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 .

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 .

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 .

TY  - JOUR
AU  - Costa, Joana
AU  - Villa, Caterina
AU  - Verhoeckx, Kitty
AU  - Ćirković-Veličković, Tanja
AU  - Schrama, Denise
AU  - Roncada, Paola
AU  - Rodrigues, Pedro M.
AU  - Piras, Cristian
AU  - Martín-Pedraza, Laura
AU  - Monaci, Linda
AU  - Molina, Elena
AU  - Mazzucchelli, Gabriel
AU  - Mafra, Isabel
AU  - Lupi, Roberta
AU  - Lozano-Ojalvo, Daniel
AU  - Larré, Colette
AU  - Klueber, Julia
AU  - Gelencser, Eva
AU  - Bueno-Diaz, Cristina
AU  - Diaz-Perales, Araceli
AU  - Benedé, Sara
AU  - Bavaro, Simona Lucia
AU  - Kuehn, Annette
AU  - Hoffmann-Sommergruber, Karin
AU  - Holzhauser, Thomas
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5791
AB  - Key determinants for the development of an allergic response to an otherwise ‘harmless’ food protein involve different factors like the predisposition of the individual, the timing, the dose, the route of exposure, the intrinsic properties of the allergen, the food matrix (e.g. lipids) and the allergen modification by food processing. Various physicochemical parameters can have an impact on the allergenicity of animal proteins. Following our previous review on how physicochemical parameters shape plant protein allergenicity, the same analysis was proceeded here for animal allergens.
T2  - Clinical Reviews in Allergy & Immunology
T1  - Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?
VL  - 62
IS  - 1
SP  - 1
EP  - 36
DO  - 10.1007/s12016-020-08826-1
ER  - 

@article{
author = "Costa, Joana and Villa, Caterina and Verhoeckx, Kitty and Ćirković-Veličković, Tanja and Schrama, Denise and Roncada, Paola and Rodrigues, Pedro M. and Piras, Cristian and Martín-Pedraza, Laura and Monaci, Linda and Molina, Elena and Mazzucchelli, Gabriel and Mafra, Isabel and Lupi, Roberta and Lozano-Ojalvo, Daniel and Larré, Colette and Klueber, Julia and Gelencser, Eva and Bueno-Diaz, Cristina and Diaz-Perales, Araceli and Benedé, Sara and Bavaro, Simona Lucia and Kuehn, Annette and Hoffmann-Sommergruber, Karin and Holzhauser, Thomas",
year = "2022",
abstract = "Key determinants for the development of an allergic response to an otherwise ‘harmless’ food protein involve different factors like the predisposition of the individual, the timing, the dose, the route of exposure, the intrinsic properties of the allergen, the food matrix (e.g. lipids) and the allergen modification by food processing. Various physicochemical parameters can have an impact on the allergenicity of animal proteins. Following our previous review on how physicochemical parameters shape plant protein allergenicity, the same analysis was proceeded here for animal allergens.",
journal = "Clinical Reviews in Allergy & Immunology",
title = "Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?",
volume = "62",
number = "1",
pages = "1-36",
doi = "10.1007/s12016-020-08826-1"
}

Costa, J., Villa, C., Verhoeckx, K., Ćirković-Veličković, T., Schrama, D., Roncada, P., Rodrigues, P. M., Piras, C., Martín-Pedraza, L., Monaci, L., Molina, E., Mazzucchelli, G., Mafra, I., Lupi, R., Lozano-Ojalvo, D., Larré, C., Klueber, J., Gelencser, E., Bueno-Diaz, C., Diaz-Perales, A., Benedé, S., Bavaro, S. L., Kuehn, A., Hoffmann-Sommergruber, K.,& Holzhauser, T.. (2022). Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?. in Clinical Reviews in Allergy & Immunology, 62(1), 1-36.
https://doi.org/10.1007/s12016-020-08826-1

Costa J, Villa C, Verhoeckx K, Ćirković-Veličković T, Schrama D, Roncada P, Rodrigues PM, Piras C, Martín-Pedraza L, Monaci L, Molina E, Mazzucchelli G, Mafra I, Lupi R, Lozano-Ojalvo D, Larré C, Klueber J, Gelencser E, Bueno-Diaz C, Diaz-Perales A, Benedé S, Bavaro SL, Kuehn A, Hoffmann-Sommergruber K, Holzhauser T. Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?. in Clinical Reviews in Allergy & Immunology. 2022;62(1):1-36.
doi:10.1007/s12016-020-08826-1 .

