TY  - PAT
AU  - Andjelković, Uroš
AU  - Sladić, Dušan
AU  - Vukasinović, Ivana
AU  - Lah, Jurij
AU  - Fonovic, Marko
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6941
AB  - The present invention relates to a novel polypeptide which displays specific carbohydrate binding activity, particularly against glycans that contain mannose, and in vivo and ex vivo methods of use thereof. Methods of use comprise administering a polypeptide of the invention, for example to a sample or a subject in which carbohydrate is present, under conditions suitable for the polypeptide to bind the carbohydrate. The carbohydrate may be expressed by a pathogen. The invention relates to polypeptides and compositions thereof with anti-pathogen activity, such as anti-viral, anti-bacterial, anti-fungal or anti-tumour activity. Also provided are methods for the prevention or treatment of diseases and conditions mediated by pathogens which express carbohydrate, for example as glycoproteins.
PB  - The World Intellectual Property Organization
T2  - The World Intellectual Property Organization
T1  - Carbohydrate binding polypeptide of Savalia Savaglia
IS  - WO20230552505A1
UR  - https://hdl.handle.net/21.15107/rcub_cer_6941
ER  - 

@misc{
author = "Andjelković, Uroš and Sladić, Dušan and Vukasinović, Ivana and Lah, Jurij and Fonovic, Marko",
year = "2023",
abstract = "The present invention relates to a novel polypeptide which displays specific carbohydrate binding activity, particularly against glycans that contain mannose, and in vivo and ex vivo methods of use thereof. Methods of use comprise administering a polypeptide of the invention, for example to a sample or a subject in which carbohydrate is present, under conditions suitable for the polypeptide to bind the carbohydrate. The carbohydrate may be expressed by a pathogen. The invention relates to polypeptides and compositions thereof with anti-pathogen activity, such as anti-viral, anti-bacterial, anti-fungal or anti-tumour activity. Also provided are methods for the prevention or treatment of diseases and conditions mediated by pathogens which express carbohydrate, for example as glycoproteins.",
publisher = "The World Intellectual Property Organization",
journal = "The World Intellectual Property Organization",
title = "Carbohydrate binding polypeptide of Savalia Savaglia",
number = "WO20230552505A1",
url = "https://hdl.handle.net/21.15107/rcub_cer_6941"
}

Andjelković, U., Sladić, D., Vukasinović, I., Lah, J.,& Fonovic, M.. (2023). Carbohydrate binding polypeptide of Savalia Savaglia. in The World Intellectual Property Organization
The World Intellectual Property Organization.(WO20230552505A1).
https://hdl.handle.net/21.15107/rcub_cer_6941

Andjelković U, Sladić D, Vukasinović I, Lah J, Fonovic M. Carbohydrate binding polypeptide of Savalia Savaglia. in The World Intellectual Property Organization. 2023;(WO20230552505A1).
https://hdl.handle.net/21.15107/rcub_cer_6941 .

Andjelković, Uroš, Sladić, Dušan, Vukasinović, Ivana, Lah, Jurij, Fonovic, Marko, "Carbohydrate binding polypeptide of Savalia Savaglia" in The World Intellectual Property Organization, no. WO20230552505A1 (2023),
https://hdl.handle.net/21.15107/rcub_cer_6941 .

TY  - PAT
AU  - Josić, Djuro
AU  - Begić, Marija
AU  - Andjelković, Uroš
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6940
AB  - A process for the purification of Prothrombin Complex Concentrate (PCC) from complete plasma or cryo-poor plasma using chromatography, the method comprising performing an initial sample displacement chromatography step of complete plasma or cryo-poor plasma, in particular undiluted cryo-poor plasma, on an anion exchanger to obtain a first fraction enriched in PCC.A fraction comprising PCC and factor IX obtainable by the process of the invention.
PB  - European Patent Office
T2  - European patent office
T1  - A process for the purification of prothrombin complex concentrate (PCC) and FIX from complete plasma or cryo-poor plasma
IS  - EP3945095A1
UR  - https://hdl.handle.net/21.15107/rcub_cer_6940
ER  - 

@misc{
author = "Josić, Djuro and Begić, Marija and Andjelković, Uroš",
year = "2022",
abstract = "A process for the purification of Prothrombin Complex Concentrate (PCC) from complete plasma or cryo-poor plasma using chromatography, the method comprising performing an initial sample displacement chromatography step of complete plasma or cryo-poor plasma, in particular undiluted cryo-poor plasma, on an anion exchanger to obtain a first fraction enriched in PCC.A fraction comprising PCC and factor IX obtainable by the process of the invention.",
publisher = "European Patent Office",
journal = "European patent office",
title = "A process for the purification of prothrombin complex concentrate (PCC) and FIX from complete plasma or cryo-poor plasma",
number = "EP3945095A1",
url = "https://hdl.handle.net/21.15107/rcub_cer_6940"
}

Josić, D., Begić, M.,& Andjelković, U.. (2022). A process for the purification of prothrombin complex concentrate (PCC) and FIX from complete plasma or cryo-poor plasma. in European patent office
European Patent Office.(EP3945095A1).
https://hdl.handle.net/21.15107/rcub_cer_6940

Josić D, Begić M, Andjelković U. A process for the purification of prothrombin complex concentrate (PCC) and FIX from complete plasma or cryo-poor plasma. in European patent office. 2022;(EP3945095A1).
https://hdl.handle.net/21.15107/rcub_cer_6940 .

Josić, Djuro, Begić, Marija, Andjelković, Uroš, "A process for the purification of prothrombin complex concentrate (PCC) and FIX from complete plasma or cryo-poor plasma" in European patent office, no. EP3945095A1 (2022),
https://hdl.handle.net/21.15107/rcub_cer_6940 .

TY  - CONF
AU  - Batas-Bjelić, Ilija
AU  - Anđelković, Uroš
AU  - Stojanović, Boban
AU  - Georgijević, Milosav
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5497
AB  - Energy systems of the future should enable transition to clean energy and reduction of CO2 emission. Various options are under consideration and research. One direction of development are photovoltaic, and rechargeable batteries used to store the electricity needed for vehicles and stationary systems (1,2). At the current technological level and market attractiveness among rechargeable batteries significant group are those based on lithium. EU production of raw materials for all batteries is about 1%. Growing demand for lithium are expected in 2050 to be 10-50 times higher than 2018. A lithium deficit in the market is expected (3,4). The companies are searching new locations for lithium mining and production facilities in order to compensate for the deficit.The mineral named Jadarit found in Serbia, contains lithium, sodium, boron and silica. Estimated reserves of Jadarit are of low significance for World production of lithium, but may be significant at EU level and for Serbian economy. Certain companies are interested to enter the production chain from Jadarit. These companies present the possibility for future industrial battery development in Serbia, which may lead innovative final products. They claim optimistic 3-15% increase of GDP (5). Public debate provided argumented shortcomings of currently proposed technology for lithium extraction from Jadarit (6). Major concerns are regarding permanent devastation of lush ecosystem, fertile soil, drinking water, air pollution. These non-monetary assets and their contribution to GDP should be monetized as sine qua non for objective cost-benefit analysis. Therefore, instead of polarization, public debate that identifies key critical points in technology of lithium extraction and its effects on human health and environment provides basis for future research that will develop new technologies capable to protect environment.
PB  - Belgrade : University of Belgrade - Faculty of Physical Chemistry
C3  - Contemporary batteries and supercapacitors : COIN2022 : program and book of abstracts / International Symposium Belgrade, June 1-2, 2022
T1  - Challenges in Sustainable Use of Lithium for Highly Innovative Final Products Created and Made in Serbia with EU Environmental Standards
UR  - https://hdl.handle.net/21.15107/rcub_dais_13012
ER  - 

@conference{
author = "Batas-Bjelić, Ilija and Anđelković, Uroš and Stojanović, Boban and Georgijević, Milosav",
year = "2022",
abstract = "Energy systems of the future should enable transition to clean energy and reduction of CO2 emission. Various options are under consideration and research. One direction of development are photovoltaic, and rechargeable batteries used to store the electricity needed for vehicles and stationary systems (1,2). At the current technological level and market attractiveness among rechargeable batteries significant group are those based on lithium. EU production of raw materials for all batteries is about 1%. Growing demand for lithium are expected in 2050 to be 10-50 times higher than 2018. A lithium deficit in the market is expected (3,4). The companies are searching new locations for lithium mining and production facilities in order to compensate for the deficit.The mineral named Jadarit found in Serbia, contains lithium, sodium, boron and silica. Estimated reserves of Jadarit are of low significance for World production of lithium, but may be significant at EU level and for Serbian economy. Certain companies are interested to enter the production chain from Jadarit. These companies present the possibility for future industrial battery development in Serbia, which may lead innovative final products. They claim optimistic 3-15% increase of GDP (5). Public debate provided argumented shortcomings of currently proposed technology for lithium extraction from Jadarit (6). Major concerns are regarding permanent devastation of lush ecosystem, fertile soil, drinking water, air pollution. These non-monetary assets and their contribution to GDP should be monetized as sine qua non for objective cost-benefit analysis. Therefore, instead of polarization, public debate that identifies key critical points in technology of lithium extraction and its effects on human health and environment provides basis for future research that will develop new technologies capable to protect environment.",
publisher = "Belgrade : University of Belgrade - Faculty of Physical Chemistry",
journal = "Contemporary batteries and supercapacitors : COIN2022 : program and book of abstracts / International Symposium Belgrade, June 1-2, 2022",
title = "Challenges in Sustainable Use of Lithium for Highly Innovative Final Products Created and Made in Serbia with EU Environmental Standards",
url = "https://hdl.handle.net/21.15107/rcub_dais_13012"
}

Batas-Bjelić, I., Anđelković, U., Stojanović, B.,& Georgijević, M.. (2022). Challenges in Sustainable Use of Lithium for Highly Innovative Final Products Created and Made in Serbia with EU Environmental Standards. in Contemporary batteries and supercapacitors : COIN2022 : program and book of abstracts / International Symposium Belgrade, June 1-2, 2022
Belgrade : University of Belgrade - Faculty of Physical Chemistry..
https://hdl.handle.net/21.15107/rcub_dais_13012

Batas-Bjelić I, Anđelković U, Stojanović B, Georgijević M. Challenges in Sustainable Use of Lithium for Highly Innovative Final Products Created and Made in Serbia with EU Environmental Standards. in Contemporary batteries and supercapacitors : COIN2022 : program and book of abstracts / International Symposium Belgrade, June 1-2, 2022. 2022;.
https://hdl.handle.net/21.15107/rcub_dais_13012 .

Batas-Bjelić, Ilija, Anđelković, Uroš, Stojanović, Boban, Georgijević, Milosav, "Challenges in Sustainable Use of Lithium for Highly Innovative Final Products Created and Made in Serbia with EU Environmental Standards" in Contemporary batteries and supercapacitors : COIN2022 : program and book of abstracts / International Symposium Belgrade, June 1-2, 2022 (2022),
https://hdl.handle.net/21.15107/rcub_dais_13012 .

TY  - CONF
AU  - Batas-Bjelić, Ilija
AU  - Anđelković, Uroš
AU  - Stojanović, Boban
AU  - Georgijević, Milosav
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5498
AB  - Energy systems of the future should enable transition to clean energy and reduction of CO2 emission. Various options are under consideration and research. One direction of development are photovoltaic, and rechargeable batteries used to store the electricity needed for vehicles and stationary systems (1,2). At the current technological level and market attractiveness among rechargeable batteries significant group are those based on lithium. EU production of raw materials for all batteries is about 1%. Growing demand for lithium are expected in 2050 to be 10-50 times higher than 2018. A lithium deficit in the market is expected (3,4). The companies are searching new locations for lithium mining and production facilities in order to compensate for the deficit.The mineral named Jadarit found in Serbia, contains lithium, sodium, boron and silica. Estimated reserves of Jadarit are of low significance for World production of lithium, but may be significant at EU level and for Serbian economy. Certain companies are interested to enter the production chain from Jadarit. These companies present the possibility for future industrial battery development in Serbia, which may lead innovative final products. They claim optimistic 3-15% increase of GDP (5). Public debate provided argumented shortcomings of currently proposed technology for lithium extraction from Jadarit (6). Major concerns are regarding permanent devastation of lush ecosystem, fertile soil, drinking water, air pollution. These non-monetary assets and their contribution to GDP should be monetized as sine qua non for objective cost-benefit analysis. Therefore, instead of polarization, public debate that identifies key critical points in technology of lithium extraction and its effects on human health and environment provides basis for future research that will develop new technologies capable to protect environment.
T1  - Challenges in Sustainable Use of Lithium for Highly Innovative Final Products Created and Made in Serbia with EU Environmental Standards
UR  - https://hdl.handle.net/21.15107/rcub_cer_5498
ER  - 

@conference{
author = "Batas-Bjelić, Ilija and Anđelković, Uroš and Stojanović, Boban and Georgijević, Milosav",
year = "2022",
abstract = "Energy systems of the future should enable transition to clean energy and reduction of CO2 emission. Various options are under consideration and research. One direction of development are photovoltaic, and rechargeable batteries used to store the electricity needed for vehicles and stationary systems (1,2). At the current technological level and market attractiveness among rechargeable batteries significant group are those based on lithium. EU production of raw materials for all batteries is about 1%. Growing demand for lithium are expected in 2050 to be 10-50 times higher than 2018. A lithium deficit in the market is expected (3,4). The companies are searching new locations for lithium mining and production facilities in order to compensate for the deficit.The mineral named Jadarit found in Serbia, contains lithium, sodium, boron and silica. Estimated reserves of Jadarit are of low significance for World production of lithium, but may be significant at EU level and for Serbian economy. Certain companies are interested to enter the production chain from Jadarit. These companies present the possibility for future industrial battery development in Serbia, which may lead innovative final products. They claim optimistic 3-15% increase of GDP (5). Public debate provided argumented shortcomings of currently proposed technology for lithium extraction from Jadarit (6). Major concerns are regarding permanent devastation of lush ecosystem, fertile soil, drinking water, air pollution. These non-monetary assets and their contribution to GDP should be monetized as sine qua non for objective cost-benefit analysis. Therefore, instead of polarization, public debate that identifies key critical points in technology of lithium extraction and its effects on human health and environment provides basis for future research that will develop new technologies capable to protect environment.",
title = "Challenges in Sustainable Use of Lithium for Highly Innovative Final Products Created and Made in Serbia with EU Environmental Standards",
url = "https://hdl.handle.net/21.15107/rcub_cer_5498"
}

Batas-Bjelić, I., Anđelković, U., Stojanović, B.,& Georgijević, M.. (2022). Challenges in Sustainable Use of Lithium for Highly Innovative Final Products Created and Made in Serbia with EU Environmental Standards. .
https://hdl.handle.net/21.15107/rcub_cer_5498

Batas-Bjelić I, Anđelković U, Stojanović B, Georgijević M. Challenges in Sustainable Use of Lithium for Highly Innovative Final Products Created and Made in Serbia with EU Environmental Standards. 2022;.
https://hdl.handle.net/21.15107/rcub_cer_5498 .

