld, M., Kazimirova, M., Starkhammar, M., Stockinger, H., Platts-Mills, T. A. E., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M.. (2020). Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978. in Allergy: European Journal of Allergy and Clinical Immunology
Wiley..
https://hdl.handle.net/21.15107/rcub_cherry_3864
Apostolović D, Mihailović J, Commins SP, Wijnveld M, Kazimirova M, Starkhammar M, Stockinger H, Platts-Mills TAE, Ćirković-Veličković T, Hamsten C, van Hage M. Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978. in Allergy: European Journal of Allergy and Clinical Immunology. 2020;.
https://hdl.handle.net/21.15107/rcub_cherry_3864 .
Apostolović, Danijela, Mihailović, Jelena, Commins, Scott P., Wijnveld, Michiel, Kazimirova, Maria, Starkhammar, Maria, Stockinger, Hannes, Platts-Mills, Thomas A. E., Ćirković-Veličković, Tanja, Hamsten, Carl, van Hage, Marianne, "Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978" in Allergy: European Journal of Allergy and Clinical Immunology (2020),
https://hdl.handle.net/21.15107/rcub_cherry_3864 .

Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy

Apostolović, Danijela; Mihailović, Jelena; Commins, Scott P.; Wijnveld, Michiel; Kazimirova, Maria; Starkhammar, Maria; Stockinger, Hannes; Platts-Mills, Thomas A. E.; Ćirković-Veličković, Tanja; Hamsten, Carl; van Hage, Marianne

(Wiley, 2020)

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Commins, Scott P.
AU  - Wijnveld, Michiel
AU  - Kazimirova, Maria
AU  - Starkhammar, Maria
AU  - Stockinger, Hannes
AU  - Platts-Mills, Thomas A. E.
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3860
PB  - Wiley
T2  - Allergy: European Journal of Allergy and Clinical Immunology
T1  - Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy
VL  - 75
IS  - 1
SP  - 217
EP  - 220
DO  - 10.1111/ALL.13978
ER  - 
@article{
author = "Apostolović, Danijela and Mihailović, Jelena and Commins, Scott P. and Wijnveld, Michiel and Kazimirova, Maria and Starkhammar, Maria and Stockinger, Hannes and Platts-Mills, Thomas A. E. and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2020",
publisher = "Wiley",
journal = "Allergy: European Journal of Allergy and Clinical Immunology",
title = "Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy",
volume = "75",
number = "1",
pages = "217-220",
doi = "10.1111/ALL.13978"
}
Apostolović, D., Mihailović, J., Commins, S. P., Wijnveld, M., Kazimirova, M., Starkhammar, M., Stockinger, H., Platts-Mills, T. A. E., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M.. (2020). Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy. in Allergy: European Journal of Allergy and Clinical Immunology
Wiley., 75(1), 217-220.
https://doi.org/10.1111/ALL.13978
Apostolović D, Mihailović J, Commins SP, Wijnveld M, Kazimirova M, Starkhammar M, Stockinger H, Platts-Mills TAE, Ćirković-Veličković T, Hamsten C, van Hage M. Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy. in Allergy: European Journal of Allergy and Clinical Immunology. 2020;75(1):217-220.
doi:10.1111/ALL.13978 .
Apostolović, Danijela, Mihailović, Jelena, Commins, Scott P., Wijnveld, Michiel, Kazimirova, Maria, Starkhammar, Maria, Stockinger, Hannes, Platts-Mills, Thomas A. E., Ćirković-Veličković, Tanja, Hamsten, Carl, van Hage, Marianne, "Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy" in Allergy: European Journal of Allergy and Clinical Immunology, 75, no. 1 (2020):217-220,
https://doi.org/10.1111/ALL.13978 . .
11
30
25
26

Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy

Apostolović, Danijela; Mihailović, Jelena; Commins, Scott P.; Wijnveld, Michiel; Kazimirova, Maria; Starkhammar, Maria; Stockinger, Hannes; Platts-Mills, Thomas A. E.; Ćirković-Veličković, Tanja; Hamsten, Carl; van Hage, Marianne

(Wiley, 2020)

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Commins, Scott P.
AU  - Wijnveld, Michiel
AU  - Kazimirova, Maria
AU  - Starkhammar, Maria
AU  - Stockinger, Hannes
AU  - Platts-Mills, Thomas A. E.
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3853
PB  - Wiley
T2  - Allergy: European Journal of Allergy and Clinical Immunology
T1  - Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy
VL  - 75
IS  - 1
SP  - 217
EP  - 220
DO  - 10.1111/all.13978
ER  - 
@article{
author = "Apostolović, Danijela and Mihailović, Jelena and Commins, Scott P. and Wijnveld, Michiel and Kazimirova, Maria and Starkhammar, Maria and Stockinger, Hannes and Platts-Mills, Thomas A. E. and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2020",
publisher = "Wiley",
journal = "Allergy: European Journal of Allergy and Clinical Immunology",
title = "Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy",
volume = "75",
number = "1",
pages = "217-220",
doi = "10.1111/all.13978"
}
Apostolović, D., Mihailović, J., Commins, S. P., Wijnveld, M., Kazimirova, M., Starkhammar, M., Stockinger, H., Platts-Mills, T. A. E., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M.. (2020). Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy. in Allergy: European Journal of Allergy and Clinical Immunology
Wiley., 75(1), 217-220.
https://doi.org/10.1111/all.13978
Apostolović D, Mihailović J, Commins SP, Wijnveld M, Kazimirova M, Starkhammar M, Stockinger H, Platts-Mills TAE, Ćirković-Veličković T, Hamsten C, van Hage M. Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy. in Allergy: European Journal of Allergy and Clinical Immunology. 2020;75(1):217-220.
doi:10.1111/all.13978 .
Apostolović, Danijela, Mihailović, Jelena, Commins, Scott P., Wijnveld, Michiel, Kazimirova, Maria, Starkhammar, Maria, Stockinger, Hannes, Platts-Mills, Thomas A. E., Ćirković-Veličković, Tanja, Hamsten, Carl, van Hage, Marianne, "Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy" in Allergy: European Journal of Allergy and Clinical Immunology, 75, no. 1 (2020):217-220,
https://doi.org/10.1111/all.13978 . .
11
30
25
26

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

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

(Elsevier, 2019)