Costa, Joana, Villa, Caterina, Verhoeckx, Kitty, Ćirković-Veličković, Tanja, Schrama, Denise, Roncada, Paola, Rodrigues, Pedro M., Piras, Cristian, Martín-Pedraza, Laura, Monaci, Linda, Molina, Elena, Mazzucchelli, Gabriel, Mafra, Isabel, Lupi, Roberta, Lozano-Ojalvo, Daniel, Larré, Colette, Klueber, Julia, Gelencser, Eva, Bueno-Diaz, Cristina, Diaz-Perales, Araceli, Benedé, Sara, Bavaro, Simona Lucia, Kuehn, Annette, Hoffmann-Sommergruber, Karin, Holzhauser, Thomas, "Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?" in Clinical Reviews in Allergy & Immunology, 62, no. 1 (2022):1-36,
https://doi.org/10.1007/s12016-020-08826-1 . .

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 . .

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 . .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Ćirković-Veličković, Tanja
AU  - Rajković, Andreja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6036
AB  - Food allergies represent important health problem in industrialized countries, with seafood being recognized as one of the 8 most common sources of allergens. While there are several proteins that have been linked to shellfish allergy, tropomyosin accounts for majority of diagnozed ingestion-related shellfish allergies. Presence of even traces of allergens in food can be a serious health hazard to consumers, which is why proper labeling of food products by food manufacturers is of critical importance for sensitized persons. On the other hand, development of reliable, specific and sensitive methods for detection and quantification of allergens in food products is of the high importance as well. The objective of this study was to develop highly sensitive immuno-polymerase chain reaction (immuno PCR) method for the detection and quantification of shellfish tropomyosin in food samples. Immuno PCR method couples standard sandwich enzyme-linked immunosorbent assay (ELISA) format with real time PCR. Monoclonal antibody was used as capture antibody, while biotinylated polyclonal antibody served as detection antibody. Reporter biotinylated DNA was coupled to detection antibody via streptavidin and subsequently amplified and quantified by real time PCR. Tropomyosin was quantified using highly purified natural shrimp tropomyosin as standard. The results were compared to standard sandwich ELISA.
PB  - University of Vienna
C3  - 2nd FoodEnTwin Workshop “Experimental animal models for food and environment”, Vienna, Austria, 3rd-4th February, 2020. In: Book of Abstracts
T1  - Development of an immuno-polymerase chain reaction for detection and quantification of shellfish tropomyosin
SP  - S4
EP  - S4
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6036
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Ćirković-Veličković, Tanja and Rajković, Andreja",
year = "2020",
abstract = "Food allergies represent important health problem in industrialized countries, with seafood being recognized as one of the 8 most common sources of allergens. While there are several proteins that have been linked to shellfish allergy, tropomyosin accounts for majority of diagnozed ingestion-related shellfish allergies. Presence of even traces of allergens in food can be a serious health hazard to consumers, which is why proper labeling of food products by food manufacturers is of critical importance for sensitized persons. On the other hand, development of reliable, specific and sensitive methods for detection and quantification of allergens in food products is of the high importance as well. The objective of this study was to develop highly sensitive immuno-polymerase chain reaction (immuno PCR) method for the detection and quantification of shellfish tropomyosin in food samples. Immuno PCR method couples standard sandwich enzyme-linked immunosorbent assay (ELISA) format with real time PCR. Monoclonal antibody was used as capture antibody, while biotinylated polyclonal antibody served as detection antibody. Reporter biotinylated DNA was coupled to detection antibody via streptavidin and subsequently amplified and quantified by real time PCR. Tropomyosin was quantified using highly purified natural shrimp tropomyosin as standard. The results were compared to standard sandwich ELISA.",
publisher = "University of Vienna",
journal = "2nd FoodEnTwin Workshop “Experimental animal models for food and environment”, Vienna, Austria, 3rd-4th February, 2020. In: Book of Abstracts",
title = "Development of an immuno-polymerase chain reaction for detection and quantification of shellfish tropomyosin",
pages = "S4-S4",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6036"
}