Batas-Bjelić, Ilija, Anđelković, Uroš, Stojanović, Boban, Georgijević, Milosav, "Challenges in Sustainable Use of Lithium for Highly Innovative Final Products Created and Made in Serbia with EU Environmental Standards" (2022),
https://hdl.handle.net/21.15107/rcub_cer_5498 .

TY  - JOUR
AU  - Lopandić, Zorana
AU  - Dragačević, Luka
AU  - Popović, Dragan M.
AU  - Anđelković, Uroš
AU  - Minić, Rajna
AU  - Gavrović-Jankulović, Marija
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4629
AB  - Fluorescently labeled lectins are useful tools for in vivo and in vitro studies of the structure and function of tissues and various pathogens such as viruses, bacteria, and fungi. For the evaluation of high-mannose glycans present on various glycoproteins, a three-dimensional (3D) model of the chimera was designed from the crystal structures of recombinant banana lectin (BanLec, Protein Data Bank entry (PDB): 5EXG) and an enhanced green fluorescent protein (eGFP, PDB 4EUL) by applying molecular modeling and molecular mechanics and expressed in Escherichia coli. BanLec-eGFP, produced as a soluble cytosolic protein of about 42 kDa, revealed β-sheets (41%) as the predominant secondary structures, with the emission peak maximum detected at 509 nm (excitation wavelength 488 nm). More than 65% of the primary structure was confirmed by mass spectrometry. Competitive BanLec-eGFP binding to high mannose glycans of the influenza vaccine (Vaxigrip®) was shown in a fluorescence-linked lectin sorbent assay (FLLSA) with monosaccharides (mannose and glucose) and wild type BanLec and H84T BanLec mutant. BanLec-eGFP exhibited binding to mannose residues on different strains of Salmonella in flow cytometry, with especially pronounced binding to a Salmonella Typhi clinical isolate. BanLec-eGFP can be a useful tool for screening high-mannose glycosylation sites on different microorganisms.
PB  - MDPI
T2  - Biomolecules
T1  - BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms
VL  - 11
IS  - 2
SP  - 180
DO  - 10.3390/biom11020180
ER  - 

@article{
author = "Lopandić, Zorana and Dragačević, Luka and Popović, Dragan M. and Anđelković, Uroš and Minić, Rajna and Gavrović-Jankulović, Marija",
year = "2021",
abstract = "Fluorescently labeled lectins are useful tools for in vivo and in vitro studies of the structure and function of tissues and various pathogens such as viruses, bacteria, and fungi. For the evaluation of high-mannose glycans present on various glycoproteins, a three-dimensional (3D) model of the chimera was designed from the crystal structures of recombinant banana lectin (BanLec, Protein Data Bank entry (PDB): 5EXG) and an enhanced green fluorescent protein (eGFP, PDB 4EUL) by applying molecular modeling and molecular mechanics and expressed in Escherichia coli. BanLec-eGFP, produced as a soluble cytosolic protein of about 42 kDa, revealed β-sheets (41%) as the predominant secondary structures, with the emission peak maximum detected at 509 nm (excitation wavelength 488 nm). More than 65% of the primary structure was confirmed by mass spectrometry. Competitive BanLec-eGFP binding to high mannose glycans of the influenza vaccine (Vaxigrip®) was shown in a fluorescence-linked lectin sorbent assay (FLLSA) with monosaccharides (mannose and glucose) and wild type BanLec and H84T BanLec mutant. BanLec-eGFP exhibited binding to mannose residues on different strains of Salmonella in flow cytometry, with especially pronounced binding to a Salmonella Typhi clinical isolate. BanLec-eGFP can be a useful tool for screening high-mannose glycosylation sites on different microorganisms.",
publisher = "MDPI",
journal = "Biomolecules",
title = "BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms",
volume = "11",
number = "2",
pages = "180",
doi = "10.3390/biom11020180"
}

Lopandić, Z., Dragačević, L., Popović, D. M., Anđelković, U., Minić, R.,& Gavrović-Jankulović, M.. (2021). BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms. in Biomolecules
MDPI., 11(2), 180.
https://doi.org/10.3390/biom11020180

Lopandić Z, Dragačević L, Popović DM, Anđelković U, Minić R, Gavrović-Jankulović M. BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms. in Biomolecules. 2021;11(2):180.
doi:10.3390/biom11020180 .

Lopandić, Zorana, Dragačević, Luka, Popović, Dragan M., Anđelković, Uroš, Minić, Rajna, Gavrović-Jankulović, Marija, "BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms" in Biomolecules, 11, no. 2 (2021):180,
https://doi.org/10.3390/biom11020180 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Gudelj, Ivan
AU  - Klarić, Thomas
AU  - Hinneburg, Hannes
AU  - Vinković, Marijana
AU  - Wittine, Karlo
AU  - Dovezenski, Nebojša
AU  - Vikić-Topić, Dražen
AU  - Lauc, Gordan
AU  - Vujčić, Zoran
AU  - Josić, Đuro
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3732
AB  - Invertases are glycosidases applied for synthesis of alkyl glycosides that are important and effective surfactants. Stability of invertases in the environment with increased content of organic solvent is crucial for increase of productivity of glycosidases. Their stability
is significantly influenced by N-glycosylation. However, yeast N-glycosylation pathways may synthesize plethora of N-glycan structures. A total natural crude mixture of invertase glycoforms (EINV) extracted from Saccharomyces cerevisiae was subfractionated
by anion-exchange chromatography on industrial monolithic supports to obtain different glycoforms (EINV1–EINV3). Separated glycoforms exhibited different stabilities in wateralcohol solutions that are in direct correlation with the amount of phosphate bound to N-glycans. Observed differences in stability of different invertase glycoforms were used to improve productivity of methyl β-d-fructofuranoside (MF) synthesis. The efficiency and yield of MF synthesis were improved more than 50% when the most stabile glycoform bearing the lowest amount of phosphorylated N-glycans is selected and utilized. These data underline the importance of analysis of glycan structures attached to glycoproteins, demonstrate different impact of N-glycans on the surface charge and enzyme stability in
regard to particular reaction environment, and provide a platform for improvement of yield of industrial enzymatic synthesis by chromatographic selection of glycoforms on monolithic supports.
PB  - Wiley
T2  - Electrophoresis
T1  - Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase
VL  - 42
IS  - 24
SP  - 2626
EP  - 2636
DO  - 10.1002/elps.202000092
ER  - 

@article{
author = "Anđelković, Uroš and Gudelj, Ivan and Klarić, Thomas and Hinneburg, Hannes and Vinković, Marijana and Wittine, Karlo and Dovezenski, Nebojša and Vikić-Topić, Dražen and Lauc, Gordan and Vujčić, Zoran and Josić, Đuro",
year = "2021",
abstract = "Invertases are glycosidases applied for synthesis of alkyl glycosides that are important and effective surfactants. Stability of invertases in the environment with increased content of organic solvent is crucial for increase of productivity of glycosidases. Their stability
is significantly influenced by N-glycosylation. However, yeast N-glycosylation pathways may synthesize plethora of N-glycan structures. A total natural crude mixture of invertase glycoforms (EINV) extracted from Saccharomyces cerevisiae was subfractionated
by anion-exchange chromatography on industrial monolithic supports to obtain different glycoforms (EINV1–EINV3). Separated glycoforms exhibited different stabilities in wateralcohol solutions that are in direct correlation with the amount of phosphate bound to N-glycans. Observed differences in stability of different invertase glycoforms were used to improve productivity of methyl β-d-fructofuranoside (MF) synthesis. The efficiency and yield of MF synthesis were improved more than 50% when the most stabile glycoform bearing the lowest amount of phosphorylated N-glycans is selected and utilized. These data underline the importance of analysis of glycan structures attached to glycoproteins, demonstrate different impact of N-glycans on the surface charge and enzyme stability in
regard to particular reaction environment, and provide a platform for improvement of yield of industrial enzymatic synthesis by chromatographic selection of glycoforms on monolithic supports.",
publisher = "Wiley",
journal = "Electrophoresis",
title = "Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase",
volume = "42",
number = "24",
pages = "2626-2636",
doi = "10.1002/elps.202000092"
}

Anđelković, U., Gudelj, I., Klarić, T., Hinneburg, H., Vinković, M., Wittine, K., Dovezenski, N., Vikić-Topić, D., Lauc, G., Vujčić, Z.,& Josić, Đ.. (2021). Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase. in Electrophoresis
Wiley., 42(24), 2626-2636.
https://doi.org/10.1002/elps.202000092

Anđelković U, Gudelj I, Klarić T, Hinneburg H, Vinković M, Wittine K, Dovezenski N, Vikić-Topić D, Lauc G, Vujčić Z, Josić Đ. Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase. in Electrophoresis. 2021;42(24):2626-2636.
doi:10.1002/elps.202000092 .

Anđelković, Uroš, Gudelj, Ivan, Klarić, Thomas, Hinneburg, Hannes, Vinković, Marijana, Wittine, Karlo, Dovezenski, Nebojša, Vikić-Topić, Dražen, Lauc, Gordan, Vujčić, Zoran, Josić, Đuro, "Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase" in Electrophoresis, 42, no. 24 (2021):2626-2636,
https://doi.org/10.1002/elps.202000092 . .

TY  - CHAP
AU  - Anđelković, Uroš
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4231
AB  - Food carries risks. Food allergies are risk that comes from certain food proteins (food allergens). These are natural constituents of food that can provokes life threatening conditions in significant part of population. With this chapter attempt is made to introduce basic data about food allergies and allergens. Focused to the question what makes a food protein an allergen, properties of certain allergens from dominant food allergen families are presented. Those parts of allergen molecule structure responsible for interactions with components of immune system are described. These information are important for understanding molecular mechanisms of allergy, assessment of risks, quality and safety control, and finding a best way for treatment and cure. Some of methods for prediction of allergenicity of food proteins emerged from the current knowledge are described. Food processing methods as a source of potential for increase or reduction of food allergenicity are listed in brief. Most promising strategies for treatment of food allergies are explained.
PB  - Elsevier
T2  - Comprehensive Foodomics
T1  - Food Allergy & Food Allergens
VL  - 3
SP  - 157
EP  - 174
DO  - 10.1016/B978-0-08-100596-5.22844-8
ER  - 

@inbook{
author = "Anđelković, Uroš",
year = "2021",
abstract = "Food carries risks. Food allergies are risk that comes from certain food proteins (food allergens). These are natural constituents of food that can provokes life threatening conditions in significant part of population. With this chapter attempt is made to introduce basic data about food allergies and allergens. Focused to the question what makes a food protein an allergen, properties of certain allergens from dominant food allergen families are presented. Those parts of allergen molecule structure responsible for interactions with components of immune system are described. These information are important for understanding molecular mechanisms of allergy, assessment of risks, quality and safety control, and finding a best way for treatment and cure. Some of methods for prediction of allergenicity of food proteins emerged from the current knowledge are described. Food processing methods as a source of potential for increase or reduction of food allergenicity are listed in brief. Most promising strategies for treatment of food allergies are explained.",
publisher = "Elsevier",
journal = "Comprehensive Foodomics",
booktitle = "Food Allergy & Food Allergens",
volume = "3",
pages = "157-174",
doi = "10.1016/B978-0-08-100596-5.22844-8"
}

Anđelković, U.. (2021). Food Allergy & Food Allergens. in Comprehensive Foodomics
Elsevier., 3, 157-174.
https://doi.org/10.1016/B978-0-08-100596-5.22844-8

Anđelković U. Food Allergy & Food Allergens. in Comprehensive Foodomics. 2021;3:157-174.
doi:10.1016/B978-0-08-100596-5.22844-8 .