TY  - JOUR
AU  - Radibratović, Milica
AU  - Al-Hanish, Ayah
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4848
AB  - α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.
PB  - Elsevier
T2  - Food Chemistry
T1  - Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study
VL  - 278
SP  - 388
EP  - 395
DO  - 10.1016/j.foodchem.2018.11.038
ER  - 
@article{
author = "Radibratović, Milica and Al-Hanish, Ayah and Minić, Simeon L. and Radomirović, Mirjana Ž. and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study",
volume = "278",
pages = "388-395",
doi = "10.1016/j.foodchem.2018.11.038"
}
Radibratović, M., Al-Hanish, A., Minić, S. L., Radomirović, M. Ž., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2019). Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. in Food Chemistry
Elsevier., 278, 388-395.
https://doi.org/10.1016/j.foodchem.2018.11.038
Radibratović M, Al-Hanish A, Minić SL, Radomirović MŽ, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. in Food Chemistry. 2019;278:388-395.
doi:10.1016/j.foodchem.2018.11.038 .
Radibratović, Milica, Al-Hanish, Ayah, Minić, Simeon L., Radomirović, Mirjana Ž., Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study" in Food Chemistry, 278 (2019):388-395,
https://doi.org/10.1016/j.foodchem.2018.11.038 . .
8
5
8

Fatty acids composition of the most common bivalves in Korean diet

Krstić-Ristivojević, Maja; Jovanović, Vesna B.; Ristivojević, Petar; Ćirković-Veličković, Tanja

(Portugal : Sociedade Portuguesa de Química, 2019)

TY  - CONF
AU  - Krstić-Ristivojević, Maja
AU  - Jovanović, Vesna B.
AU  - Ristivojević, Petar
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3777
AB  - Consumption of bivalve molluscs, such as oysters, mussels, clams and scallops, makes a significant part of the daily Korean diet. Bivalves provide high quality proteins with all the dietary-essential amino acids, lipids, vitamins, minerals and other bioactive nutrients, which offer a variety of health benefits to the consumer [1]. This food contains less than 5 percent of total fat, so it is considered a low-fat food. Beside the amount of total fat, the proportions of saturated, monounsaturated and polyunsaturated fatty acids (FA) (S, M and P, respectively), as well as ratio of n-3 (ω-3) and n-6 (ω-6) P in food are very important for the health diet [2].
Fourteen species of bivalves Anadara broughtonii (AB), Ruditapes philippinarum (Manila clam (RP)), Tegillarca granosa (TG), Pecten yessoensis (Yesso scallop (YS), Argopecten spp. (small scallop (SS), Chlamys farreri farreri (CF), Cyclina sinensis (CS), Leukoma jedoensis (LJ), Mytilus califorianus (MCa) Mytilus galloprovancialis (MG), Maretrix lusoria (ML), Mactra quadrangularis (MQ), Sinovacula constricta (SC) and Crassostrea gigas (Pacific oyster (PC)) were bought in two fish markets in Incheon, Korea, in order to determine FA composition using GC/EI-MS of fatty acid methyl esters (FAME). The FAME were identified by comparing their retention times with those of the FAME standards or by comparing their mass spectra with those stored in the NIST Mass Spectral Library.
In the bivalve samples, 43 different FA were identified, of which 10 were S, 12 M and 13 P, other FA were 7 methyl-FA and 1 hydroxyl-FA. The P/S ratio and ω-6/ω-3 P ratio are the most significant markers of lipid composition in a healthy diet and both should be close to 1 [3]. Among analysed species, only YS and SS have P/S ratio close to 1 (1,20 and 1.16, respectively), while other species have value between 0.07 and 0.73. The obtained values for ω-6/ω-3 P ratio were from 0.008 to 0.55, which indicates that bivalve molluscs are the valuable source of ω-3 P (EPA and DHA). These ω-3 P play important roles in growth, development, and maintenance of health.
PB  - Portugal : Sociedade Portuguesa de Química
C3  - Book of Abstracts of the XX EuroFoodChem Congress
T1  - Fatty acids composition of the most common bivalves in Korean diet
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3777
ER  - 
@conference{
author = "Krstić-Ristivojević, Maja and Jovanović, Vesna B. and Ristivojević, Petar and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Consumption of bivalve molluscs, such as oysters, mussels, clams and scallops, makes a significant part of the daily Korean diet. Bivalves provide high quality proteins with all the dietary-essential amino acids, lipids, vitamins, minerals and other bioactive nutrients, which offer a variety of health benefits to the consumer [1]. This food contains less than 5 percent of total fat, so it is considered a low-fat food. Beside the amount of total fat, the proportions of saturated, monounsaturated and polyunsaturated fatty acids (FA) (S, M and P, respectively), as well as ratio of n-3 (ω-3) and n-6 (ω-6) P in food are very important for the health diet [2].
Fourteen species of bivalves Anadara broughtonii (AB), Ruditapes philippinarum (Manila clam (RP)), Tegillarca granosa (TG), Pecten yessoensis (Yesso scallop (YS), Argopecten spp. (small scallop (SS), Chlamys farreri farreri (CF), Cyclina sinensis (CS), Leukoma jedoensis (LJ), Mytilus califorianus (MCa) Mytilus galloprovancialis (MG), Maretrix lusoria (ML), Mactra quadrangularis (MQ), Sinovacula constricta (SC) and Crassostrea gigas (Pacific oyster (PC)) were bought in two fish markets in Incheon, Korea, in order to determine FA composition using GC/EI-MS of fatty acid methyl esters (FAME). The FAME were identified by comparing their retention times with those of the FAME standards or by comparing their mass spectra with those stored in the NIST Mass Spectral Library.
In the bivalve samples, 43 different FA were identified, of which 10 were S, 12 M and 13 P, other FA were 7 methyl-FA and 1 hydroxyl-FA. The P/S ratio and ω-6/ω-3 P ratio are the most significant markers of lipid composition in a healthy diet and both should be close to 1 [3]. Among analysed species, only YS and SS have P/S ratio close to 1 (1,20 and 1.16, respectively), while other species have value between 0.07 and 0.73. The obtained values for ω-6/ω-3 P ratio were from 0.008 to 0.55, which indicates that bivalve molluscs are the valuable source of ω-3 P (EPA and DHA). These ω-3 P play important roles in growth, development, and maintenance of health.",
publisher = "Portugal : Sociedade Portuguesa de Química",
journal = "Book of Abstracts of the XX EuroFoodChem Congress",
title = "Fatty acids composition of the most common bivalves in Korean diet",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3777"
}
Krstić-Ristivojević, M., Jovanović, V. B., Ristivojević, P.,& Ćirković-Veličković, T.. (2019). Fatty acids composition of the most common bivalves in Korean diet. in Book of Abstracts of the XX EuroFoodChem Congress
Portugal : Sociedade Portuguesa de Química..
https://hdl.handle.net/21.15107/rcub_cherry_3777
Krstić-Ristivojević M, Jovanović VB, Ristivojević P, Ćirković-Veličković T. Fatty acids composition of the most common bivalves in Korean diet. in Book of Abstracts of the XX EuroFoodChem Congress. 2019;.
https://hdl.handle.net/21.15107/rcub_cherry_3777 .
Krstić-Ristivojević, Maja, Jovanović, Vesna B., Ristivojević, Petar, Ćirković-Veličković, Tanja, "Fatty acids composition of the most common bivalves in Korean diet" in Book of Abstracts of the XX EuroFoodChem Congress (2019),
https://hdl.handle.net/21.15107/rcub_cherry_3777 .