Radomirović, M. Ž., Ćirković-Veličković, T.,& Rajković, A.. (2020). Development of an immuno-polymerase chain reaction for detection and quantification of shellfish tropomyosin. in 2nd FoodEnTwin Workshop “Experimental animal models for food and environment”, Vienna, Austria, 3rd-4th February, 2020. In: Book of Abstracts
University of Vienna., S4-S4.
https://hdl.handle.net/21.15107/rcub_cherry_6036

Radomirović MŽ, Ćirković-Veličković T, Rajković A. Development of an immuno-polymerase chain reaction for detection and quantification of shellfish tropomyosin. in 2nd FoodEnTwin Workshop “Experimental animal models for food and environment”, Vienna, Austria, 3rd-4th February, 2020. In: Book of Abstracts. 2020;:S4-S4.
https://hdl.handle.net/21.15107/rcub_cherry_6036 .

Radomirović, Mirjana Ž., Ćirković-Veličković, Tanja, Rajković, Andreja, "Development of an immuno-polymerase chain reaction for detection and quantification of shellfish tropomyosin" in 2nd FoodEnTwin Workshop “Experimental animal models for food and environment”, Vienna, Austria, 3rd-4th February, 2020. In: Book of Abstracts (2020):S4-S4,
https://hdl.handle.net/21.15107/rcub_cherry_6036 .

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 . .

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 . .

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 .

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 .

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 . .

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 . .

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 .

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 . .

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 . .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić Šipka, Sanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6037
AB  - The ruthenium-based antitumour compounds act more via protein targets involved in carcinogenesis, in contrast to platinum-based compounds. Also, after intravenous administration of antitumour complexes proteins are the first binding targets in circulation. Therefore, interactions of anticancer compounds with proteins are important for elucidation of their pharmacokinetic pathways. Four half-sandwich ruthenium(II)-cymene complexes (C1, C2, C3 and C4), developed earlier and with promising cytotoxic activity, are investigated for their interactions with cytochrome c (Cyt). Complexes  were incubated with Cyt for 48 h at 37 °C and high-resolution LTQ-Orbitrap ESI MS was used to monitor the formed adducts. The changes in heme state and tertiary structure around the heme were monitored by CD and UV-VIS spectra in the presence of oxygen. The complexes containing two chloride ligands (C2 and C3) were more reactive toward Cyt than those with only one (C1 and C4). The complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). All complexes reduced heme iron of Cyt, but the extent of reduction was inverse to the order of their reactivity to Cyt (C1>C4>>C2>C3). CD spectra in Soret region indicated that Cyt reduction was accompanied with slight tertiary structure change, the rupture of ferro-Met-80 and occupation of this heme coordination site by His-33/His-26. Extent of  heme reduction by complexes inverse with respect to their reactivity implies that initially noncovalent binding of complexes occures, causing heme reduction, followed by comlex coordination to protein. In the presence of less reactive complexes more intensive reduction of heme leaves less available histidine residues (main targets for Ru coordination), leading to less efficient formation of adducts.
C3  - 1st FoodEnTwin Workshop “Food and Environmental –Omics”, Belgrade, Serbia, 20th-21st June, 2019. In: Book of Abstracts
T1  - Interactions of ruthenium(II)-cymene complexes with cytochrome c
SP  - 24
EP  - 24
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6037
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Stanić-Vučinić, Dragana and Nikolić, Stefan and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić Šipka, Sanja",
year = "2019",
abstract = "The ruthenium-based antitumour compounds act more via protein targets involved in carcinogenesis, in contrast to platinum-based compounds. Also, after intravenous administration of antitumour complexes proteins are the first binding targets in circulation. Therefore, interactions of anticancer compounds with proteins are important for elucidation of their pharmacokinetic pathways. Four half-sandwich ruthenium(II)-cymene complexes (C1, C2, C3 and C4), developed earlier and with promising cytotoxic activity, are investigated for their interactions with cytochrome c (Cyt). Complexes  were incubated with Cyt for 48 h at 37 °C and high-resolution LTQ-Orbitrap ESI MS was used to monitor the formed adducts. The changes in heme state and tertiary structure around the heme were monitored by CD and UV-VIS spectra in the presence of oxygen. The complexes containing two chloride ligands (C2 and C3) were more reactive toward Cyt than those with only one (C1 and C4). The complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). All complexes reduced heme iron of Cyt, but the extent of reduction was inverse to the order of their reactivity to Cyt (C1>C4>>C2>C3). CD spectra in Soret region indicated that Cyt reduction was accompanied with slight tertiary structure change, the rupture of ferro-Met-80 and occupation of this heme coordination site by His-33/His-26. Extent of  heme reduction by complexes inverse with respect to their reactivity implies that initially noncovalent binding of complexes occures, causing heme reduction, followed by comlex coordination to protein. In the presence of less reactive complexes more intensive reduction of heme leaves less available histidine residues (main targets for Ru coordination), leading to less efficient formation of adducts.",
journal = "1st FoodEnTwin Workshop “Food and Environmental –Omics”, Belgrade, Serbia, 20th-21st June, 2019. In: Book of Abstracts",
title = "Interactions of ruthenium(II)-cymene complexes with cytochrome c",
pages = "24-24",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6037"
}