Anđelković, Uroš, "Food Allergy & Food Allergens" in Comprehensive Foodomics, 3 (2021):157-174,
https://doi.org/10.1016/B978-0-08-100596-5.22844-8 . .

TY  - JOUR
AU  - Srajer-Gajdošik, Martina
AU  - Anđelković, Uroš
AU  - Gašo Sokač, Dajana
AU  - Pavlović, Hrvoje
AU  - Shevchuk, Olga
AU  - Martinović, Tamara
AU  - Clifton, James
AU  - Begić, Marija
AU  - Josić, Djuro
PY  - 2020
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6923
AB  - Proteomic analysis of foodborne pathogen Listeria monocytogenes after treatment with three disinfectants based on ammonium salts of pyridoxal oxime (POD) reveal perturbation of cellular processes. These inhibitors caused disturbance in the synthesis of plasma membrane proteins and cell wall proteoglycans. Some of key proteins and proteoglycans from these two groups that are important for bacterial growth are down-regulated. Additionally, we demonstrated that the main bacterial toxin Listeriolysin O (LLO) is significantly down-regulated after treatment with each of three investigated inhibitors. These investigations confirm already postulated mechanism of action of POD-based inhibitors that results in disturbance of key cell surface proteins and proteoglycans in Gram-positive bacteria. Additionally, the use of some proteins such as LLO, as potential biomarker candidates of food poisoning with this bacterium is discussed.
PB  - Elsevier
T2  - Food Research International
T1  - Proteomic analysis of pyridoxal oxime derivatives treated Listeria monocytogenes reveals down-regulation of the main virulence factor, Listeriolysin O
VL  - 131
SP  - 108951
DO  - 10.1016/j.foodres.2019.108951
ER  - 

@article{
author = "Srajer-Gajdošik, Martina and Anđelković, Uroš and Gašo Sokač, Dajana and Pavlović, Hrvoje and Shevchuk, Olga and Martinović, Tamara and Clifton, James and Begić, Marija and Josić, Djuro",
year = "2020",
abstract = "Proteomic analysis of foodborne pathogen Listeria monocytogenes after treatment with three disinfectants based on ammonium salts of pyridoxal oxime (POD) reveal perturbation of cellular processes. These inhibitors caused disturbance in the synthesis of plasma membrane proteins and cell wall proteoglycans. Some of key proteins and proteoglycans from these two groups that are important for bacterial growth are down-regulated. Additionally, we demonstrated that the main bacterial toxin Listeriolysin O (LLO) is significantly down-regulated after treatment with each of three investigated inhibitors. These investigations confirm already postulated mechanism of action of POD-based inhibitors that results in disturbance of key cell surface proteins and proteoglycans in Gram-positive bacteria. Additionally, the use of some proteins such as LLO, as potential biomarker candidates of food poisoning with this bacterium is discussed.",
publisher = "Elsevier",
journal = "Food Research International",
title = "Proteomic analysis of pyridoxal oxime derivatives treated Listeria monocytogenes reveals down-regulation of the main virulence factor, Listeriolysin O",
volume = "131",
pages = "108951",
doi = "10.1016/j.foodres.2019.108951"
}

Srajer-Gajdošik, M., Anđelković, U., Gašo Sokač, D., Pavlović, H., Shevchuk, O., Martinović, T., Clifton, J., Begić, M.,& Josić, D.. (2020). Proteomic analysis of pyridoxal oxime derivatives treated Listeria monocytogenes reveals down-regulation of the main virulence factor, Listeriolysin O. in Food Research International
Elsevier., 131, 108951.
https://doi.org/10.1016/j.foodres.2019.108951

Srajer-Gajdošik M, Anđelković U, Gašo Sokač D, Pavlović H, Shevchuk O, Martinović T, Clifton J, Begić M, Josić D. Proteomic analysis of pyridoxal oxime derivatives treated Listeria monocytogenes reveals down-regulation of the main virulence factor, Listeriolysin O. in Food Research International. 2020;131:108951.
doi:10.1016/j.foodres.2019.108951 .

Srajer-Gajdošik, Martina, Anđelković, Uroš, Gašo Sokač, Dajana, Pavlović, Hrvoje, Shevchuk, Olga, Martinović, Tamara, Clifton, James, Begić, Marija, Josić, Djuro, "Proteomic analysis of pyridoxal oxime derivatives treated Listeria monocytogenes reveals down-regulation of the main virulence factor, Listeriolysin O" in Food Research International, 131 (2020):108951,
https://doi.org/10.1016/j.foodres.2019.108951 . .

TY  - JOUR
AU  - Wittine, Karlo
AU  - Antolović, Roberto
AU  - Jelić, Dubravko
AU  - Bracanović, Sara
AU  - Cetina, Mario
AU  - Anđelković, Uroš
AU  - Wittine, Ozren
AU  - Kraljević Pavelić, Sandra
AU  - Vinter, Adrijana
PY  - 2020
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3614
AB  - Furanocoumarins, particularly furo[3,2-c]coumarins, are found in many natural products. However, coumarins
annulated to a thiophene ring have received scarce attention to date in the literature. Therefore, we synthesized
4-oxo-4H-thieno[3,2-c]chromene derivatives and tested in vitro their anti-inflammatory activity. Anti-inflammatory
potential of the synthesized compounds (1, 2, 6–8, 9a–e and 10a–c) has been evaluated by measuring
various pSTAT (signal transducer and activator of transcription) inhibition within the JAK (Janus-activated
family kinase)/STAT signaling pathway. Ethyl 7-hydroxy-4-oxo-4H-thieno[3,2-c]chromene-2-carboxylate
(7) showed best inhibition properties on pSTAT5 in GM-CSF (Granulocyte-macrophage colony-stimulating
factor)-triggered PBMC assay, with IC50 value of 5.0 μM.
PB  - Elsevier
T2  - Bioorganic & Medicinal Chemistry Letters
T1  - Thienochromene derivatives inhibit pSTAT1 and pSTAT5 signaling induced by cytokines
VL  - 30
IS  - 18
SP  - 127415
DO  - 10.1016/j.bmcl.2020.127415
ER  - 

@article{
author = "Wittine, Karlo and Antolović, Roberto and Jelić, Dubravko and Bracanović, Sara and Cetina, Mario and Anđelković, Uroš and Wittine, Ozren and Kraljević Pavelić, Sandra and Vinter, Adrijana",
year = "2020",
abstract = "Furanocoumarins, particularly furo[3,2-c]coumarins, are found in many natural products. However, coumarins
annulated to a thiophene ring have received scarce attention to date in the literature. Therefore, we synthesized
4-oxo-4H-thieno[3,2-c]chromene derivatives and tested in vitro their anti-inflammatory activity. Anti-inflammatory
potential of the synthesized compounds (1, 2, 6–8, 9a–e and 10a–c) has been evaluated by measuring
various pSTAT (signal transducer and activator of transcription) inhibition within the JAK (Janus-activated
family kinase)/STAT signaling pathway. Ethyl 7-hydroxy-4-oxo-4H-thieno[3,2-c]chromene-2-carboxylate
(7) showed best inhibition properties on pSTAT5 in GM-CSF (Granulocyte-macrophage colony-stimulating
factor)-triggered PBMC assay, with IC50 value of 5.0 μM.",
publisher = "Elsevier",
journal = "Bioorganic & Medicinal Chemistry Letters",
title = "Thienochromene derivatives inhibit pSTAT1 and pSTAT5 signaling induced by cytokines",
volume = "30",
number = "18",
pages = "127415",
doi = "10.1016/j.bmcl.2020.127415"
}

Wittine, K., Antolović, R., Jelić, D., Bracanović, S., Cetina, M., Anđelković, U., Wittine, O., Kraljević Pavelić, S.,& Vinter, A.. (2020). Thienochromene derivatives inhibit pSTAT1 and pSTAT5 signaling induced by cytokines. in Bioorganic & Medicinal Chemistry Letters
Elsevier., 30(18), 127415.
https://doi.org/10.1016/j.bmcl.2020.127415

Wittine K, Antolović R, Jelić D, Bracanović S, Cetina M, Anđelković U, Wittine O, Kraljević Pavelić S, Vinter A. Thienochromene derivatives inhibit pSTAT1 and pSTAT5 signaling induced by cytokines. in Bioorganic & Medicinal Chemistry Letters. 2020;30(18):127415.
doi:10.1016/j.bmcl.2020.127415 .

Wittine, Karlo, Antolović, Roberto, Jelić, Dubravko, Bracanović, Sara, Cetina, Mario, Anđelković, Uroš, Wittine, Ozren, Kraljević Pavelić, Sandra, Vinter, Adrijana, "Thienochromene derivatives inhibit pSTAT1 and pSTAT5 signaling induced by cytokines" in Bioorganic & Medicinal Chemistry Letters, 30, no. 18 (2020):127415,
https://doi.org/10.1016/j.bmcl.2020.127415 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Gudelj, Ivan
AU  - Klarić, Thomas
AU  - Hinneburg, Hannes
AU  - Vinković, Marijana
AU  - Wittine, Karlo
AU  - Dovezenski, Nebojša
AU  - Vikić-Topić, Dražen
AU  - Lauc, Gordan
AU  - Vujčić, Zoran
AU  - Josić, Đuro
PY  - 2020
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3989
AB  - Invertases are glycosidases applied for synthesis of alkyl glycosides that are important and effective surfactants. Stability of invertases in the environment with increased content of organic solvent is crucial for increase of productivity of glycosidases. Their stabilityis significantly influenced by N-glycosylation. However, yeast N-glycosylation pathways may synthesize plethora of N-glycan structures. A total natural crude mixture of invertase glycoforms (EINV) extracted from Saccharomyces cerevisiae was subfractionatedby anion-exchange chromatography on industrial monolithic supports to obtain different glycoforms (EINV1–EINV3). Separated glycoforms exhibited different stabilities in wateralcohol solutions that are in direct correlation with the amount of phosphate bound to N-glycans. Observed differences in stability of different invertase glycoforms were used to improve productivity of methyl β-d-fructofuranoside (MF) synthesis. The efficiency and yield of MF synthesis were improved more than 50% when the most stabile glycoform bearing the lowest amount of phosphorylated N-glycans is selected and utilized. These data underline the importance of analysis of glycan structures attached to glycoproteins, demonstrate different impact of N-glycans on the surface charge and enzyme stability inregard to particular reaction environment, and provide a platform for improvement of yield of industrial enzymatic synthesis by chromatographic selection of glycoforms on monolithic supports.
PB  - Wiley
T2  - Electrophoresis
T1  - Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase
DO  - 10.1002/elps.202000092
ER  - 

@article{
author = "Anđelković, Uroš and Gudelj, Ivan and Klarić, Thomas and Hinneburg, Hannes and Vinković, Marijana and Wittine, Karlo and Dovezenski, Nebojša and Vikić-Topić, Dražen and Lauc, Gordan and Vujčić, Zoran and Josić, Đuro",
year = "2020",
abstract = "Invertases are glycosidases applied for synthesis of alkyl glycosides that are important and effective surfactants. Stability of invertases in the environment with increased content of organic solvent is crucial for increase of productivity of glycosidases. Their stabilityis significantly influenced by N-glycosylation. However, yeast N-glycosylation pathways may synthesize plethora of N-glycan structures. A total natural crude mixture of invertase glycoforms (EINV) extracted from Saccharomyces cerevisiae was subfractionatedby anion-exchange chromatography on industrial monolithic supports to obtain different glycoforms (EINV1–EINV3). Separated glycoforms exhibited different stabilities in wateralcohol solutions that are in direct correlation with the amount of phosphate bound to N-glycans. Observed differences in stability of different invertase glycoforms were used to improve productivity of methyl β-d-fructofuranoside (MF) synthesis. The efficiency and yield of MF synthesis were improved more than 50% when the most stabile glycoform bearing the lowest amount of phosphorylated N-glycans is selected and utilized. These data underline the importance of analysis of glycan structures attached to glycoproteins, demonstrate different impact of N-glycans on the surface charge and enzyme stability inregard to particular reaction environment, and provide a platform for improvement of yield of industrial enzymatic synthesis by chromatographic selection of glycoforms on monolithic supports.",
publisher = "Wiley",
journal = "Electrophoresis",
title = "Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase",
doi = "10.1002/elps.202000092"
}

Anđelković, U., Gudelj, I., Klarić, T., Hinneburg, H., Vinković, M., Wittine, K., Dovezenski, N., Vikić-Topić, D., Lauc, G., Vujčić, Z.,& Josić, Đ.. (2020). Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase. in Electrophoresis
Wiley..
https://doi.org/10.1002/elps.202000092

Anđelković U, Gudelj I, Klarić T, Hinneburg H, Vinković M, Wittine K, Dovezenski N, Vikić-Topić D, Lauc G, Vujčić Z, Josić Đ. Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase. in Electrophoresis. 2020;.
doi:10.1002/elps.202000092 .

Anđelković, Uroš, Gudelj, Ivan, Klarić, Thomas, Hinneburg, Hannes, Vinković, Marijana, Wittine, Karlo, Dovezenski, Nebojša, Vikić-Topić, Dražen, Lauc, Gordan, Vujčić, Zoran, Josić, Đuro, "Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase" in Electrophoresis (2020),
https://doi.org/10.1002/elps.202000092 . .