In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Cvetković, Anka; Veljović, Đorđe; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija M.; Ćirković-Veličković, Tanja

(Elsevier, 2019)

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Cvetković, Anka
AU  - Veljović, Đorđe
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2857
AB  - An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.
PB  - Elsevier
T2  - Environment International
T1  - In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress
VL  - 126
SP  - 644
EP  - 658
DO  - 10.1016/j.envint.2019.03.001
ER  - 
@article{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Cvetković, Anka and Veljović, Đorđe and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.",
publisher = "Elsevier",
journal = "Environment International",
title = "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress",
volume = "126",
pages = "644-658",
doi = "10.1016/j.envint.2019.03.001"
}
Smiljanić, K., Prodić, I., Apostolović, D., Cvetković, A., Veljović, Đ., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2019). In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress. in Environment International
Elsevier., 126, 644-658.
https://doi.org/10.1016/j.envint.2019.03.001
Smiljanić K, Prodić I, Apostolović D, Cvetković A, Veljović Đ, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress. in Environment International. 2019;126:644-658.
doi:10.1016/j.envint.2019.03.001 .
Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Cvetković, Anka, Veljović, Đorđe, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija M., Ćirković-Veličković, Tanja, "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress" in Environment International, 126 (2019):644-658,
https://doi.org/10.1016/j.envint.2019.03.001 . .
2
6
5
7

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  - https://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  - 10.3390/foods8100463
ER  - 
@article{
author = "Prodić, Ivana and Smiljanić, Katarina and Simović, Ana and Radosavljević, Jelena and Ćirković-Veličković, Tanja",
year = "2019",
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 = "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. in Foods
MDPI., 8(10), 1-18.
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. in Foods. 2019;8(10):1-18.
doi:10.3390/foods8100463 .
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" in Foods, 8, no. 10 (2019):1-18,
https://doi.org/10.3390/foods8100463 . .
4
1
4

Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija M.; Ćirković-Veličković, Tanja

(Belgrade : Faculty of Chemistry, 2019)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3742
AB  - Field-realistic exposure studies provide the most relevant assessment of the
effects of the intensity and diversity of urban and industrial contamination on
pollen structure and allergenicity. The significance of in-depth post-translational
modification (PTM) studies of pollen proteomes, when compared with studies on
other aspects of pollution and altered pollen allergenicity, has not yet been
determined; hence, little progress has been made within this field.
PB  - Belgrade : Faculty of Chemistry
C3  - 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia
T1  - Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments
SP  - 6
EP  - 7
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3742
ER  - 
@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Field-realistic exposure studies provide the most relevant assessment of the
effects of the intensity and diversity of urban and industrial contamination on
pollen structure and allergenicity. The significance of in-depth post-translational
modification (PTM) studies of pollen proteomes, when compared with studies on
other aspects of pollution and altered pollen allergenicity, has not yet been
determined; hence, little progress has been made within this field.",
publisher = "Belgrade : Faculty of Chemistry",
journal = "1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia",
title = "Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments",
pages = "6-7",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3742"
}
Smiljanić, K., Prodić, I., Apostolović, D., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2019). Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments. in 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia
Belgrade : Faculty of Chemistry., 6-7.
https://hdl.handle.net/21.15107/rcub_cherry_3742
Smiljanić K, Prodić I, Apostolović D, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments. in 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia. 2019;:6-7.
https://hdl.handle.net/21.15107/rcub_cherry_3742 .
Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija M., Ćirković-Veličković, Tanja, "Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments" in 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia (2019):6-7,
https://hdl.handle.net/21.15107/rcub_cherry_3742 .

Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija M.; Ćirković-Veličković, Tanja