Radomirović, M. Ž., Stanić-Vučinić, D., Nikolić, S., Mihailović, J., Ćirković-Veličković, T.,& Grgurić Šipka, S.. (2019). Interactions of ruthenium(II)-cymene complexes with cytochrome c. in 1st FoodEnTwin Workshop “Food and Environmental –Omics”, Belgrade, Serbia, 20th-21st June, 2019. In: Book of Abstracts, 24-24.
https://hdl.handle.net/21.15107/rcub_cherry_6037

Radomirović MŽ, Stanić-Vučinić D, Nikolić S, Mihailović J, Ćirković-Veličković T, Grgurić Šipka S. Interactions of ruthenium(II)-cymene complexes with cytochrome c. in 1st FoodEnTwin Workshop “Food and Environmental –Omics”, Belgrade, Serbia, 20th-21st June, 2019. In: Book of Abstracts. 2019;:24-24.
https://hdl.handle.net/21.15107/rcub_cherry_6037 .

Radomirović, Mirjana Ž., Stanić-Vučinić, Dragana, Nikolić, Stefan, Mihailović, Jelena, Ćirković-Veličković, Tanja, Grgurić Šipka, Sanja, "Interactions of ruthenium(II)-cymene complexes with cytochrome c" in 1st FoodEnTwin Workshop “Food and Environmental –Omics”, Belgrade, Serbia, 20th-21st June, 2019. In: Book of Abstracts (2019):24-24,
https://hdl.handle.net/21.15107/rcub_cherry_6037 .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić Šipka, Sanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6038
AB  - Objective. In contrast to platinum-based antitumour compounds, the mode of action of ruthenium-based compounds is via protein targets involved in cellular signaling pathways and the histone proteins. As proteins are the first potential binding targets for the complexes in the bloodstream after their intravenous administration, interactions of anticancer therapeutics with proteins are very important to be investigated with aim to elucidate their pharmacokinetic pathways. Four half-sandwich ruthenium(II)-cymene complexes, developed earlier and with promising cytotoxic activity, are investigated  for their interactions with proteins, cytochrome c and lysozyme.

Material and Methods. Ruthenium(II)-cymene complexes were incubated for 24 and 48 h at 37 °C in the presence of cytochrome c and lysozyme, both in 20 mM ammonium hydrogen carbonate pH 7.4 and water. High-resolution LTQ-Orbitrap ESI MS was used to monitor the adducts formed between ruthenium complexes and proteins.