TY  - CONF
AU  - Andjelković, Uroš
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7526
AB  - Alergije izazvane pojedinim proteinima hrane pogađaju 2-4% populacije zapadnog sveta i predstavlјaju značajan socio-ekonomski problem. Dodatno, biotehnološki pristupi fokusirani na podmirivanje rastućih zahteva za hranom, kao što je genetički inženjering ili nove metode obrade hrane, uvode u lanac ishrane nove proteine ili njihove proteoforme koji su potencijalni alergeni. Koncept-omiks pristupa u analizi hrane, fudomiks, ima za cilј pobolјšanje dobrobiti, zdravlјa i pouzdanosti potrošača primenom naprednih tehnologija. Jedna od njih, trenutno najbrže rastuća, je tandemska masena spektrometrija (MS) spregnuta sa tečnom hromatografijom. Maseni spektrometri su kompleksni analitički uređaji kojima je moguće identifikovati i kvantifikovati pojedinačne alergene hrane prisutne u niskim, ali biološki bitnim, koncentracijama. Analitičke mogućnosti pojedinačnih masenih spektrometara zavise od tipa masenog spektrometra i obučenosti osoblјa. Primena MS metoda kontrole alergena u hrani podrazumeva uzorkovanje hrane, pripremu uzorka, snimanje masenih spektara i bioinformatičku analizu masenih spektara. Većina MS metoda za kontrolu prisutnosti proteinskih alergena u hrani zasniva sa na proteolizi uzorka i cilјanom prikuplјanju masenih spektara praćenjem selektovanih reakcija. Razvoj ovih MS metoda zahteva precizno poznavanje strukture alergena i njihovih posttranslacionih modifikacija (uklјučujući i one nastale u procesu obrade hrane), dizajn standarda za kvantifikaciju, optimizaciju uzorkovanja i pripreme uzoraka za pojedinačne vrste namirnica i tip njihove pripreme kao i detalјnu validaciju metode. Novi kvantitativni pristupi, kao što je paralelno praćenje reakcija, razvijeni na masenim spektrometrima ultra-visoke rezoulcije bitno olakšavaju razvoj MS metoda. Tokom poslednjih 20 godina MS je postala nazaobilazna tehnologija u određivanju strukture proteinskih alergena hrane, identifikaciji novih, proceni njihovog alergenog potencijala (npr. profilisanje peptida vezanih za glavni kompleks histokompatibilnosti dendritičnih ćelija nakon izlaganja alergenu), kao i istraživanjima bioloških mehanizama alergenosti. Dva su glavna pristupa u ovim istraživanjima, analiza na nivou intaktnih proteina i analiza peptida generisanih specifičnom proteolizom proteoma. U ovom drugom pristupu, danas dominantnom, razvijen je niz metoda prikuplјanja masenih spektara (klasifikovanih kao zavisne, cilјane i nezavisne) kako bi se približili analizi kompleksnosti proteoma neophodnoj za razumevanje bioloških procesa kao što su i alergijske reakcije.
AB  - Food allergy caused by certain food proteins affects 2-4% of population in the western world and they represent important socio-economic problem. Additionally, biotechnological approaches focused to meet growing demands for food, such as genetic engineering or new food processing technologies, introduce into the food chain new proteins or their proteoforms which are potential allergens. Concept of –omics approach in food analysis, foodomics, aims to improve consumer’s well-being, health, and confidence by implementation of advanced technologies. One such, currently fastest growing, is tandem mass spectrometry (MS) coupled to liquid chromatography. Mass spectrometers are complex analytical devices that enable identification and quantification of individual food allergens present in small, but biologically relevant, concentrations. Analytical capabilities of individual mass spectrometers depend on the type of mass spectrometer and skills of analyst. Application of MS in control of food allergens includes sampling, sample preparation, acquisition of mass spectra and bioinformatics analysis of mass spectra. The majority of MS methods for control of food allergens are based on bottom-up approach with targeted selected reaction monitoring acquisition. Development of these MS methods requires detailed knowledge of allergen structure, its posttranslational modifications (including those arose during food processing), design of quantification standards, optimization of sampling and sample preparation for individual type of food and food processing, as well as thorough method validation. The new approaches, such as parallel reaction monitoring, developed on ultra-high resolution mass spectrometers substantially facilitate development of MS methods. Over last 20 years MS become the main technology for determination of the structure of food allergens, identification of new allergens, assessment of their allergenic potential (e.g. profiling of peptides incorporated into MHC of dendritic cells after exposure to individual allergen), and research of biological mechanisms of allergy. Two main approaches are analysis at the level of intact proteins (top down) and analysis of peptides generated by specific proteolysis of proteome (bottom-up). In the second one, that is currently dominant, a range of methods are developed for acquisition of mass spectra (data dependent, targeted and data independent) in order to approach high complexity of proteome which is a prerequisite for understanding of complex biological processes including allergies.
PB  - Belgrade : University of Belgrade
C3  - Unifood Conference, Program i zbornik radova, Beograd, 5 i 6 oktobar 2018. / Unifood Conference, Programme & Book of Abstracts, Belgrade Octobre 5-6 2018
T1  - Masena spektrometrija kao fudomički alat za istraživanje i kontrolu proteinskih alergena hrane
T1  - Mass spectrometry as foodomics tool in research and control of food allergen proteins
SP  - PPP3 / IL3
UR  - https://hdl.handle.net/21.15107/rcub_cer_7526
ER  - 

@conference{
author = "Andjelković, Uroš",
year = "2018",
abstract = "Alergije izazvane pojedinim proteinima hrane pogađaju 2-4% populacije zapadnog sveta i predstavlјaju značajan socio-ekonomski problem. Dodatno, biotehnološki pristupi fokusirani na podmirivanje rastućih zahteva za hranom, kao što je genetički inženjering ili nove metode obrade hrane, uvode u lanac ishrane nove proteine ili njihove proteoforme koji su potencijalni alergeni. Koncept-omiks pristupa u analizi hrane, fudomiks, ima za cilј pobolјšanje dobrobiti, zdravlјa i pouzdanosti potrošača primenom naprednih tehnologija. Jedna od njih, trenutno najbrže rastuća, je tandemska masena spektrometrija (MS) spregnuta sa tečnom hromatografijom. Maseni spektrometri su kompleksni analitički uređaji kojima je moguće identifikovati i kvantifikovati pojedinačne alergene hrane prisutne u niskim, ali biološki bitnim, koncentracijama. Analitičke mogućnosti pojedinačnih masenih spektrometara zavise od tipa masenog spektrometra i obučenosti osoblјa. Primena MS metoda kontrole alergena u hrani podrazumeva uzorkovanje hrane, pripremu uzorka, snimanje masenih spektara i bioinformatičku analizu masenih spektara. Većina MS metoda za kontrolu prisutnosti proteinskih alergena u hrani zasniva sa na proteolizi uzorka i cilјanom prikuplјanju masenih spektara praćenjem selektovanih reakcija. Razvoj ovih MS metoda zahteva precizno poznavanje strukture alergena i njihovih posttranslacionih modifikacija (uklјučujući i one nastale u procesu obrade hrane), dizajn standarda za kvantifikaciju, optimizaciju uzorkovanja i pripreme uzoraka za pojedinačne vrste namirnica i tip njihove pripreme kao i detalјnu validaciju metode. Novi kvantitativni pristupi, kao što je paralelno praćenje reakcija, razvijeni na masenim spektrometrima ultra-visoke rezoulcije bitno olakšavaju razvoj MS metoda. Tokom poslednjih 20 godina MS je postala nazaobilazna tehnologija u određivanju strukture proteinskih alergena hrane, identifikaciji novih, proceni njihovog alergenog potencijala (npr. profilisanje peptida vezanih za glavni kompleks histokompatibilnosti dendritičnih ćelija nakon izlaganja alergenu), kao i istraživanjima bioloških mehanizama alergenosti. Dva su glavna pristupa u ovim istraživanjima, analiza na nivou intaktnih proteina i analiza peptida generisanih specifičnom proteolizom proteoma. U ovom drugom pristupu, danas dominantnom, razvijen je niz metoda prikuplјanja masenih spektara (klasifikovanih kao zavisne, cilјane i nezavisne) kako bi se približili analizi kompleksnosti proteoma neophodnoj za razumevanje bioloških procesa kao što su i alergijske reakcije., Food allergy caused by certain food proteins affects 2-4% of population in the western world and they represent important socio-economic problem. Additionally, biotechnological approaches focused to meet growing demands for food, such as genetic engineering or new food processing technologies, introduce into the food chain new proteins or their proteoforms which are potential allergens. Concept of –omics approach in food analysis, foodomics, aims to improve consumer’s well-being, health, and confidence by implementation of advanced technologies. One such, currently fastest growing, is tandem mass spectrometry (MS) coupled to liquid chromatography. Mass spectrometers are complex analytical devices that enable identification and quantification of individual food allergens present in small, but biologically relevant, concentrations. Analytical capabilities of individual mass spectrometers depend on the type of mass spectrometer and skills of analyst. Application of MS in control of food allergens includes sampling, sample preparation, acquisition of mass spectra and bioinformatics analysis of mass spectra. The majority of MS methods for control of food allergens are based on bottom-up approach with targeted selected reaction monitoring acquisition. Development of these MS methods requires detailed knowledge of allergen structure, its posttranslational modifications (including those arose during food processing), design of quantification standards, optimization of sampling and sample preparation for individual type of food and food processing, as well as thorough method validation. The new approaches, such as parallel reaction monitoring, developed on ultra-high resolution mass spectrometers substantially facilitate development of MS methods. Over last 20 years MS become the main technology for determination of the structure of food allergens, identification of new allergens, assessment of their allergenic potential (e.g. profiling of peptides incorporated into MHC of dendritic cells after exposure to individual allergen), and research of biological mechanisms of allergy. Two main approaches are analysis at the level of intact proteins (top down) and analysis of peptides generated by specific proteolysis of proteome (bottom-up). In the second one, that is currently dominant, a range of methods are developed for acquisition of mass spectra (data dependent, targeted and data independent) in order to approach high complexity of proteome which is a prerequisite for understanding of complex biological processes including allergies.",
publisher = "Belgrade : University of Belgrade",
journal = "Unifood Conference, Program i zbornik radova, Beograd, 5 i 6 oktobar 2018. / Unifood Conference, Programme & Book of Abstracts, Belgrade Octobre 5-6 2018",
title = "Masena spektrometrija kao fudomički alat za istraživanje i kontrolu proteinskih alergena hrane, Mass spectrometry as foodomics tool in research and control of food allergen proteins",
pages = "PPP3 / IL3",
url = "https://hdl.handle.net/21.15107/rcub_cer_7526"
}

Andjelković, U.. (2018). Masena spektrometrija kao fudomički alat za istraživanje i kontrolu proteinskih alergena hrane. in Unifood Conference, Program i zbornik radova, Beograd, 5 i 6 oktobar 2018. / Unifood Conference, Programme & Book of Abstracts, Belgrade Octobre 5-6 2018
Belgrade : University of Belgrade., PPP3 / IL3.
https://hdl.handle.net/21.15107/rcub_cer_7526

Andjelković U. Masena spektrometrija kao fudomički alat za istraživanje i kontrolu proteinskih alergena hrane. in Unifood Conference, Program i zbornik radova, Beograd, 5 i 6 oktobar 2018. / Unifood Conference, Programme & Book of Abstracts, Belgrade Octobre 5-6 2018. 2018;:PPP3 / IL3.
https://hdl.handle.net/21.15107/rcub_cer_7526 .

Andjelković, Uroš, "Masena spektrometrija kao fudomički alat za istraživanje i kontrolu proteinskih alergena hrane" in Unifood Conference, Program i zbornik radova, Beograd, 5 i 6 oktobar 2018. / Unifood Conference, Programme & Book of Abstracts, Belgrade Octobre 5-6 2018 (2018):PPP3 / IL3,
https://hdl.handle.net/21.15107/rcub_cer_7526 .