(2019)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3763
AB  - The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. 
Therefore, we created a comprehensive approach for the comparison of pollen from polluted and environmentally preserved areas. To examine the effects of long-term, in vivo pollen exposure to multiple source pollutants, Phleum pratense (Timothy grass) pollen samples were collected along a regional road in Kruševac, central Serbia and were compared with pollen samples from rural, environmentally preserved area over two consecutive pollination seasons. We combined the quantitative comparison of proteome expression profiles from in-solution and 2D-gels with unrestrictive in-depth quantitative PTM profiling using high resolution tandem mass spectrometry and the PEAKS 8.5 Suite platform.
An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, and significantly higher content of mercury, cadmium, and manganese. Antioxidative defense-related enzymes were significantly upregulated. Seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected pollen allergens, especially Phl p 6, with several different oxidative modifications. 
Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach was used for the first time to map extensive modifications in the pollen proteome, reflecting increased environmental oxidative stress, primarily caused by increased content of heavy metals in pollen.
C3  - XIV Italian Proteomics Association Annual Meeting with HPS, 2019.
T1  - Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution
SP  - 38
EP  - 38
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3763
ER  - 
@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. 
Therefore, we created a comprehensive approach for the comparison of pollen from polluted and environmentally preserved areas. To examine the effects of long-term, in vivo pollen exposure to multiple source pollutants, Phleum pratense (Timothy grass) pollen samples were collected along a regional road in Kruševac, central Serbia and were compared with pollen samples from rural, environmentally preserved area over two consecutive pollination seasons. We combined the quantitative comparison of proteome expression profiles from in-solution and 2D-gels with unrestrictive in-depth quantitative PTM profiling using high resolution tandem mass spectrometry and the PEAKS 8.5 Suite platform.
An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, and significantly higher content of mercury, cadmium, and manganese. Antioxidative defense-related enzymes were significantly upregulated. Seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected pollen allergens, especially Phl p 6, with several different oxidative modifications. 
Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach was used for the first time to map extensive modifications in the pollen proteome, reflecting increased environmental oxidative stress, primarily caused by increased content of heavy metals in pollen.",
journal = "XIV Italian Proteomics Association Annual Meeting with HPS, 2019.",
title = "Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution",
pages = "38-38",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3763"
}
Smiljanić, K., Prodić, I., Apostolović, D., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2019). Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution. in XIV Italian Proteomics Association Annual Meeting with HPS, 2019., 38-38.
https://hdl.handle.net/21.15107/rcub_cherry_3763
Smiljanić K, Prodić I, Apostolović D, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution. in XIV Italian Proteomics Association Annual Meeting with HPS, 2019.. 2019;:38-38.
https://hdl.handle.net/21.15107/rcub_cherry_3763 .
Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija M., Ćirković-Veličković, Tanja, "Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution" in XIV Italian Proteomics Association Annual Meeting with HPS, 2019. (2019):38-38,
https://hdl.handle.net/21.15107/rcub_cherry_3763 .

Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu

Mihailović, Jelena

(Универзитет у Београду, Хемијски факултет, 2019)

TY  - THES
AU  - Mihailović, Jelena
PY  - 2019
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=7675
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:22858/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=24146185
UR  - https://nardus.mpn.gov.rs/handle/123456789/17611
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4381
AB  - Alergija na hranu je reakcija preosetljivosti imunskog sistema na hranu koja dovodi dostvaranja IgE antitela. Ne postoji efikasan tretman i izbegavanje namirnica koje izazivajusimptome je jedini način za sprečavanje ozbiljnih posledica. Cilj ove teze je izučavanjeposttranslacionih i hemijskih modifikacija (PTM i HM) i interakcija alergena hrane sabiološki aktivnim polifenolom biljnog porekla.Alergija na crveno meso je novootkriveni tip odložene reakcije, sa PTM galaktozil-α-1,3-galaktozom (α-Gal) kao epitopom. Ispitani su podložnost model proteina - tiroglobulina(TG) digestiji pepsinom, prisustvo α-Gal na rezultujućim peptidima i pretpostavljenomesto vezivanja α-Gal za TG. Pokazano je da je α-Gal celim tokom simulirane želudačnedigestije vezan za nastale peptide TG, koji zadržavaju sposobnost da vežu IgE.Alergija na kikiriki je među najopasnijim zbog učestalosti, postojanosti i ozbiljnostisimptoma. Postoje razlike u alergenosti između sirovog i pečenog kikirikija, koje mogupoticati od razlika u modifikacijama alergena. U ovoj disertaciji je proučena razlika umodifikacijama glavnih alergena iz sirovog i pečenog kikirikija. Detektovano je 27modifikacija, od kojih 4 isključivo na proteinima pečenog kikirikija. Pokazane su razlikeu profilima modifikacija proteina između ekstrakata, koje mogu uticati na alergenost.2S albumini kikirikija su zbog kompaktne strukture otporni na delovanje digestivnihenzima, što se povezuje sa njihovom alergenošću. Ispitane su interakcije između njih iepigalokatehin-3-galata (EGCG), katehina zelenog čaja sa imunomodulatornimsvojstvima koji pospešuje digestiju proteina pepsinom. Vezivanje EGCG-a za alergeneizaziva promene u njihovoj strukturi (entalpijski povoljan proces), sa konstantamavezivanja reda veličine 104 M-1.