Results. The complexes with two Cl- ligands have shown higher reactivity to proteins than those with only one, and were more reactive toward cytochrome c in comparison to lysozyme. The complex with S,N-chelating ligand was less reactive to proteins than one with O,N-chelating ligand. Species initially coordinating the proteins are most likely dehalogenated complexes. During the time, vivid ligand exchange of non-arene organic ligand L with CO32- and OH- takes place after initial formation of protein adducts. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could be expected generating different intermediate protein species. 

Conclusions. Protein reactivity toward Ru(II) complexes is determined by protein structure and ligands in Ru(II) coordination sphere, but this reactivity should be described from both kinetics, as well as stability aspect. In extracellular or intracellular milieu, ability of metal binding ligands (such as carbonate ions) to bind and to leave, determinate both the extent and mechanism of the binding of ruthenium complexes to the target biomacromolecules for cancer therapy.
PB  - Faculty of Sciences
PB  - University of Novi Sad
PB  - Serbian Proteomics Assosication
C3  - V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad, Serbia, 31st May, 2019. In: The Book of Abstracts
T1  - Lysozyme and Cytochrome C adducts of ruthenium(II)-cymene complexes
SP  - P2
EP  - P2
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6038
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Stanić-Vučinić, Dragana and Nikolić, Stefan and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić Šipka, Sanja",
year = "2019",
abstract = "Objective. In contrast to platinum-based antitumour compounds, the mode of action of ruthenium-based compounds is via protein targets involved in cellular signaling pathways and the histone proteins. As proteins are the first potential binding targets for the complexes in the bloodstream after their intravenous administration, interactions of anticancer therapeutics with proteins are very important to be investigated with aim to elucidate their pharmacokinetic pathways. Four half-sandwich ruthenium(II)-cymene complexes, developed earlier and with promising cytotoxic activity, are investigated  for their interactions with proteins, cytochrome c and lysozyme.

Material and Methods. Ruthenium(II)-cymene complexes were incubated for 24 and 48 h at 37 °C in the presence of cytochrome c and lysozyme, both in 20 mM ammonium hydrogen carbonate pH 7.4 and water. High-resolution LTQ-Orbitrap ESI MS was used to monitor the adducts formed between ruthenium complexes and proteins.

Results. The complexes with two Cl- ligands have shown higher reactivity to proteins than those with only one, and were more reactive toward cytochrome c in comparison to lysozyme. The complex with S,N-chelating ligand was less reactive to proteins than one with O,N-chelating ligand. Species initially coordinating the proteins are most likely dehalogenated complexes. During the time, vivid ligand exchange of non-arene organic ligand L with CO32- and OH- takes place after initial formation of protein adducts. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could be expected generating different intermediate protein species. 

Conclusions. Protein reactivity toward Ru(II) complexes is determined by protein structure and ligands in Ru(II) coordination sphere, but this reactivity should be described from both kinetics, as well as stability aspect. In extracellular or intracellular milieu, ability of metal binding ligands (such as carbonate ions) to bind and to leave, determinate both the extent and mechanism of the binding of ruthenium complexes to the target biomacromolecules for cancer therapy.",
publisher = "Faculty of Sciences, University of Novi Sad, Serbian Proteomics Assosication",
journal = "V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad, Serbia, 31st May, 2019. In: The Book of Abstracts",
title = "Lysozyme and Cytochrome C adducts of ruthenium(II)-cymene complexes",
pages = "P2-P2",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6038"
}

Radomirović, M. Ž., Stanić-Vučinić, D., Nikolić, S., Mihailović, J., Ćirković-Veličković, T.,& Grgurić Šipka, S.. (2019). Lysozyme and Cytochrome C adducts of ruthenium(II)-cymene complexes. in V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad, Serbia, 31st May, 2019. In: The Book of Abstracts
Faculty of Sciences., P2-P2.
https://hdl.handle.net/21.15107/rcub_cherry_6038

Radomirović MŽ, Stanić-Vučinić D, Nikolić S, Mihailović J, Ćirković-Veličković T, Grgurić Šipka S. Lysozyme and Cytochrome C adducts of ruthenium(II)-cymene complexes. in V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad, Serbia, 31st May, 2019. In: The Book of Abstracts. 2019;:P2-P2.
https://hdl.handle.net/21.15107/rcub_cherry_6038 .