TY  - CONF
AU  - Protić-Rosić, Isidora
AU  - Popović, Milica
AU  - Anđelković, Uroš
AU  - Gavrović-Jankulović, Marija
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3546
AB  - The sublingual route of allergens administration in allergen-specific immunotherapy (ASIT) is proven to be a successful way to treat patients with respiratory allergy. The trend of replacing natural extracts with purified recombinant allergens is growing. Although the purified allergens themselves are not good immunogens, the combined vector systems and adjuvans can improve their immunogenicity 1. Cell surfaces are decorated by different glycan structures, so the lectins specific for these glycans can be used to deliver particular therapeutic to target specific tissue 2. Banana lectin (BanLec) is mannose-specific protein which belongs to the subfamily of Jacalin related lectins 3. Apart from its characteristic to bind glycans, BanLec also modulates immune cells in vitro 4. On the other hand, Bet v 1 (Betula verrucosa) is the major birch pollen allergen. T-cell epitops are distributed over almost entire protein structure 5. In the study the recombinant BanLec-Bet v 1 construct is designed, produced by the recombinant DNA technology, purified and characterized by classical biochemical methods for the application in the ASIT of birch pollen allergy. The expression of newly designed BanLec-Bet v 1 was performed in E. coli BL21 (DE3). After expression the protein was found in the inclusion bodies from which it was extracted with 4 M urea solution. After renaturation, affinity chromatography (Sephadex G-75 superfine) was used for protein purification. Biochemical characterization of the chimera was performed by: SDS PAGE electrophoreses, CD spectroscopy and mass spectrometry. Biological activity of the construct was confirmed by binding of BanLecBet v 1 to a horseradish peroxidase glycoprotein in ELISA. Purified BanLec-Bet v 1 showed molecular mass of 32 kDa. CD spectra of the recombinant construct revealed well defined secondary structures with predominant beta sheets (41.2%). By mass spectrometry 51.8% of the BanLec-Bet v 1 primary structure was confirmed. Biologicaly active recombinant BanLec-Bet v 1 was produced by the recombinant DNA technology. Further in vitro and in vivo studies will evaluate immunomodulatory potential of BanLec-Bet v 1 for application in ASIT.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Eighth Conference with international participation, “Coordination in Biochemistry and Life”, University of Novi Sad – Rectorate Hall, 16.11.2018. Novi Sad, Serbia
T1  - Production, purification and structural characterisation of recombinant BanLec-Bet v 1
SP  - 177
EP  - 178
UR  - https://hdl.handle.net/21.15107/rcub_cer_3546
ER  - 

@conference{
author = "Protić-Rosić, Isidora and Popović, Milica and Anđelković, Uroš and Gavrović-Jankulović, Marija",
year = "2018",
abstract = "The sublingual route of allergens administration in allergen-specific immunotherapy (ASIT) is proven to be a successful way to treat patients with respiratory allergy. The trend of replacing natural extracts with purified recombinant allergens is growing. Although the purified allergens themselves are not good immunogens, the combined vector systems and adjuvans can improve their immunogenicity 1. Cell surfaces are decorated by different glycan structures, so the lectins specific for these glycans can be used to deliver particular therapeutic to target specific tissue 2. Banana lectin (BanLec) is mannose-specific protein which belongs to the subfamily of Jacalin related lectins 3. Apart from its characteristic to bind glycans, BanLec also modulates immune cells in vitro 4. On the other hand, Bet v 1 (Betula verrucosa) is the major birch pollen allergen. T-cell epitops are distributed over almost entire protein structure 5. In the study the recombinant BanLec-Bet v 1 construct is designed, produced by the recombinant DNA technology, purified and characterized by classical biochemical methods for the application in the ASIT of birch pollen allergy. The expression of newly designed BanLec-Bet v 1 was performed in E. coli BL21 (DE3). After expression the protein was found in the inclusion bodies from which it was extracted with 4 M urea solution. After renaturation, affinity chromatography (Sephadex G-75 superfine) was used for protein purification. Biochemical characterization of the chimera was performed by: SDS PAGE electrophoreses, CD spectroscopy and mass spectrometry. Biological activity of the construct was confirmed by binding of BanLecBet v 1 to a horseradish peroxidase glycoprotein in ELISA. Purified BanLec-Bet v 1 showed molecular mass of 32 kDa. CD spectra of the recombinant construct revealed well defined secondary structures with predominant beta sheets (41.2%). By mass spectrometry 51.8% of the BanLec-Bet v 1 primary structure was confirmed. Biologicaly active recombinant BanLec-Bet v 1 was produced by the recombinant DNA technology. Further in vitro and in vivo studies will evaluate immunomodulatory potential of BanLec-Bet v 1 for application in ASIT.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Eighth Conference with international participation, “Coordination in Biochemistry and Life”, University of Novi Sad – Rectorate Hall, 16.11.2018. Novi Sad, Serbia",
title = "Production, purification and structural characterisation of recombinant BanLec-Bet v 1",
pages = "177-178",
url = "https://hdl.handle.net/21.15107/rcub_cer_3546"
}

Protić-Rosić, I., Popović, M., Anđelković, U.,& Gavrović-Jankulović, M.. (2018). Production, purification and structural characterisation of recombinant BanLec-Bet v 1. in Serbian Biochemical Society Eighth Conference with international participation, “Coordination in Biochemistry and Life”, University of Novi Sad – Rectorate Hall, 16.11.2018. Novi Sad, Serbia
Serbian Biochemical Society., 177-178.
https://hdl.handle.net/21.15107/rcub_cer_3546

Protić-Rosić I, Popović M, Anđelković U, Gavrović-Jankulović M. Production, purification and structural characterisation of recombinant BanLec-Bet v 1. in Serbian Biochemical Society Eighth Conference with international participation, “Coordination in Biochemistry and Life”, University of Novi Sad – Rectorate Hall, 16.11.2018. Novi Sad, Serbia. 2018;:177-178.
https://hdl.handle.net/21.15107/rcub_cer_3546 .

Protić-Rosić, Isidora, Popović, Milica, Anđelković, Uroš, Gavrović-Jankulović, Marija, "Production, purification and structural characterisation of recombinant BanLec-Bet v 1" in Serbian Biochemical Society Eighth Conference with international participation, “Coordination in Biochemistry and Life”, University of Novi Sad – Rectorate Hall, 16.11.2018. Novi Sad, Serbia (2018):177-178,
https://hdl.handle.net/21.15107/rcub_cer_3546 .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Josić, Djuro
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2287
AB  - Background.: As a comprehensive discipline that studies food and nutrition, foodomics requires reliable qualitative and quantitative information about the food proteome component in order to extract new integrative information from the complex multivariable space of omics. This new information is necessary to achieve a higher level of understanding of processes in food science and technology, consequently new functions of food and improved markers of food quality and safety and completely transform concept of food safety. Scope and approach: We are making an effort to present mass spectrometry (MS) based proteomic approaches that are being utilized in different proteomic studies, not necessarily in the field of foodomics, which are important and have the potential to advance this field. Current analytical capabilities of MS-based proteomics together with sample preparation procedures and quantification strategies, and recent technical developments were presented. Key findings and conclusions: MS-based proteomics enables the analysis of different aspects of proteins and provides a variety of approaches for reliable quantification of individual proteinsand/or food proteome. This is a complex field and its successful implementation requires a dedicated analyst, a thorough design of sample preparation procedure, the selection of an MS technique and approach, an adequate type of mass spectrometer, a thorough data analysis and validation. Improvements in the technology of mass spectrometers are continuously expanding capabilities of MS-based proteomics.
PB  - Elsevier Science London, London
T2  - Trends in Food Science & Technology
T1  - Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety
VL  - 77
SP  - 100
EP  - 119
DO  - 10.1016/j.tifs.2018.04.008
ER  - 

@article{
author = "Anđelković, Uroš and Josić, Djuro",
year = "2018",
abstract = "Background.: As a comprehensive discipline that studies food and nutrition, foodomics requires reliable qualitative and quantitative information about the food proteome component in order to extract new integrative information from the complex multivariable space of omics. This new information is necessary to achieve a higher level of understanding of processes in food science and technology, consequently new functions of food and improved markers of food quality and safety and completely transform concept of food safety. Scope and approach: We are making an effort to present mass spectrometry (MS) based proteomic approaches that are being utilized in different proteomic studies, not necessarily in the field of foodomics, which are important and have the potential to advance this field. Current analytical capabilities of MS-based proteomics together with sample preparation procedures and quantification strategies, and recent technical developments were presented. Key findings and conclusions: MS-based proteomics enables the analysis of different aspects of proteins and provides a variety of approaches for reliable quantification of individual proteinsand/or food proteome. This is a complex field and its successful implementation requires a dedicated analyst, a thorough design of sample preparation procedure, the selection of an MS technique and approach, an adequate type of mass spectrometer, a thorough data analysis and validation. Improvements in the technology of mass spectrometers are continuously expanding capabilities of MS-based proteomics.",
publisher = "Elsevier Science London, London",
journal = "Trends in Food Science & Technology",
title = "Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety",
volume = "77",
pages = "100-119",
doi = "10.1016/j.tifs.2018.04.008"
}

Anđelković, U.,& Josić, D.. (2018). Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety. in Trends in Food Science & Technology
Elsevier Science London, London., 77, 100-119.
https://doi.org/10.1016/j.tifs.2018.04.008

Anđelković U, Josić D. Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety. in Trends in Food Science & Technology. 2018;77:100-119.
doi:10.1016/j.tifs.2018.04.008 .

Anđelković, Uroš, Josić, Djuro, "Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety" in Trends in Food Science & Technology, 77 (2018):100-119,
https://doi.org/10.1016/j.tifs.2018.04.008 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Josić, Djuro
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4280
AB  - Background.: As a comprehensive discipline that studies food and nutrition, foodomics requires reliable qualitative and quantitative information about the food proteome component in order to extract new integrative information from the complex multivariable space of omics. This new information is necessary to achieve a higher level of understanding of processes in food science and technology, consequently new functions of food and improved markers of food quality and safety and completely transform concept of food safety. Scope and approach: We are making an effort to present mass spectrometry (MS) based proteomic approaches that are being utilized in different proteomic studies, not necessarily in the field of foodomics, which are important and have the potential to advance this field. Current analytical capabilities of MS-based proteomics together with sample preparation procedures and quantification strategies, and recent technical developments were presented. Key findings and conclusions: MS-based proteomics enables the analysis of different aspects of proteins and provides a variety of approaches for reliable quantification of individual proteinsand/or food proteome. This is a complex field and its successful implementation requires a dedicated analyst, a thorough design of sample preparation procedure, the selection of an MS technique and approach, an adequate type of mass spectrometer, a thorough data analysis and validation. Improvements in the technology of mass spectrometers are continuously expanding capabilities of MS-based proteomics.
PB  - Elsevier Science London, London
T2  - Trends in Food Science & Technology
T1  - Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety
VL  - 77
SP  - 100
EP  - 119
DO  - 10.1016/j.tifs.2018.04.008
ER  - 

@article{
author = "Anđelković, Uroš and Josić, Djuro",
year = "2018",
abstract = "Background.: As a comprehensive discipline that studies food and nutrition, foodomics requires reliable qualitative and quantitative information about the food proteome component in order to extract new integrative information from the complex multivariable space of omics. This new information is necessary to achieve a higher level of understanding of processes in food science and technology, consequently new functions of food and improved markers of food quality and safety and completely transform concept of food safety. Scope and approach: We are making an effort to present mass spectrometry (MS) based proteomic approaches that are being utilized in different proteomic studies, not necessarily in the field of foodomics, which are important and have the potential to advance this field. Current analytical capabilities of MS-based proteomics together with sample preparation procedures and quantification strategies, and recent technical developments were presented. Key findings and conclusions: MS-based proteomics enables the analysis of different aspects of proteins and provides a variety of approaches for reliable quantification of individual proteinsand/or food proteome. This is a complex field and its successful implementation requires a dedicated analyst, a thorough design of sample preparation procedure, the selection of an MS technique and approach, an adequate type of mass spectrometer, a thorough data analysis and validation. Improvements in the technology of mass spectrometers are continuously expanding capabilities of MS-based proteomics.",
publisher = "Elsevier Science London, London",
journal = "Trends in Food Science & Technology",
title = "Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety",
volume = "77",
pages = "100-119",
doi = "10.1016/j.tifs.2018.04.008"
}

Anđelković, U.,& Josić, D.. (2018). Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety. in Trends in Food Science & Technology
Elsevier Science London, London., 77, 100-119.
https://doi.org/10.1016/j.tifs.2018.04.008

Anđelković U, Josić D. Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety. in Trends in Food Science & Technology. 2018;77:100-119.
doi:10.1016/j.tifs.2018.04.008 .

Anđelković, Uroš, Josić, Djuro, "Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety" in Trends in Food Science & Technology, 77 (2018):100-119,
https://doi.org/10.1016/j.tifs.2018.04.008 . .

TY  - JOUR
AU  - Nikolić, Jasna
AU  - Nešić, Andrijana
AU  - Čavić, Milena
AU  - Đorđević, Neda O.
AU  - Anđelković, Uroš
AU  - Atanasković-Marković, Marina
AU  - Drakulić, Branko
AU  - Gavrović-Jankulović, Marija
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2058
AB  - Background: Protein oxidation can occur as a consequence of lipid peroxidation during food processing. The aim of this work was to explore the effect of malondialdehyde (MDA) modification of ovalbumin (OVA) on its interaction with T84 intestinal cells. Methods: Molecular dynamics simulation was employed for the prediction of MDA modification in the OVA, while introduced structural changes were evaluated by measurement of carbonyl group content, fluorescence spectra, MS/MS analysis, and IgE reactivity. Effects of MDA modified OVA on T84 epithelial cells were analyzed by gene expression for pro-inflammatory cytokines and protein secretion. Results: Out of 9 predicted, five modified Lys residues were confirmed by MS/MS analysis: (51)TQINKVVR(58), (85)DILNQITKPNDVYSFSLASR(104), (111)YPILPEYLQCVKELYR(126), (187)AFKDEDTQAMPFR(99), (KIKVYLPR284)-K-277, and (IKVYLPR284)-I-278. The introduced MDA modifications influenced profile of IgE reactivity to OVA. Treatment of T84 epithelial cells with OVA and OVA modified with 1 mM MDA, induced up-regulation of pro-inflammatory cytokines (IL-1 beta,IL-25, IL-33, TSLP and TNF alpha), while OVA modification with 10 mM MDA induced down regulation of the cytokine expression profile, except for IL-1 beta. OVA and OVA modified with 1 mM MDA induced secretion of epithelial cells specific cytokine IL-33. Conclusions: This finding indicated that OVA and its MDA modified form have the potential to trigger the innate immunity by inducing up-regulation and secretion of pro-allergenic IL-33 in T84 intestinal epithelial cells. General significance: Interactions of ovalbumin and its MDA modified form with intestinal epithelial cells can induce a specific immunological priming necessary for the downstream activation of innate immunity.
PB  - Elsevier
T2  - Biochimica et Biophysica Acta-General Subjects
T1  - Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells
VL  - 1861
IS  - 2
SP  - 126
EP  - 134
DO  - 10.1016/j.bbagen.2016.11.021
ER  - 