AB  - Food allergy is an immune system reaction to certain foods that results in IgE antibodygeneration. Efficient treatment does not exist, so avoidance of trigger foods is the onlyway to prevent serious consequences. The aim of this thesis was to study posttranslationaland chemical modifications (PTM and CM) of food allergens and their interactions withbiologically active plant polyphenol.Red meat allergy is a newly discovered type of allergy with delayed symptoms and aPTM - galactose-α-1,3-galactose (α-Gal) as an epitope. Digestibility of a model protein -thyroglobulin (TG) by pepsin and presence of α-Gal on resulting peptides was studied,and the position of α-Gal containing glycan on TG was proposed. It was shown thatthroughout simulated gastric digestion α-Gal remains bound to IgE reactive TG peptides.Peanut allergy is among most dangerous types of food allergies due to prevalence,persistence and symptom severity. Differences in allergenicity between raw and roastedpeanuts were previously shown and might stem from differences in protein modifications.Differences in major allergen modifications between raw and roasted peanut werestudied. Twenty-seven modifications were detected, 4 of which exclusively on allergensfrom roasted peanuts. Differences in modification profiling were found between the twoprotein preparations that can affect their allergenicity.Peanut 2S albumins are compact digestion-resistant proteins, which attributes to theirallergenicity. Their interactions with epigallocatechin-3-gallate (EGCG), animmunomodulatory green tea catechin that facilitates pepsin digestion of proteins werestudied. The results show that binding of EGCG to these allergens induces conformationalchanges, and is enthalpy favorable with binding constants of 104 M-1.
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu
UR  - https://hdl.handle.net/21.15107/rcub_nardus_17611
ER  - 
@phdthesis{
author = "Mihailović, Jelena",
year = "2019",
abstract = "Alergija na hranu je reakcija preosetljivosti imunskog sistema na hranu koja dovodi dostvaranja IgE antitela. Ne postoji efikasan tretman i izbegavanje namirnica koje izazivajusimptome je jedini način za sprečavanje ozbiljnih posledica. Cilj ove teze je izučavanjeposttranslacionih i hemijskih modifikacija (PTM i HM) i interakcija alergena hrane sabiološki aktivnim polifenolom biljnog porekla.Alergija na crveno meso je novootkriveni tip odložene reakcije, sa PTM galaktozil-α-1,3-galaktozom (α-Gal) kao epitopom. Ispitani su podložnost model proteina - tiroglobulina(TG) digestiji pepsinom, prisustvo α-Gal na rezultujućim peptidima i pretpostavljenomesto vezivanja α-Gal za TG. Pokazano je da je α-Gal celim tokom simulirane želudačnedigestije vezan za nastale peptide TG, koji zadržavaju sposobnost da vežu IgE.Alergija na kikiriki je među najopasnijim zbog učestalosti, postojanosti i ozbiljnostisimptoma. Postoje razlike u alergenosti između sirovog i pečenog kikirikija, koje mogupoticati od razlika u modifikacijama alergena. U ovoj disertaciji je proučena razlika umodifikacijama glavnih alergena iz sirovog i pečenog kikirikija. Detektovano je 27modifikacija, od kojih 4 isključivo na proteinima pečenog kikirikija. Pokazane su razlikeu profilima modifikacija proteina između ekstrakata, koje mogu uticati na alergenost.2S albumini kikirikija su zbog kompaktne strukture otporni na delovanje digestivnihenzima, što se povezuje sa njihovom alergenošću. Ispitane su interakcije između njih iepigalokatehin-3-galata (EGCG), katehina zelenog čaja sa imunomodulatornimsvojstvima koji pospešuje digestiju proteina pepsinom. Vezivanje EGCG-a za alergeneizaziva promene u njihovoj strukturi (entalpijski povoljan proces), sa konstantamavezivanja reda veličine 104 M-1., Food allergy is an immune system reaction to certain foods that results in IgE antibodygeneration. Efficient treatment does not exist, so avoidance of trigger foods is the onlyway to prevent serious consequences. The aim of this thesis was to study posttranslationaland chemical modifications (PTM and CM) of food allergens and their interactions withbiologically active plant polyphenol.Red meat allergy is a newly discovered type of allergy with delayed symptoms and aPTM - galactose-α-1,3-galactose (α-Gal) as an epitope. Digestibility of a model protein -thyroglobulin (TG) by pepsin and presence of α-Gal on resulting peptides was studied,and the position of α-Gal containing glycan on TG was proposed. It was shown thatthroughout simulated gastric digestion α-Gal remains bound to IgE reactive TG peptides.Peanut allergy is among most dangerous types of food allergies due to prevalence,persistence and symptom severity. Differences in allergenicity between raw and roastedpeanuts were previously shown and might stem from differences in protein modifications.Differences in major allergen modifications between raw and roasted peanut werestudied. Twenty-seven modifications were detected, 4 of which exclusively on allergensfrom roasted peanuts. Differences in modification profiling were found between the twoprotein preparations that can affect their allergenicity.Peanut 2S albumins are compact digestion-resistant proteins, which attributes to theirallergenicity. Their interactions with epigallocatechin-3-gallate (EGCG), animmunomodulatory green tea catechin that facilitates pepsin digestion of proteins werestudied. The results show that binding of EGCG to these allergens induces conformationalchanges, and is enthalpy favorable with binding constants of 104 M-1.",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu",
url = "https://hdl.handle.net/21.15107/rcub_nardus_17611"
}
Mihailović, J.. (2019). Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
https://hdl.handle.net/21.15107/rcub_nardus_17611
Mihailović J. Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu. in Универзитет у Београду. 2019;.
https://hdl.handle.net/21.15107/rcub_nardus_17611 .
Mihailović, Jelena, "Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu" in Универзитет у Београду (2019),
https://hdl.handle.net/21.15107/rcub_nardus_17611 .

Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu

Prodić, Ivana

(Универзитет у Београду, Хемијски факултет, 2019)

TY  - THES
AU  - Prodić, Ivana
PY  - 2019
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=7705
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:22917/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=23935753
UR  - https://nardus.mpn.gov.rs/handle/123456789/17617
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4384
AB  - INFOGEST metoda predstavlja standardizovani protokol za in vitro simulacijudigestije kompletne hrane, zasnovanom na fiziološki relevantnim uslovima. Predmetrada ove disertacije je ispitivanje digestibilnosti alergena kikirikija iz celog zrnaprimenom INFOGEST metode, kao i karakterizacija njihovih fragmenata otpornih naproteolizu.Za odstranjivanje lipida primenjena je metoda taloženja proteina, koja se pokazala kaosuperiornija u odnosu ekstrakciju lipida organskim rastvaračem, usled manjegkvalitativnog i kvantitativnog gubitka proteina.U ovoj tezi je pokazano da termički tretmani kikirikija, pored matriksa hrane, dodatnootežavaju oslobađanje proteina iz zrna, što čini glavne alergene kikirikija Ara h 1, Ara h2 Ara h 3 i Ara h 6 nedostupnijim za pepsinsku hidrolizu. Oslobađanje proteinakikirikija, kao i digestibilnost, u gastričnoj fazi se pokazala znatno izraženijom, uodnosu na intestinalnu fazu, s tim da je digestija kod pečenog kikirikija otežana uodnosu na sirovi. Nakon oralno-gastrične digestije celog zrna sirovog kikirikija, glavnialergeni kikirikija u velikoj meri ostaju intaktni, a njihovi peptidi otporni na digestijuzadržavaju alergeni kapacitet. Pokazano je da većina Ara h 2 i Ara h 6 alergena ostajerezistentna na digestiju. Ara h 1 i Ara h 3 kaskadno podležu pepsinolizi, do fragmenatakoji i dalje zadržavaju IgE vezujući potencijal. Mali peptidi koji potiču od Ara h 2alergena, su se pokazali kao najpotentniji inhibitori vezivanja IgE iz seruma pacijenataalergičnih na kikiriki, u odnosu na male Ara h 1 i Ara h 3 peptide.U ovoj disertaciji je pokazana izuzetno važna uloga efekata matriksa hrane, kao i njenetermičke obrade, na digestiju proteina hrane, koji mogu povećati stabilnost alergenahrane tokom digestije, i time omogućiti zadržavanje potencijala aktivacije alergijskereakcije nakon oralno-gastrične faze digestije.
AB  - INFOGEST method is standardized protocol for in vitro simulation of complete fooddigestion, based on physiologicaly relevant conditions. The objective of thisdissertation was to investigate digestibility of peanut allergens from whole peanutkernel by INFOGEST method, as well as to characterize their fragments resistant toproteolysis.For delipidation, protein precipitation approach was applied, showing to be superior incomparison to delipidation by organic solevent, due to lower qualitative andquantitative protein loss.In this thesis it was shown that peanut thermal processing, in addition to effect of foodmatix, further complicates the extractability and digestibility of proteins from the grain,making peanut allergens Ara h 1, 2, 3 and 6, less accessible for pepsin hydrolysis.Extractability and digestibility of peanut proteins in the gastric phase have shown to besignificantly more pronounced, in comparison to intestinal phase, and roasted peanutdigestion was impaired compared to the raw. It was shown that after oral and gastricdigestion of whole raw peanut grains peanut allergens largely remain intact, and theirdigestion resistant peptides retain allergenic capacity. The most Ara h 2 and Ara h 6allergens have been shown to remain resistant to digestion. Ara h 1 and Ara h 3undergo pepsinolysis with cascade pattern to consequently smaller peptide fragmentswith retained IgE binding capacity. Small peptides from Ara h 2 allergens were themost potent inhibitors of IgE binding from sera of peanut allergic patients, compared tosmall peptides from Ara h 1 and Ara h 3.This thesis points to the great importance of the effects of food matrix, as well as foodthermal processing, on protein digestibility, which can create additional stability offood allergens during digestion, and thus enable retaining of their potential for thesensitization or triggering of allergic reactions.
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu
UR  - https://hdl.handle.net/21.15107/rcub_nardus_17617
ER  - 
@phdthesis{
author = "Prodić, Ivana",
year = "2019",
abstract = "INFOGEST metoda predstavlja standardizovani protokol za in vitro simulacijudigestije kompletne hrane, zasnovanom na fiziološki relevantnim uslovima. Predmetrada ove disertacije je ispitivanje digestibilnosti alergena kikirikija iz celog zrnaprimenom INFOGEST metode, kao i karakterizacija njihovih fragmenata otpornih naproteolizu.Za odstranjivanje lipida primenjena je metoda taloženja proteina, koja se pokazala kaosuperiornija u odnosu ekstrakciju lipida organskim rastvaračem, usled manjegkvalitativnog i kvantitativnog gubitka proteina.U ovoj tezi je pokazano da termički tretmani kikirikija, pored matriksa hrane, dodatnootežavaju oslobađanje proteina iz zrna, što čini glavne alergene kikirikija Ara h 1, Ara h2 Ara h 3 i Ara h 6 nedostupnijim za pepsinsku hidrolizu. Oslobađanje proteinakikirikija, kao i digestibilnost, u gastričnoj fazi se pokazala znatno izraženijom, uodnosu na intestinalnu fazu, s tim da je digestija kod pečenog kikirikija otežana uodnosu na sirovi. Nakon oralno-gastrične digestije celog zrna sirovog kikirikija, glavnialergeni kikirikija u velikoj meri ostaju intaktni, a njihovi peptidi otporni na digestijuzadržavaju alergeni kapacitet. Pokazano je da većina Ara h 2 i Ara h 6 alergena ostajerezistentna na digestiju. Ara h 1 i Ara h 3 kaskadno podležu pepsinolizi, do fragmenatakoji i dalje zadržavaju IgE vezujući potencijal. Mali peptidi koji potiču od Ara h 2alergena, su se pokazali kao najpotentniji inhibitori vezivanja IgE iz seruma pacijenataalergičnih na kikiriki, u odnosu na male Ara h 1 i Ara h 3 peptide.U ovoj disertaciji je pokazana izuzetno važna uloga efekata matriksa hrane, kao i njenetermičke obrade, na digestiju proteina hrane, koji mogu povećati stabilnost alergenahrane tokom digestije, i time omogućiti zadržavanje potencijala aktivacije alergijskereakcije nakon oralno-gastrične faze digestije., INFOGEST method is standardized protocol for in vitro simulation of complete fooddigestion, based on physiologicaly relevant conditions. The objective of thisdissertation was to investigate digestibility of peanut allergens from whole peanutkernel by INFOGEST method, as well as to characterize their fragments resistant toproteolysis.For delipidation, protein precipitation approach was applied, showing to be superior incomparison to delipidation by organic solevent, due to lower qualitative andquantitative protein loss.In this thesis it was shown that peanut thermal processing, in addition to effect of foodmatix, further complicates the extractability and digestibility of proteins from the grain,making peanut allergens Ara h 1, 2, 3 and 6, less accessible for pepsin hydrolysis.Extractability and digestibility of peanut proteins in the gastric phase have shown to besignificantly more pronounced, in comparison to intestinal phase, and roasted peanutdigestion was impaired compared to the raw. It was shown that after oral and gastricdigestion of whole raw peanut grains peanut allergens largely remain intact, and theirdigestion resistant peptides retain allergenic capacity. The most Ara h 2 and Ara h 6allergens have been shown to remain resistant to digestion. Ara h 1 and Ara h 3undergo pepsinolysis with cascade pattern to consequently smaller peptide fragmentswith retained IgE binding capacity. Small peptides from Ara h 2 allergens were themost potent inhibitors of IgE binding from sera of peanut allergic patients, compared tosmall peptides from Ara h 1 and Ara h 3.This thesis points to the great importance of the effects of food matrix, as well as foodthermal processing, on protein digestibility, which can create additional stability offood allergens during digestion, and thus enable retaining of their potential for thesensitization or triggering of allergic reactions.",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu",
url = "https://hdl.handle.net/21.15107/rcub_nardus_17617"
}
Prodić, I.. (2019). Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
https://hdl.handle.net/21.15107/rcub_nardus_17617
Prodić I. Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu. in Универзитет у Београду. 2019;.
https://hdl.handle.net/21.15107/rcub_nardus_17617 .
Prodić, Ivana, "Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu" in Универзитет у Београду (2019),
https://hdl.handle.net/21.15107/rcub_nardus_17617 .