Radomirović, Mirjana Ž., Stanić-Vučinić, Dragana, Nikolić, Stefan, Mihailović, Jelena, Ćirković-Veličković, Tanja, Grgurić Šipka, Sanja, "Lysozyme and Cytochrome C adducts of ruthenium(II)-cymene complexes" in V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad, Serbia, 31st May, 2019. In: The Book of Abstracts (2019):P2-P2,
https://hdl.handle.net/21.15107/rcub_cherry_6038 .

TY  - CONF
AU  - Peruško, Marija
AU  - Apostolović, Danijela
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - van Hage, Marianne
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3735
AB  - Novel insights into the allergenic relationship between red meat and bovine milk
Marija Perusko1, Danijela Apostolovic2, Maria Starkhammar3, Tanja Cirkovic Velickovic4,5,6,7, Marianne van Hage2
1Innovation Center of the Faculty of Chemistry, Belgrade, Serbia
2Department of Medicine, Solna, Immunology and Allergy Unit, Karolinska Institutet and University Hospital, Stockholm, Sweden
3Department of Internal Medicine, Sodersjukhuset, Stockholm, Sweden
4Serbian Academy of Sciences and Arts, Belgrade, Serbia
5Center of Excellence for Molecular Food Sciences & Department of Biochemistry, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia
6Ghent University Global Campus, Yeonsu-gu, Incheon, South Korea
7Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium
 
Background
Red meat allergy is a severe form of food allergy with delayed symptoms including anaphylaxis where the IgE antibodies are directed against a carbohydrate epitope, galactose-α-1,3-galactose (α-Gal). Many red meat allergic patients report allergic symptoms upon consumption of milk or dairy products. The aim of the project was to investigate the allergenic relationship between bovine milk and red meat at a molecular level.
Methods
Adults with diagnosed red meat allergy (n = 27) were recruited and their specific IgE levels to α-Gal, beef and milk were analyzed by ImmunoCAP. Milk proteins were assayed by immunoblot and inhibition ELISA for the presence of the α-Gal epitope and for the binding to red meat allergic patients’ IgE. The involvement of the carbohydrate epitope in the IgE binding to milk proteins was assessed by an inhibition assay with thyroglobulin. Basophil activation test was performed with milk and milk proteins in samples from 11 red meat allergic patients and 2 controls.
Results
All patients were IgE positive to milk, but the IgE levels to milk were lower than those to α-Gal or beef. Significant correlations between IgE levels to milk and α-Gal (rs=0.64, P < 0.01), as well as between milk and beef (rs=0.90, P < 0.01) were observed. Immunoblot analysis of milk proteins revealed bovine γ-globulin (BGG) as α-Gal carrier. Other milk proteins, α-lactalbumin, β-lactoglobulin, α-casein, β-casein and κ-casein were negative for the presence of α-Gal epitope. BGG was also shown to bind IgE antibodies of red meat allergic patients. Inhibition immunoblot with thyroglobulin resulted in the loss of IgE binding to BGG. Additionally, ELISA experiments showed that BGG, as well as whey proteins exert a dose-dependent inhibition of red meat allergic patients’ IgE binding to -Gal. Inhibition with raw milk and commercially available milk preparations showed that raw milk exerted a slightly higher inhibition of the IgE binding to the α-Gal epitope than the commercially available milks. Importantly, activation of red meat allergic patient’s basophils by BGG and milk was demonstrated.
Conclusion
BGG was identified as a major milk carrier of the -Gal epitope that bound IgE antibodies and furthermore activated basophils of red meat allergic patients. This study highlights the importance of milk as allergenic food source among the meat allergic population.
PB  - Wiley
C3  - Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)
T1  - Novel insights into the allergenic relationship between red meat and bovine milk
VL  - 74
VL  - supp. 106
SP  - 596
EP  - 596
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3735
ER  - 