@article{
author = "Nikolić, Jasna and Nešić, Andrijana and Čavić, Milena and Đorđević, Neda O. and Anđelković, Uroš and Atanasković-Marković, Marina and Drakulić, Branko and Gavrović-Jankulović, Marija",
year = "2017",
abstract = "Background: Protein oxidation can occur as a consequence of lipid peroxidation during food processing. The aim of this work was to explore the effect of malondialdehyde (MDA) modification of ovalbumin (OVA) on its interaction with T84 intestinal cells. Methods: Molecular dynamics simulation was employed for the prediction of MDA modification in the OVA, while introduced structural changes were evaluated by measurement of carbonyl group content, fluorescence spectra, MS/MS analysis, and IgE reactivity. Effects of MDA modified OVA on T84 epithelial cells were analyzed by gene expression for pro-inflammatory cytokines and protein secretion. Results: Out of 9 predicted, five modified Lys residues were confirmed by MS/MS analysis: (51)TQINKVVR(58), (85)DILNQITKPNDVYSFSLASR(104), (111)YPILPEYLQCVKELYR(126), (187)AFKDEDTQAMPFR(99), (KIKVYLPR284)-K-277, and (IKVYLPR284)-I-278. The introduced MDA modifications influenced profile of IgE reactivity to OVA. Treatment of T84 epithelial cells with OVA and OVA modified with 1 mM MDA, induced up-regulation of pro-inflammatory cytokines (IL-1 beta,IL-25, IL-33, TSLP and TNF alpha), while OVA modification with 10 mM MDA induced down regulation of the cytokine expression profile, except for IL-1 beta. OVA and OVA modified with 1 mM MDA induced secretion of epithelial cells specific cytokine IL-33. Conclusions: This finding indicated that OVA and its MDA modified form have the potential to trigger the innate immunity by inducing up-regulation and secretion of pro-allergenic IL-33 in T84 intestinal epithelial cells. General significance: Interactions of ovalbumin and its MDA modified form with intestinal epithelial cells can induce a specific immunological priming necessary for the downstream activation of innate immunity.",
publisher = "Elsevier",
journal = "Biochimica et Biophysica Acta-General Subjects",
title = "Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells",
volume = "1861",
number = "2",
pages = "126-134",
doi = "10.1016/j.bbagen.2016.11.021"
}

Nikolić, J., Nešić, A., Čavić, M., Đorđević, N. O., Anđelković, U., Atanasković-Marković, M., Drakulić, B.,& Gavrović-Jankulović, M.. (2017). Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells. in Biochimica et Biophysica Acta-General Subjects
Elsevier., 1861(2), 126-134.
https://doi.org/10.1016/j.bbagen.2016.11.021

Nikolić J, Nešić A, Čavić M, Đorđević NO, Anđelković U, Atanasković-Marković M, Drakulić B, Gavrović-Jankulović M. Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells. in Biochimica et Biophysica Acta-General Subjects. 2017;1861(2):126-134.
doi:10.1016/j.bbagen.2016.11.021 .

Nikolić, Jasna, Nešić, Andrijana, Čavić, Milena, Đorđević, Neda O., Anđelković, Uroš, Atanasković-Marković, Marina, Drakulić, Branko, Gavrović-Jankulović, Marija, "Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells" in Biochimica et Biophysica Acta-General Subjects, 1861, no. 2 (2017):126-134,
https://doi.org/10.1016/j.bbagen.2016.11.021 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Gavrović-Jankulović, Marija
AU  - Martinović, Tamara
AU  - Josić, Djuro
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2113
AB  - Use of foodomics, mostly proteomic and genomic based methods, for study of allergens in food is presented. Immunological methods and nucleic acid-based methods are still most frequently used for diagnosis of allergies and for qualitative and quantitative determination of food allergens. They are sensitive, and can be used for the determination of allergens in trace concentrations. However, lack of specificity and cross-reaction of some antibodies can still be a relevant source of bias. The epitopes of protein allergens with posttranslational modifications and their changes originated during food processing cannot be traced by use of nucleic acid-based strategies. Recent developments of both antibody and nucleic acid-based biosensors, their miniaturization and increasing application of nanotechnology, significantly supported further use of both strategies. Regarding accuracy, reliability and sensitivity, mass spectrometry-based methods bring important advantage over both above presented strategies. Furthermore, the increasing use of mass spectrometry (MS) is discussed. Combined with proper sample preparation, liquid chromatography (LC) and/or different electrophoretic methods, targeted approach in mass spectrometry-based allergen analysis brings an additional strategic advance. However, MS is still rarely used for high-throughput analyses and detection and quantification of allergens for the reasons of price and relatively long time necessary for analysis. Recent developments of new high-resolution instruments are encouraging and enable development in the direction of a high-throughput strategy. Consequently, fast, very sensitive, reliable and accurate detection and quantification of allergens in highly complex samples such as food matrices, and the use of MS in routine determination of allergens can be reached in near future.
PB  - Elsevier Sci Ltd, Oxford
T2  - Trac-Trends in Analytical Chemistry
T1  - Omics methods as a tool for investigation of food allergies
VL  - 96
SP  - 107
EP  - 115
DO  - 10.1016/j.trac.2017.07.011
ER  - 

@article{
author = "Anđelković, Uroš and Gavrović-Jankulović, Marija and Martinović, Tamara and Josić, Djuro",
year = "2017",
abstract = "Use of foodomics, mostly proteomic and genomic based methods, for study of allergens in food is presented. Immunological methods and nucleic acid-based methods are still most frequently used for diagnosis of allergies and for qualitative and quantitative determination of food allergens. They are sensitive, and can be used for the determination of allergens in trace concentrations. However, lack of specificity and cross-reaction of some antibodies can still be a relevant source of bias. The epitopes of protein allergens with posttranslational modifications and their changes originated during food processing cannot be traced by use of nucleic acid-based strategies. Recent developments of both antibody and nucleic acid-based biosensors, their miniaturization and increasing application of nanotechnology, significantly supported further use of both strategies. Regarding accuracy, reliability and sensitivity, mass spectrometry-based methods bring important advantage over both above presented strategies. Furthermore, the increasing use of mass spectrometry (MS) is discussed. Combined with proper sample preparation, liquid chromatography (LC) and/or different electrophoretic methods, targeted approach in mass spectrometry-based allergen analysis brings an additional strategic advance. However, MS is still rarely used for high-throughput analyses and detection and quantification of allergens for the reasons of price and relatively long time necessary for analysis. Recent developments of new high-resolution instruments are encouraging and enable development in the direction of a high-throughput strategy. Consequently, fast, very sensitive, reliable and accurate detection and quantification of allergens in highly complex samples such as food matrices, and the use of MS in routine determination of allergens can be reached in near future.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Trac-Trends in Analytical Chemistry",
title = "Omics methods as a tool for investigation of food allergies",
volume = "96",
pages = "107-115",
doi = "10.1016/j.trac.2017.07.011"
}

Anđelković, U., Gavrović-Jankulović, M., Martinović, T.,& Josić, D.. (2017). Omics methods as a tool for investigation of food allergies. in Trac-Trends in Analytical Chemistry
Elsevier Sci Ltd, Oxford., 96, 107-115.
https://doi.org/10.1016/j.trac.2017.07.011

Anđelković U, Gavrović-Jankulović M, Martinović T, Josić D. Omics methods as a tool for investigation of food allergies. in Trac-Trends in Analytical Chemistry. 2017;96:107-115.
doi:10.1016/j.trac.2017.07.011 .

Anđelković, Uroš, Gavrović-Jankulović, Marija, Martinović, Tamara, Josić, Djuro, "Omics methods as a tool for investigation of food allergies" in Trac-Trends in Analytical Chemistry, 96 (2017):107-115,
https://doi.org/10.1016/j.trac.2017.07.011 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Gavrović-Jankulović, Marija
AU  - Martinović, Tamara
AU  - Josić, Djuro
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2937
AB  - Use of foodomics, mostly proteomic and genomic based methods, for study of allergens in food is presented. Immunological methods and nucleic acid-based methods are still most frequently used for diagnosis of allergies and for qualitative and quantitative determination of food allergens. They are sensitive, and can be used for the determination of allergens in trace concentrations. However, lack of specificity and cross-reaction of some antibodies can still be a relevant source of bias. The epitopes of protein allergens with posttranslational modifications and their changes originated during food processing cannot be traced by use of nucleic acid-based strategies. Recent developments of both antibody and nucleic acid-based biosensors, their miniaturization and increasing application of nanotechnology, significantly supported further use of both strategies. Regarding accuracy, reliability and sensitivity, mass spectrometry-based methods bring important advantage over both above presented strategies. Furthermore, the increasing use of mass spectrometry (MS) is discussed. Combined with proper sample preparation, liquid chromatography (LC) and/or different electrophoretic methods, targeted approach in mass spectrometry-based allergen analysis brings an additional strategic advance. However, MS is still rarely used for high-throughput analyses and detection and quantification of allergens for the reasons of price and relatively long time necessary for analysis. Recent developments of new high-resolution instruments are encouraging and enable development in the direction of a high-throughput strategy. Consequently, fast, very sensitive, reliable and accurate detection and quantification of allergens in highly complex samples such as food matrices, and the use of MS in routine determination of allergens can be reached in near future.
PB  - Elsevier
T2  - Trac-Trends in Analytical Chemistry
T1  - Omics methods as a tool for investigation of food allergies
VL  - 96
SP  - 107
EP  - 115
DO  - 10.1016/j.trac.2017.07.011
ER  - 

@article{
author = "Anđelković, Uroš and Gavrović-Jankulović, Marija and Martinović, Tamara and Josić, Djuro",
year = "2017",
abstract = "Use of foodomics, mostly proteomic and genomic based methods, for study of allergens in food is presented. Immunological methods and nucleic acid-based methods are still most frequently used for diagnosis of allergies and for qualitative and quantitative determination of food allergens. They are sensitive, and can be used for the determination of allergens in trace concentrations. However, lack of specificity and cross-reaction of some antibodies can still be a relevant source of bias. The epitopes of protein allergens with posttranslational modifications and their changes originated during food processing cannot be traced by use of nucleic acid-based strategies. Recent developments of both antibody and nucleic acid-based biosensors, their miniaturization and increasing application of nanotechnology, significantly supported further use of both strategies. Regarding accuracy, reliability and sensitivity, mass spectrometry-based methods bring important advantage over both above presented strategies. Furthermore, the increasing use of mass spectrometry (MS) is discussed. Combined with proper sample preparation, liquid chromatography (LC) and/or different electrophoretic methods, targeted approach in mass spectrometry-based allergen analysis brings an additional strategic advance. However, MS is still rarely used for high-throughput analyses and detection and quantification of allergens for the reasons of price and relatively long time necessary for analysis. Recent developments of new high-resolution instruments are encouraging and enable development in the direction of a high-throughput strategy. Consequently, fast, very sensitive, reliable and accurate detection and quantification of allergens in highly complex samples such as food matrices, and the use of MS in routine determination of allergens can be reached in near future.",
publisher = "Elsevier",
journal = "Trac-Trends in Analytical Chemistry",
title = "Omics methods as a tool for investigation of food allergies",
volume = "96",
pages = "107-115",
doi = "10.1016/j.trac.2017.07.011"
}

Anđelković, U., Gavrović-Jankulović, M., Martinović, T.,& Josić, D.. (2017). Omics methods as a tool for investigation of food allergies. in Trac-Trends in Analytical Chemistry
Elsevier., 96, 107-115.
https://doi.org/10.1016/j.trac.2017.07.011

Anđelković U, Gavrović-Jankulović M, Martinović T, Josić D. Omics methods as a tool for investigation of food allergies. in Trac-Trends in Analytical Chemistry. 2017;96:107-115.
doi:10.1016/j.trac.2017.07.011 .

Anđelković, Uroš, Gavrović-Jankulović, Marija, Martinović, Tamara, Josić, Djuro, "Omics methods as a tool for investigation of food allergies" in Trac-Trends in Analytical Chemistry, 96 (2017):107-115,
https://doi.org/10.1016/j.trac.2017.07.011 . .