Physicochemical characterization of soluble proteins of whole camel milk powders produced by spray drying treatment at high temperatures

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

(2019)

TY  - CONF
AU  - Peruško, Marija
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Smiljanić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Stanić-Vučinić, Dragana
AU  - Ghnimi, Sami
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5131
AB  - Objective. Camel milk is highly nutritious food with numerous health benefits
proposed. Demand for camel milk has increased worldwide. Production of camel milk
powders facilitate its transport, prolonge shelf-life, and also offer an attractive additive
for various food products. In this study we characterized proteins of soluble fraction of
freeze/spray dried camel milk powders.
Material and Methods. Whole camel milk powders were prepared by spray drying
treatment at six different inlet temperatures (190°C - 250°C) or by freeze drying. The
soluble protein fractions upon the treatments were analysed by combination of
electrophoretic and spectroscopic techniques. Functional properties, such as
antioxidant activity and protein solubility were assessed.
Results. SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while
native electrophoresis revealed non-uniform decrease in pI values with increased inlet
temperature of spray drying. That indicated attachement of lactose moieties to NH2-
group of proteins via non-enzymatic Maillard reaction. Spectrophotometric analysis
showed formation of intermediate Maillard reaction products (increased absorbance at
294 nm) and no detectable late Maillard reaction products formation. Far-UV circular
dichroism spectra showed no differences in secondary structures between freeze and
spray dried samples. Antioxidant activity and protein solubility were increased with
increase in inlet temperature.
Conclusions. Our results showed that spray drying treatment promoted non-enzymatic
glycation of camel milk proteins. Glycation of food proteins affects their technofunctional
properties, shelf-life and nutritional value. Thus, optimization of spray
drying parametars is essential for production of high quality camel milk powders.
Acknowledgements: This research work was funded the Ministry of Education and Science of the Republic
of Serbia, GA No. OI172024, Ghent University Global Campus, Belgian Special Research Fund BOF StG No.
01N01718, Serbian Academy of Sciences and Arts Project F-26. The project leading to this application
has received funding from the European Union's Horizon 2020 research and innovation programme under
grant agreement No 810752.
C3  - 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Book of Abstracts, June 20-21, 2019, Belgrade, Serbia
T1  - Physicochemical characterization of soluble proteins of whole camel milk powders produced by spray drying treatment at high temperatures
SP  - 27
EP  - 27
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5131
ER  - 
@conference{
author = "Peruško, Marija and Simović, Ana and Stevanović, Nikola R. and Smiljanić, Katarina and Radomirović, Mirjana Ž. and Stanić-Vučinić, Dragana and Ghnimi, Sami and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Objective. Camel milk is highly nutritious food with numerous health benefits
proposed. Demand for camel milk has increased worldwide. Production of camel milk
powders facilitate its transport, prolonge shelf-life, and also offer an attractive additive
for various food products. In this study we characterized proteins of soluble fraction of
freeze/spray dried camel milk powders.
Material and Methods. Whole camel milk powders were prepared by spray drying
treatment at six different inlet temperatures (190°C - 250°C) or by freeze drying. The
soluble protein fractions upon the treatments were analysed by combination of
electrophoretic and spectroscopic techniques. Functional properties, such as
antioxidant activity and protein solubility were assessed.
Results. SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while
native electrophoresis revealed non-uniform decrease in pI values with increased inlet
temperature of spray drying. That indicated attachement of lactose moieties to NH2-
group of proteins via non-enzymatic Maillard reaction. Spectrophotometric analysis
showed formation of intermediate Maillard reaction products (increased absorbance at
294 nm) and no detectable late Maillard reaction products formation. Far-UV circular
dichroism spectra showed no differences in secondary structures between freeze and
spray dried samples. Antioxidant activity and protein solubility were increased with
increase in inlet temperature.
Conclusions. Our results showed that spray drying treatment promoted non-enzymatic
glycation of camel milk proteins. Glycation of food proteins affects their technofunctional
properties, shelf-life and nutritional value. Thus, optimization of spray
drying parametars is essential for production of high quality camel milk powders.
Acknowledgements: This research work was funded the Ministry of Education and Science of the Republic
of Serbia, GA No. OI172024, Ghent University Global Campus, Belgian Special Research Fund BOF StG No.
01N01718, Serbian Academy of Sciences and Arts Project F-26. The project leading to this application
has received funding from the European Union's Horizon 2020 research and innovation programme under
grant agreement No 810752.",
journal = "1st FoodEnTwin Workshop “Food and Environmental -Omics”, Book of Abstracts, June 20-21, 2019, Belgrade, Serbia",
title = "Physicochemical characterization of soluble proteins of whole camel milk powders produced by spray drying treatment at high temperatures",
pages = "27-27",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5131"
}
Peruško, M., Simović, A., Stevanović, N. R., Smiljanić, K., Radomirović, M. Ž., Stanić-Vučinić, D., Ghnimi, S.,& Ćirković-Veličković, T.. (2019). Physicochemical characterization of soluble proteins of whole camel milk powders produced by spray drying treatment at high temperatures. in 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Book of Abstracts, June 20-21, 2019, Belgrade, Serbia, 27-27.
https://hdl.handle.net/21.15107/rcub_cherry_5131
Peruško M, Simović A, Stevanović NR, Smiljanić K, Radomirović MŽ, Stanić-Vučinić D, Ghnimi S, Ćirković-Veličković T. Physicochemical characterization of soluble proteins of whole camel milk powders produced by spray drying treatment at high temperatures. in 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Book of Abstracts, June 20-21, 2019, Belgrade, Serbia. 2019;:27-27.
https://hdl.handle.net/21.15107/rcub_cherry_5131 .
Peruško, Marija, Simović, Ana, Stevanović, Nikola R., Smiljanić, Katarina, Radomirović, Mirjana Ž., Stanić-Vučinić, Dragana, Ghnimi, Sami, Ćirković-Veličković, Tanja, "Physicochemical characterization of soluble proteins of whole camel milk powders produced by spray drying treatment at high temperatures" in 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Book of Abstracts, June 20-21, 2019, Belgrade, Serbia (2019):27-27,
https://hdl.handle.net/21.15107/rcub_cherry_5131 .

Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment

Peruško, Marija; Simović, Ana; Stevanović, Nikola; Smiljanić, Katarina; Radomirović, Mirjana Ž.; Stanić-Vučinić, Dragana; Ghnimi, Sami; Ćirković-Veličković, Tanja

(The Faculty of Sciences, University of Novi Sad, Serbian proteomic association, 2019)

TY  - CONF
AU  - Peruško, Marija
AU  - Simović, Ana
AU  - Stevanović, Nikola
AU  - Smiljanić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Stanić-Vučinić, Dragana
AU  - Ghnimi, Sami
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5129
AB  - Objective: Camel milk is highly nutritious food with numerous health benefits proposed. Demand
for camel milk has increased worldwide.Production of camel milk powders facilitate its transport,
prolonge shelf-life, and also offer an attractive additive for various food products. In this study we
characterized proteins of soluble fraction of freeze/spray dried camel milk powders.
Material and Methods: Whole camel milk powders were prepared by spray drying treatment at six
different inlet temperatures (190°C - 250°C) or by freeze drying. The soluble protein fractions upon
the treatments were analysed by combination of electrophoretic techniques and circular dichroism.
Freeze dried camel milk and spray dried at 250°C were analysed by mass spectrometry.
Results: SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while native
electrophoresis revealed non-uniform decrease in pI values with increased inlet temperature of
spray drying. That indicated occurence of the Maillard reaction. Far-UV circular dichroism spectra
showed no differences in secondary structures between freeze and spray dried samples. Mass
spectrometry identified α-lactalbumin, glycosylation-dependant cell adhesion molecule 1
(GLYCAM1), immunoglobulin heavy chain, peptidoglycan recognition protein and camel serum
albumin as dominant proteins in soluble fraction of camel milk powders. Carboxymethyl-lisyne
(CML), well known marker of Maillard reaction in food analysis, was detected on GLYCAM1 and on
immunoglobulin heavy chain.
Conclusions: Our results indicate glycation of camel milk proteins via Maillard reaction upon spray
drying treatment which further may affect techno-functional properties of camel milk powders,
their shelf-life and nutritional value.
Acknowledgments: This work was supported by the Ministry of Education, Science and
Technological Development of the Republic of Serbia, grant number 172024. The project leading to
this application has received funding from the European Union's Horizon 2020 research and
innovation programme under grant agreement No 810752.
PB  - The Faculty of Sciences, University of Novi Sad, Serbian proteomic association
C3  - The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia
T1  - Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment
SP  - 7
EP  - 7
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5129
ER  - 
@conference{
author = "Peruško, Marija and Simović, Ana and Stevanović, Nikola and Smiljanić, Katarina and Radomirović, Mirjana Ž. and Stanić-Vučinić, Dragana and Ghnimi, Sami and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Objective: Camel milk is highly nutritious food with numerous health benefits proposed. Demand
for camel milk has increased worldwide.Production of camel milk powders facilitate its transport,
prolonge shelf-life, and also offer an attractive additive for various food products. In this study we
characterized proteins of soluble fraction of freeze/spray dried camel milk powders.
Material and Methods: Whole camel milk powders were prepared by spray drying treatment at six
different inlet temperatures (190°C - 250°C) or by freeze drying. The soluble protein fractions upon
the treatments were analysed by combination of electrophoretic techniques and circular dichroism.
Freeze dried camel milk and spray dried at 250°C were analysed by mass spectrometry.
Results: SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while native
electrophoresis revealed non-uniform decrease in pI values with increased inlet temperature of
spray drying. That indicated occurence of the Maillard reaction. Far-UV circular dichroism spectra
showed no differences in secondary structures between freeze and spray dried samples. Mass
spectrometry identified α-lactalbumin, glycosylation-dependant cell adhesion molecule 1
(GLYCAM1), immunoglobulin heavy chain, peptidoglycan recognition protein and camel serum
albumin as dominant proteins in soluble fraction of camel milk powders. Carboxymethyl-lisyne
(CML), well known marker of Maillard reaction in food analysis, was detected on GLYCAM1 and on
immunoglobulin heavy chain.
Conclusions: Our results indicate glycation of camel milk proteins via Maillard reaction upon spray
drying treatment which further may affect techno-functional properties of camel milk powders,
their shelf-life and nutritional value.
Acknowledgments: This work was supported by the Ministry of Education, Science and
Technological Development of the Republic of Serbia, grant number 172024. The project leading to
this application has received funding from the European Union's Horizon 2020 research and
innovation programme under grant agreement No 810752.",
publisher = "The Faculty of Sciences, University of Novi Sad, Serbian proteomic association",
journal = "The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia",
title = "Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment",
pages = "7-7",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5129"
}
Peruško, M., Simović, A., Stevanović, N., Smiljanić, K., Radomirović, M. Ž., Stanić-Vučinić, D., Ghnimi, S.,& Ćirković-Veličković, T.. (2019). Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment. in The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia
The Faculty of Sciences, University of Novi Sad, Serbian proteomic association., 7-7.
https://hdl.handle.net/21.15107/rcub_cherry_5129
Peruško M, Simović A, Stevanović N, Smiljanić K, Radomirović MŽ, Stanić-Vučinić D, Ghnimi S, Ćirković-Veličković T. Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment. in The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia. 2019;:7-7.
https://hdl.handle.net/21.15107/rcub_cherry_5129 .
Peruško, Marija, Simović, Ana, Stevanović, Nikola, Smiljanić, Katarina, Radomirović, Mirjana Ž., Stanić-Vučinić, Dragana, Ghnimi, Sami, Ćirković-Veličković, Tanja, "Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment" in The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia (2019):7-7,
https://hdl.handle.net/21.15107/rcub_cherry_5129 .

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

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

(Elsevier, 2019)

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

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

EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study",
volume = "278",
pages = "388-395",
doi = "10.1016/j.foodchem.2018.11.038"
}
Radibratović, M., Al-Hanish, A., Minić, S. L., Radomirović, M. Ž., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2019). Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. in Food Chemistry
Elsevier., 278, 388-395.
https://doi.org/10.1016/j.foodchem.2018.11.038
Radibratović M, Al-Hanish A, Minić SL, Radomirović MŽ, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. in Food Chemistry. 2019;278:388-395.
doi:10.1016/j.foodchem.2018.11.038 .
Radibratović, Milica, Al-Hanish, Ayah, Minić, Simeon L., Radomirović, Mirjana Ž., Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study" in Food Chemistry, 278 (2019):388-395,
https://doi.org/10.1016/j.foodchem.2018.11.038 . .
8
5
8