@conference{
author = "Peruško, Marija and Apostolović, Danijela and Starkhammar, Maria and Ćirković-Veličković, Tanja and van Hage, Marianne",
year = "2019",
abstract = "Novel insights into the allergenic relationship between red meat and bovine milk
Marija Perusko1, Danijela Apostolovic2, Maria Starkhammar3, Tanja Cirkovic Velickovic4,5,6,7, Marianne van Hage2
1Innovation Center of the Faculty of Chemistry, Belgrade, Serbia
2Department of Medicine, Solna, Immunology and Allergy Unit, Karolinska Institutet and University Hospital, Stockholm, Sweden
3Department of Internal Medicine, Sodersjukhuset, Stockholm, Sweden
4Serbian Academy of Sciences and Arts, Belgrade, Serbia
5Center of Excellence for Molecular Food Sciences & Department of Biochemistry, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia
6Ghent University Global Campus, Yeonsu-gu, Incheon, South Korea
7Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium
 
Background
Red meat allergy is a severe form of food allergy with delayed symptoms including anaphylaxis where the IgE antibodies are directed against a carbohydrate epitope, galactose-α-1,3-galactose (α-Gal). Many red meat allergic patients report allergic symptoms upon consumption of milk or dairy products. The aim of the project was to investigate the allergenic relationship between bovine milk and red meat at a molecular level.
Methods
Adults with diagnosed red meat allergy (n = 27) were recruited and their specific IgE levels to α-Gal, beef and milk were analyzed by ImmunoCAP. Milk proteins were assayed by immunoblot and inhibition ELISA for the presence of the α-Gal epitope and for the binding to red meat allergic patients’ IgE. The involvement of the carbohydrate epitope in the IgE binding to milk proteins was assessed by an inhibition assay with thyroglobulin. Basophil activation test was performed with milk and milk proteins in samples from 11 red meat allergic patients and 2 controls.
Results
All patients were IgE positive to milk, but the IgE levels to milk were lower than those to α-Gal or beef. Significant correlations between IgE levels to milk and α-Gal (rs=0.64, P < 0.01), as well as between milk and beef (rs=0.90, P < 0.01) were observed. Immunoblot analysis of milk proteins revealed bovine γ-globulin (BGG) as α-Gal carrier. Other milk proteins, α-lactalbumin, β-lactoglobulin, α-casein, β-casein and κ-casein were negative for the presence of α-Gal epitope. BGG was also shown to bind IgE antibodies of red meat allergic patients. Inhibition immunoblot with thyroglobulin resulted in the loss of IgE binding to BGG. Additionally, ELISA experiments showed that BGG, as well as whey proteins exert a dose-dependent inhibition of red meat allergic patients’ IgE binding to -Gal. Inhibition with raw milk and commercially available milk preparations showed that raw milk exerted a slightly higher inhibition of the IgE binding to the α-Gal epitope than the commercially available milks. Importantly, activation of red meat allergic patient’s basophils by BGG and milk was demonstrated.
Conclusion
BGG was identified as a major milk carrier of the -Gal epitope that bound IgE antibodies and furthermore activated basophils of red meat allergic patients. This study highlights the importance of milk as allergenic food source among the meat allergic population.",
publisher = "Wiley",
journal = "Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)",
title = "Novel insights into the allergenic relationship between red meat and bovine milk",
volume = "74, supp. 106",
pages = "596-596",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3735"
}

Peruško, M., Apostolović, D., Starkhammar, M., Ćirković-Veličković, T.,& van Hage, M.. (2019). Novel insights into the allergenic relationship between red meat and bovine milk. in Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)
Wiley., 74, 596-596.
https://hdl.handle.net/21.15107/rcub_cherry_3735

Peruško M, Apostolović D, Starkhammar M, Ćirković-Veličković T, van Hage M. Novel insights into the allergenic relationship between red meat and bovine milk. in Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI). 2019;74:596-596.
https://hdl.handle.net/21.15107/rcub_cherry_3735 .