TY  - JOUR
AU  - Nikolić, Jasna
AU  - Nešić, Andrijana
AU  - Čavić, Milena
AU  - Đorđević, Neda O.
AU  - Anđelković, Uroš
AU  - Atanasković-Marković, Marina
AU  - Drakulić, Branko
AU  - Gavrović-Jankulović, Marija
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3042
AB  - Background: Protein oxidation can occur as a consequence of lipid peroxidation during food processing. The aim of this work was to explore the effect of malondialdehyde (MDA) modification of ovalbumin (OVA) on its interaction with T84 intestinal cells. Methods: Molecular dynamics simulation was employed for the prediction of MDA modification in the OVA, while introduced structural changes were evaluated by measurement of carbonyl group content, fluorescence spectra, MS/MS analysis, and IgE reactivity. Effects of MDA modified OVA on T84 epithelial cells were analyzed by gene expression for pro-inflammatory cytokines and protein secretion. Results: Out of 9 predicted, five modified Lys residues were confirmed by MS/MS analysis: (51)TQINKVVR(58), (85)DILNQITKPNDVYSFSLASR(104), (111)YPILPEYLQCVKELYR(126), (187)AFKDEDTQAMPFR(99), (KIKVYLPR284)-K-277, and (IKVYLPR284)-I-278. The introduced MDA modifications influenced profile of IgE reactivity to OVA. Treatment of T84 epithelial cells with OVA and OVA modified with 1 mM MDA, induced up-regulation of pro-inflammatory cytokines (IL-1 beta,IL-25, IL-33, TSLP and TNF alpha), while OVA modification with 10 mM MDA induced down regulation of the cytokine expression profile, except for IL-1 beta. OVA and OVA modified with 1 mM MDA induced secretion of epithelial cells specific cytokine IL-33. Conclusions: This finding indicated that OVA and its MDA modified form have the potential to trigger the innate immunity by inducing up-regulation and secretion of pro-allergenic IL-33 in T84 intestinal epithelial cells. General significance: Interactions of ovalbumin and its MDA modified form with intestinal epithelial cells can induce a specific immunological priming necessary for the downstream activation of innate immunity.
PB  - Elsevier
T2  - Biochimica et Biophysica Acta-General Subjects
T1  - Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells
VL  - 1861
IS  - 2
SP  - 126
EP  - 134
DO  - 10.1016/j.bbagen.2016.11.021
ER  - 

@article{
author = "Nikolić, Jasna and Nešić, Andrijana and Čavić, Milena and Đorđević, Neda O. and Anđelković, Uroš and Atanasković-Marković, Marina and Drakulić, Branko and Gavrović-Jankulović, Marija",
year = "2017",
abstract = "Background: Protein oxidation can occur as a consequence of lipid peroxidation during food processing. The aim of this work was to explore the effect of malondialdehyde (MDA) modification of ovalbumin (OVA) on its interaction with T84 intestinal cells. Methods: Molecular dynamics simulation was employed for the prediction of MDA modification in the OVA, while introduced structural changes were evaluated by measurement of carbonyl group content, fluorescence spectra, MS/MS analysis, and IgE reactivity. Effects of MDA modified OVA on T84 epithelial cells were analyzed by gene expression for pro-inflammatory cytokines and protein secretion. Results: Out of 9 predicted, five modified Lys residues were confirmed by MS/MS analysis: (51)TQINKVVR(58), (85)DILNQITKPNDVYSFSLASR(104), (111)YPILPEYLQCVKELYR(126), (187)AFKDEDTQAMPFR(99), (KIKVYLPR284)-K-277, and (IKVYLPR284)-I-278. The introduced MDA modifications influenced profile of IgE reactivity to OVA. Treatment of T84 epithelial cells with OVA and OVA modified with 1 mM MDA, induced up-regulation of pro-inflammatory cytokines (IL-1 beta,IL-25, IL-33, TSLP and TNF alpha), while OVA modification with 10 mM MDA induced down regulation of the cytokine expression profile, except for IL-1 beta. OVA and OVA modified with 1 mM MDA induced secretion of epithelial cells specific cytokine IL-33. Conclusions: This finding indicated that OVA and its MDA modified form have the potential to trigger the innate immunity by inducing up-regulation and secretion of pro-allergenic IL-33 in T84 intestinal epithelial cells. General significance: Interactions of ovalbumin and its MDA modified form with intestinal epithelial cells can induce a specific immunological priming necessary for the downstream activation of innate immunity.",
publisher = "Elsevier",
journal = "Biochimica et Biophysica Acta-General Subjects",
title = "Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells",
volume = "1861",
number = "2",
pages = "126-134",
doi = "10.1016/j.bbagen.2016.11.021"
}

Nikolić, J., Nešić, A., Čavić, M., Đorđević, N. O., Anđelković, U., Atanasković-Marković, M., Drakulić, B.,& Gavrović-Jankulović, M.. (2017). Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells. in Biochimica et Biophysica Acta-General Subjects
Elsevier., 1861(2), 126-134.
https://doi.org/10.1016/j.bbagen.2016.11.021

Nikolić J, Nešić A, Čavić M, Đorđević NO, Anđelković U, Atanasković-Marković M, Drakulić B, Gavrović-Jankulović M. Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells. in Biochimica et Biophysica Acta-General Subjects. 2017;1861(2):126-134.
doi:10.1016/j.bbagen.2016.11.021 .

Nikolić, Jasna, Nešić, Andrijana, Čavić, Milena, Đorđević, Neda O., Anđelković, Uroš, Atanasković-Marković, Marina, Drakulić, Branko, Gavrović-Jankulović, Marija, "Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells" in Biochimica et Biophysica Acta-General Subjects, 1861, no. 2 (2017):126-134,
https://doi.org/10.1016/j.bbagen.2016.11.021 . .

TY  - JOUR
AU  - Srajer-Gajdošik, Martina
AU  - Anđelković, Uroš
AU  - Gašo Sokač, Dajana
AU  - Pavlović, Hrvoje
AU  - Shevchuk, Olga
AU  - Martinović, Tamara
AU  - Clifton, James
AU  - Josić, Djuro
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6918
AB  - A comprehensive proteomic analysis of food borne pathogens after treatment with disinfectants based on ammonium salts of pyridinium oxime was performed. Changes in proteomes of the Gram-positive bacterium Bacillus subtilis and the Gram-negative one, Escherichia coli, were evaluated. Up and down-regulated proteins in these bacteria after growth under the inhibition with four different disinfectants based on chloride and bromide salts of pyridinium oxime were identified and their cellular localizations and functions were determined by gene ontology searching. Proteome changes presented here demonstrate different mechanisms of action of these disinfectants. In the Gram-positive food pathogen Bacillus subtilis, the inhibitory substances seem to act mainly at the cell surface and cause significant alterations of membrane and cell surface proteins. On the other hand, intracellular proteins were more affected in the Gram-negative pathogen Escherichia coli. This research is a contribution to the investigation of the virulence and pathogenicity of food borne bacteria and their survival under stress conditions, and can also lead the way for further development of new inhibitors of microbial growth and studies of mechanism of their actions.
PB  - Elsevier
T2  - Food Research International
T1  - Proteomic analysis of food borne pathogens following the mode of action of the disinfectants based on pyridoxal oxime derivatives
VL  - 99
SP  - 560
EP  - 570
DO  - 10.1016/j.foodres.2017.06.016
ER  - 

@article{
author = "Srajer-Gajdošik, Martina and Anđelković, Uroš and Gašo Sokač, Dajana and Pavlović, Hrvoje and Shevchuk, Olga and Martinović, Tamara and Clifton, James and Josić, Djuro",
year = "2017",
abstract = "A comprehensive proteomic analysis of food borne pathogens after treatment with disinfectants based on ammonium salts of pyridinium oxime was performed. Changes in proteomes of the Gram-positive bacterium Bacillus subtilis and the Gram-negative one, Escherichia coli, were evaluated. Up and down-regulated proteins in these bacteria after growth under the inhibition with four different disinfectants based on chloride and bromide salts of pyridinium oxime were identified and their cellular localizations and functions were determined by gene ontology searching. Proteome changes presented here demonstrate different mechanisms of action of these disinfectants. In the Gram-positive food pathogen Bacillus subtilis, the inhibitory substances seem to act mainly at the cell surface and cause significant alterations of membrane and cell surface proteins. On the other hand, intracellular proteins were more affected in the Gram-negative pathogen Escherichia coli. This research is a contribution to the investigation of the virulence and pathogenicity of food borne bacteria and their survival under stress conditions, and can also lead the way for further development of new inhibitors of microbial growth and studies of mechanism of their actions.",
publisher = "Elsevier",
journal = "Food Research International",
title = "Proteomic analysis of food borne pathogens following the mode of action of the disinfectants based on pyridoxal oxime derivatives",
volume = "99",
pages = "560-570",
doi = "10.1016/j.foodres.2017.06.016"
}

Srajer-Gajdošik, M., Anđelković, U., Gašo Sokač, D., Pavlović, H., Shevchuk, O., Martinović, T., Clifton, J.,& Josić, D.. (2017). Proteomic analysis of food borne pathogens following the mode of action of the disinfectants based on pyridoxal oxime derivatives. in Food Research International
Elsevier., 99, 560-570.
https://doi.org/10.1016/j.foodres.2017.06.016

Srajer-Gajdošik M, Anđelković U, Gašo Sokač D, Pavlović H, Shevchuk O, Martinović T, Clifton J, Josić D. Proteomic analysis of food borne pathogens following the mode of action of the disinfectants based on pyridoxal oxime derivatives. in Food Research International. 2017;99:560-570.
doi:10.1016/j.foodres.2017.06.016 .

Srajer-Gajdošik, Martina, Anđelković, Uroš, Gašo Sokač, Dajana, Pavlović, Hrvoje, Shevchuk, Olga, Martinović, Tamara, Clifton, James, Josić, Djuro, "Proteomic analysis of food borne pathogens following the mode of action of the disinfectants based on pyridoxal oxime derivatives" in Food Research International, 99 (2017):560-570,
https://doi.org/10.1016/j.foodres.2017.06.016 . .

TY  - JOUR
AU  - Srajer-Gajdošik, Martina
AU  - Anđelković, Uroš
AU  - Gašo Sokač, Dajana
AU  - Pavlović, Hrvoje
AU  - Shevchuk, Olga
AU  - Martinović, Tamara
AU  - Clifton, James
AU  - Josić, Djuro
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6919
AB  - Food borne pathogens, namely the Gram-positive bacterium Bacillus subtilis and the Gram-negative bacterium Escherichia coli, were grown under the inhibition with four different disinfectants based on chloride and bromide salts of pyridinium oxime. Bacterial samples were subjected to the sequential extraction of proteins and the in-solution tryptic digestion of obtained extracts was performed prior to the identification of proteins with LC-ESI-MS/MS. Proteomic analysis identified up- and down-regulated proteins in these bacteria after treatment with each compound. The tables with differently expressed proteins are presented with this article.
PB  - Elsevier
T2  - Data in brief
T1  - Data set of proteomic analysis of food borne pathogens after treatment with the disinfectants based on pyridoxal oxime derivatives
VL  - 15
SP  - 738
EP  - 741
DO  - 10.1016/j.dib.2017.09.060
ER  - 

@article{
author = "Srajer-Gajdošik, Martina and Anđelković, Uroš and Gašo Sokač, Dajana and Pavlović, Hrvoje and Shevchuk, Olga and Martinović, Tamara and Clifton, James and Josić, Djuro",
year = "2017",
abstract = "Food borne pathogens, namely the Gram-positive bacterium Bacillus subtilis and the Gram-negative bacterium Escherichia coli, were grown under the inhibition with four different disinfectants based on chloride and bromide salts of pyridinium oxime. Bacterial samples were subjected to the sequential extraction of proteins and the in-solution tryptic digestion of obtained extracts was performed prior to the identification of proteins with LC-ESI-MS/MS. Proteomic analysis identified up- and down-regulated proteins in these bacteria after treatment with each compound. The tables with differently expressed proteins are presented with this article.",
publisher = "Elsevier",
journal = "Data in brief",
title = "Data set of proteomic analysis of food borne pathogens after treatment with the disinfectants based on pyridoxal oxime derivatives",
volume = "15",
pages = "738-741",
doi = "10.1016/j.dib.2017.09.060"
}

Srajer-Gajdošik, M., Anđelković, U., Gašo Sokač, D., Pavlović, H., Shevchuk, O., Martinović, T., Clifton, J.,& Josić, D.. (2017). Data set of proteomic analysis of food borne pathogens after treatment with the disinfectants based on pyridoxal oxime derivatives. in Data in brief
Elsevier., 15, 738-741.
https://doi.org/10.1016/j.dib.2017.09.060

Srajer-Gajdošik M, Anđelković U, Gašo Sokač D, Pavlović H, Shevchuk O, Martinović T, Clifton J, Josić D. Data set of proteomic analysis of food borne pathogens after treatment with the disinfectants based on pyridoxal oxime derivatives. in Data in brief. 2017;15:738-741.
doi:10.1016/j.dib.2017.09.060 .

Srajer-Gajdošik, Martina, Anđelković, Uroš, Gašo Sokač, Dajana, Pavlović, Hrvoje, Shevchuk, Olga, Martinović, Tamara, Clifton, James, Josić, Djuro, "Data set of proteomic analysis of food borne pathogens after treatment with the disinfectants based on pyridoxal oxime derivatives" in Data in brief, 15 (2017):738-741,
https://doi.org/10.1016/j.dib.2017.09.060 . .