Peruško, Marija, Apostolović, Danijela, Starkhammar, Maria, Ćirković-Veličković, Tanja, van Hage, Marianne, "Novel insights into the allergenic relationship between red meat and bovine milk" in Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI), 74 (2019):596-596,
https://hdl.handle.net/21.15107/rcub_cherry_3735 .

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 .

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 .

TY  - CONF
AU  - Peruško, Marija
AU  - Stevanović, Nikola
AU  - Simović, Ana
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/123456789/5126
AB  - Camel milk (CM) powders are nutritious food with many health benefits. We investigated physicochemical properties of CM proteins upon spray drying at six inlet temperatures (190°C - 250°C). Electrophoretic and spectrophotometric analysis revealed occurrence of Maillard reaction upon spray drying. Size exclusion chromatography showed increase in protein Mw and aggregates formation. Spray drying inlet temperatures exerted significant effects on the properties of CM powder proteins. Project was supported by the GA No.172024 of Ministry of Education, Science and Technological Development.
PB  - Serbian Chemical Society
C3  - 56th meeting of the Serbian chemical society, Book of Abstracts, June 7-8, 2019, Niš, Serbia
T1  - Spray drying of camel milk induces protein aggregates and Maillard reaction products formation
SP  - 73
EP  - 73
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5126
ER  - 

@conference{
author = "Peruško, Marija and Stevanović, Nikola and Simović, Ana and Radomirović, Mirjana Ž. and Stanić-Vučinić, Dragana and Ghnimi, Sami and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Camel milk (CM) powders are nutritious food with many health benefits. We investigated physicochemical properties of CM proteins upon spray drying at six inlet temperatures (190°C - 250°C). Electrophoretic and spectrophotometric analysis revealed occurrence of Maillard reaction upon spray drying. Size exclusion chromatography showed increase in protein Mw and aggregates formation. Spray drying inlet temperatures exerted significant effects on the properties of CM powder proteins. Project was supported by the GA No.172024 of Ministry of Education, Science and Technological Development.",
publisher = "Serbian Chemical Society",
journal = "56th meeting of the Serbian chemical society, Book of Abstracts, June 7-8, 2019, Niš, Serbia",
title = "Spray drying of camel milk induces protein aggregates and Maillard reaction products formation",
pages = "73-73",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5126"
}

Peruško, M., Stevanović, N., Simović, A., Radomirović, M. Ž., Stanić-Vučinić, D., Ghnimi, S.,& Ćirković-Veličković, T.. (2019). Spray drying of camel milk induces protein aggregates and Maillard reaction products formation. in 56th meeting of the Serbian chemical society, Book of Abstracts, June 7-8, 2019, Niš, Serbia
Serbian Chemical Society., 73-73.
https://hdl.handle.net/21.15107/rcub_cherry_5126

Peruško M, Stevanović N, Simović A, Radomirović MŽ, Stanić-Vučinić D, Ghnimi S, Ćirković-Veličković T. Spray drying of camel milk induces protein aggregates and Maillard reaction products formation. in 56th meeting of the Serbian chemical society, Book of Abstracts, June 7-8, 2019, Niš, Serbia. 2019;:73-73.
https://hdl.handle.net/21.15107/rcub_cherry_5126 .

Peruško, Marija, Stevanović, Nikola, Simović, Ana, Radomirović, Mirjana Ž., Stanić-Vučinić, Dragana, Ghnimi, Sami, Ćirković-Veličković, Tanja, "Spray drying of camel milk induces protein aggregates and Maillard reaction products formation" in 56th meeting of the Serbian chemical society, Book of Abstracts, June 7-8, 2019, Niš, Serbia (2019):73-73,
https://hdl.handle.net/21.15107/rcub_cherry_5126 .

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 . .

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 . .

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 . .