TY  - JOUR
AU  - Martinović, Tamara
AU  - Anđelković, Uroš
AU  - Klobučar, Marko
AU  - Černigoj, Urh
AU  - Vidič, Jana
AU  - Lučić, Marina
AU  - Pavelić, Krešimir
AU  - Josić, Djuro
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6922
AB  - Posttranslational modifications of immunoglobulins have been a topic of great interest and have been repeatedly reported as a major factor in disease pathology. Cost-effective, reproducible, and high-throughput (HTP) isolation of immunoglobulins from human serum is vital for studying the changes in protein structure and the following understanding of disease development. Although there are many methods for the isolation of specific immunoglobulin classes, only a few of them are applicable for isolation of all subtypes and variants. Here, we present the development of a scheme for fast and simultaneous affinity purification of α (A), γ (G), and μ (M) immunoglobulins from human serum through affinity monolith chromatography. Affinity-based monolithic columns with immobilized protein A, G, or L were used for antibody isolation. Monolithic stationary phases have a high surface accessibility of binding sites, large flow-through channels, and can be operated at high flow rates, making them the ideal supports for HTP isolation of biopolymers. The presented method can be used for HTP screening of human serum in order to simultaneously isolate all three above-mentioned immunoglobulins and determine their concentration and changes in their glycosylation pattern as potential prognostic and diagnostic disease biomarkers.
PB  - Willey
T2  - Electrophoresis
T1  - Affinity chromatography on monolithic supports for simultaneous and high-throughput isolation of immunoglobulins from human serum
VL  - 38
IS  - 22-23
SP  - 2909
EP  - 2913
DO  - 10.1002/elps.201700216
ER  - 

@article{
author = "Martinović, Tamara and Anđelković, Uroš and Klobučar, Marko and Černigoj, Urh and Vidič, Jana and Lučić, Marina and Pavelić, Krešimir and Josić, Djuro",
year = "2017",
abstract = "Posttranslational modifications of immunoglobulins have been a topic of great interest and have been repeatedly reported as a major factor in disease pathology. Cost-effective, reproducible, and high-throughput (HTP) isolation of immunoglobulins from human serum is vital for studying the changes in protein structure and the following understanding of disease development. Although there are many methods for the isolation of specific immunoglobulin classes, only a few of them are applicable for isolation of all subtypes and variants. Here, we present the development of a scheme for fast and simultaneous affinity purification of α (A), γ (G), and μ (M) immunoglobulins from human serum through affinity monolith chromatography. Affinity-based monolithic columns with immobilized protein A, G, or L were used for antibody isolation. Monolithic stationary phases have a high surface accessibility of binding sites, large flow-through channels, and can be operated at high flow rates, making them the ideal supports for HTP isolation of biopolymers. The presented method can be used for HTP screening of human serum in order to simultaneously isolate all three above-mentioned immunoglobulins and determine their concentration and changes in their glycosylation pattern as potential prognostic and diagnostic disease biomarkers.",
publisher = "Willey",
journal = "Electrophoresis",
title = "Affinity chromatography on monolithic supports for simultaneous and high-throughput isolation of immunoglobulins from human serum",
volume = "38",
number = "22-23",
pages = "2909-2913",
doi = "10.1002/elps.201700216"
}

Martinović, T., Anđelković, U., Klobučar, M., Černigoj, U., Vidič, J., Lučić, M., Pavelić, K.,& Josić, D.. (2017). Affinity chromatography on monolithic supports for simultaneous and high-throughput isolation of immunoglobulins from human serum. in Electrophoresis
Willey., 38(22-23), 2909-2913.
https://doi.org/10.1002/elps.201700216

Martinović T, Anđelković U, Klobučar M, Černigoj U, Vidič J, Lučić M, Pavelić K, Josić D. Affinity chromatography on monolithic supports for simultaneous and high-throughput isolation of immunoglobulins from human serum. in Electrophoresis. 2017;38(22-23):2909-2913.
doi:10.1002/elps.201700216 .

Martinović, Tamara, Anđelković, Uroš, Klobučar, Marko, Černigoj, Urh, Vidič, Jana, Lučić, Marina, Pavelić, Krešimir, Josić, Djuro, "Affinity chromatography on monolithic supports for simultaneous and high-throughput isolation of immunoglobulins from human serum" in Electrophoresis, 38, no. 22-23 (2017):2909-2913,
https://doi.org/10.1002/elps.201700216 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Tufegdžić, Srđan
AU  - Popović, Milica
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2122
AB  - The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.
PB  - Wiley, Hoboken
T2  - Electrophoresis
T1  - Use of monolithic supports for high-throughput protein and peptide separation in proteomics
VL  - 38
IS  - 22-23
SP  - 2851
EP  - 2869
DO  - 10.1002/elps.201700260
ER  - 

@article{
author = "Anđelković, Uroš and Tufegdžić, Srđan and Popović, Milica",
year = "2017",
abstract = "The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.",
publisher = "Wiley, Hoboken",
journal = "Electrophoresis",
title = "Use of monolithic supports for high-throughput protein and peptide separation in proteomics",
volume = "38",
number = "22-23",
pages = "2851-2869",
doi = "10.1002/elps.201700260"
}

Anđelković, U., Tufegdžić, S.,& Popović, M.. (2017). Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis
Wiley, Hoboken., 38(22-23), 2851-2869.
https://doi.org/10.1002/elps.201700260

Anđelković U, Tufegdžić S, Popović M. Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis. 2017;38(22-23):2851-2869.
doi:10.1002/elps.201700260 .

Anđelković, Uroš, Tufegdžić, Srđan, Popović, Milica, "Use of monolithic supports for high-throughput protein and peptide separation in proteomics" in Electrophoresis, 38, no. 22-23 (2017):2851-2869,
https://doi.org/10.1002/elps.201700260 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Šrajer Gajdošik, Martina
AU  - Gašo-Sokač, Dajana
AU  - Martinović, Tamara
AU  - Josić, Đuro
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2156
AB  - The power of foodomics as a discipline that is now broadly used for quality assurance of food products and adulteration identifi cation, as well as for determining the safety of food, is presented. Concerning sample preparation and application, maintenance of highly sophisticated instruments for both high-performance and high-throughput techniques, and analysis and data interpretation, special att ention has to be paid to the development of skilled analysts. The obtained data shall be integrated under a strong bioinformatics environment. Modern mass spectrometry is an extremely powerful analytical tool since it can provide direct qualitative and quantitative information about a molecule of interest from only a minute amount of sample. Quality of this information is infl uenced by the sample preparation procedure, the type of mass spectrometer used and the analyst's skills. Technical advances are bringing new instruments of increased sensitivity, resolution and speed to the market. Other methods presented here give additional information and can be used as complementary tools to mass spectrometry or for validation of obtained results. Genomics and transcriptomics, as well as affi nity-based methods, still have a broad use in food analysis. Serious drawbacks of some of them, especially the affi nity-based methods, are the cross-reactivity between similar molecules and the infl uence of complex food matrices. However, these techniques can be used for pre-screening in order to reduce the large number of samples. Great progress has been made in the application of bioinformatics in foodomics. These developments enabled processing of large amounts of generated data for both identifi cation and quantifi cation, and for corresponding modeling.
PB  - University of Zagreb
T2  - Food Technology and Biotechnology
T1  - Foodomics and Food Safety: Where We Are
VL  - 55
IS  - 3
SP  - 290
EP  - 307
DO  - 10.17113/ftb.55.03.17.5044
ER  - 

@article{
author = "Anđelković, Uroš and Šrajer Gajdošik, Martina and Gašo-Sokač, Dajana and Martinović, Tamara and Josić, Đuro",
year = "2017",
abstract = "The power of foodomics as a discipline that is now broadly used for quality assurance of food products and adulteration identifi cation, as well as for determining the safety of food, is presented. Concerning sample preparation and application, maintenance of highly sophisticated instruments for both high-performance and high-throughput techniques, and analysis and data interpretation, special att ention has to be paid to the development of skilled analysts. The obtained data shall be integrated under a strong bioinformatics environment. Modern mass spectrometry is an extremely powerful analytical tool since it can provide direct qualitative and quantitative information about a molecule of interest from only a minute amount of sample. Quality of this information is infl uenced by the sample preparation procedure, the type of mass spectrometer used and the analyst's skills. Technical advances are bringing new instruments of increased sensitivity, resolution and speed to the market. Other methods presented here give additional information and can be used as complementary tools to mass spectrometry or for validation of obtained results. Genomics and transcriptomics, as well as affi nity-based methods, still have a broad use in food analysis. Serious drawbacks of some of them, especially the affi nity-based methods, are the cross-reactivity between similar molecules and the infl uence of complex food matrices. However, these techniques can be used for pre-screening in order to reduce the large number of samples. Great progress has been made in the application of bioinformatics in foodomics. These developments enabled processing of large amounts of generated data for both identifi cation and quantifi cation, and for corresponding modeling.",
publisher = "University of Zagreb",
journal = "Food Technology and Biotechnology",
title = "Foodomics and Food Safety: Where We Are",
volume = "55",
number = "3",
pages = "290-307",
doi = "10.17113/ftb.55.03.17.5044"
}

Anđelković, U., Šrajer Gajdošik, M., Gašo-Sokač, D., Martinović, T.,& Josić, Đ.. (2017). Foodomics and Food Safety: Where We Are. in Food Technology and Biotechnology
University of Zagreb., 55(3), 290-307.
https://doi.org/10.17113/ftb.55.03.17.5044

Anđelković U, Šrajer Gajdošik M, Gašo-Sokač D, Martinović T, Josić Đ. Foodomics and Food Safety: Where We Are. in Food Technology and Biotechnology. 2017;55(3):290-307.
doi:10.17113/ftb.55.03.17.5044 .

Anđelković, Uroš, Šrajer Gajdošik, Martina, Gašo-Sokač, Dajana, Martinović, Tamara, Josić, Đuro, "Foodomics and Food Safety: Where We Are" in Food Technology and Biotechnology, 55, no. 3 (2017):290-307,
https://doi.org/10.17113/ftb.55.03.17.5044 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Tufegdžić, Srđan
AU  - Popović, Milica
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2985
AB  - The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.
PB  - Wiley, Hoboken
T2  - Electrophoresis
T1  - Use of monolithic supports for high-throughput protein and peptide separation in proteomics
VL  - 38
IS  - 22-23
SP  - 2851
EP  - 2869
DO  - 10.1002/elps.201700260
ER  - 

@article{
author = "Anđelković, Uroš and Tufegdžić, Srđan and Popović, Milica",
year = "2017",
abstract = "The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.",
publisher = "Wiley, Hoboken",
journal = "Electrophoresis",
title = "Use of monolithic supports for high-throughput protein and peptide separation in proteomics",
volume = "38",
number = "22-23",
pages = "2851-2869",
doi = "10.1002/elps.201700260"
}

Anđelković, U., Tufegdžić, S.,& Popović, M.. (2017). Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis
Wiley, Hoboken., 38(22-23), 2851-2869.
https://doi.org/10.1002/elps.201700260

Anđelković U, Tufegdžić S, Popović M. Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis. 2017;38(22-23):2851-2869.
doi:10.1002/elps.201700260 .

Anđelković, Uroš, Tufegdžić, Srđan, Popović, Milica, "Use of monolithic supports for high-throughput protein and peptide separation in proteomics" in Electrophoresis, 38, no. 22-23 (2017):2851-2869,
https://doi.org/10.1002/elps.201700260 . .

TY  - CHAP
AU  - Anđelković, Uroš
AU  - Giacometti, Jasminka
AU  - Josić, Đuro
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4233
AB  - Since the introduction of suitable, highly porous supports and later nonporous and monolithic supports, chromatography has been an indispensibleindispensable method for protein separations on the analytical and preparative scales. The most frequently used methods for protein chromatography are ion exchange, reversed- phase, hydrophobic hydrophobic-interaction chromatography, chromatography on hydroxyapatite and different types of affinity, and pseudo-affinity chromatography. Because of the use of organic solvents during the separation in reversed-phase chromatography, denaturation and loss of biological activity frequently occurs, and this method is less suitable for the separation of biologically active, therapeutic proteins. Chromatography on monolithic supports and chromatography in the displacement mode offer additional opportunities for fast, highly effective separation of proteins on both the analytical and preparative scales.
PB  - Elsevier
T2  - Liquid Chromatography: Applications
T1  - Protein and Peptide Separations
VL  - 2
SP  - 107
EP  - 157
DO  - 10.1016/B978-0-12-805392-8.00005-0
ER  - 

@inbook{
author = "Anđelković, Uroš and Giacometti, Jasminka and Josić, Đuro",
year = "2017",
abstract = "Since the introduction of suitable, highly porous supports and later nonporous and monolithic supports, chromatography has been an indispensibleindispensable method for protein separations on the analytical and preparative scales. The most frequently used methods for protein chromatography are ion exchange, reversed- phase, hydrophobic hydrophobic-interaction chromatography, chromatography on hydroxyapatite and different types of affinity, and pseudo-affinity chromatography. Because of the use of organic solvents during the separation in reversed-phase chromatography, denaturation and loss of biological activity frequently occurs, and this method is less suitable for the separation of biologically active, therapeutic proteins. Chromatography on monolithic supports and chromatography in the displacement mode offer additional opportunities for fast, highly effective separation of proteins on both the analytical and preparative scales.",
publisher = "Elsevier",
journal = "Liquid Chromatography: Applications",
booktitle = "Protein and Peptide Separations",
volume = "2",
pages = "107-157",
doi = "10.1016/B978-0-12-805392-8.00005-0"
}

Anđelković, U., Giacometti, J.,& Josić, Đ.. (2017). Protein and Peptide Separations. in Liquid Chromatography: Applications
Elsevier., 2, 107-157.
https://doi.org/10.1016/B978-0-12-805392-8.00005-0

Anđelković U, Giacometti J, Josić Đ. Protein and Peptide Separations. in Liquid Chromatography: Applications. 2017;2:107-157.
doi:10.1016/B978-0-12-805392-8.00005-0 .

Anđelković, Uroš, Giacometti, Jasminka, Josić, Đuro, "Protein and Peptide Separations" in Liquid Chromatography: Applications, 2 (2017):107-157,
https://doi.org/10.1016/B978-0-12-805392-8.00005-0 . .