Stanić-Vučinić, Dragana

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Authority KeyName Variants
orcid::0000-0003-2576-3074
  • Stanić-Vučinić, Dragana (85)
  • Stanić, Dragana (14)
  • Stanić Vučinić, Dragana (1)
Projects
Molecular properties and modifications of some respiratory and nutritional allergens Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research
FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200168 (University of Belgrade, Faculty of Chemistry)
COST Action [FA 1005] Rational design and synthesis of biologically active and coordination compounds and functional materials, relevant for (bio)nanotechnology
Ispitivanje strukture i funkcije biološki važnih makromolekula u fiziološkim i patološkim stanjima CAPSIDO – Developement of the assays for detection of SARS Cov-2 virus capsid proteins in biological fluids of COVID19 patients
Ghent University Global Campus, Belgian Special Research Fund BOF StG No. 01N01718. Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200288 (Innovation Center of the Faculty of Chemistry)
Hemijske i biohemijske konsekvence metal-ligand interakcija, II. deo Serbian Academy of Sciences and Arts Project F-26.
COST Action [FA1402] Modeling and Numerical Simulations of Complex Many-Body Systems
Serbian Academy of Sciences and Arts GA No. F-26. UNDP project "Preventing and Responding to COVID-19 in At-risk areas - Sustainable production of the serological IgG test for SARS CoV-2 in Serbia".
Austrian Federal Ministry of Economy Austrian Research Promotion Agency (FFG Project) [822768]
COST Action [928] COST Action [FA1005]
COST Actions [928, FA1005] Ghent University Global Campus, Belgian Special Research Fund (BOF) [StG no. 01N01718].
Immunomodulatory effects of environmental xenobiotics and biotic factors on the populations of mouse-like rodents Razvoj novih terapijskih postupaka u prevenciji i lečenju bolesti jetre: Uloga i mehanizam delovanja polinezasićenih masnih kiselina
Laura Bassi Centers of Expertise program MEST, MEST-CT-2005-020924
Serbian Academy of Sciences and Arts, grant number F-26. Serbian Academy of Sciences and Arts [project no. F-26].
Stockholm County Council Swedish Research Council

Author's Bibliography

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

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

(Bentham Science, 2022)

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

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

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

(Bentham Science, 2022)

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

Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain

Simović, Ana; Radomirović, Mirjana; Gligorijević, Nikola; Stanić Vučinić, Dragana; Minić, Simeon; Nikolić, Milan; Ćirković-Veličković, Tanja

(Faculty of Chemistry, Serbian Biochemical Society, 2022)

TY  - CONF
AU  - Simović, Ana
AU  - Radomirović, Mirjana
AU  - Gligorijević, Nikola
AU  - Stanić Vučinić, Dragana
AU  - Minić, Simeon
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5520
AB  - The emergence of the coronavirus SARS-CoV-2 has attracted attention of the whole scientific community. The SARS-CoV-2 spike (S) protein plays the most important role in viral attachment to host receptor angiotensin-converting enzyme 2 (ACE2), via the receptor-binding domain (RBD), fusion and entry into the host, and it serves as a target for the development of antibodies, entry inhibitors and vaccines. It has been demonstrated that phycocyanobilin (PCB), a bioactive open-chain tetrapyrrole chromophore of phycocyanin (PC), chromoprotein derived from the cyanobacterium Arthrospira platensis, can bind a plethora of different proteins, both in a noncovalent and covalent manner. This study aimed to investigate interactions of PCB with S protein and RBD respectively. Electrophoretic techniques, fluorescence spectroscopy, and inhibition of S–PCB and RBD–PCB covalent adduct formation using iodoacetamide and N-ethylmaleimide, were employed to examine interactions of PCB with S protein and RBD, while the effects of PCB binding on RBD structure were studied by CD spectroscopy. SDS-PAGE with Zn2+ staining has revealed that PCB covalently binds to both S protein and RBD, via free cysteine residues. Binding constants determined by the fluorescence quenching method were: 2.1×107 M–1 for PCB and S protein and 8.4×104 M–1 for PCB and RBD. Far-UV circular dichroism spectra showed that the binding of PCB influences RBD structure by decreasing the disordered structure content. Due to moderately strong noncovalent interactions of PCB with S protein and RBD, as well as covalent adducts formation, it may exert one of its many bioactive effects via impact on S protein binding to ACE2 receptor.
PB  - Faculty of Chemistry, Serbian Biochemical Society
C3  - Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia
T1  - Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain
SP  - 130
EP  - 131
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5520
ER  - 
@conference{
author = "Simović, Ana and Radomirović, Mirjana and Gligorijević, Nikola and Stanić Vučinić, Dragana and Minić, Simeon and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "The emergence of the coronavirus SARS-CoV-2 has attracted attention of the whole scientific community. The SARS-CoV-2 spike (S) protein plays the most important role in viral attachment to host receptor angiotensin-converting enzyme 2 (ACE2), via the receptor-binding domain (RBD), fusion and entry into the host, and it serves as a target for the development of antibodies, entry inhibitors and vaccines. It has been demonstrated that phycocyanobilin (PCB), a bioactive open-chain tetrapyrrole chromophore of phycocyanin (PC), chromoprotein derived from the cyanobacterium Arthrospira platensis, can bind a plethora of different proteins, both in a noncovalent and covalent manner. This study aimed to investigate interactions of PCB with S protein and RBD respectively. Electrophoretic techniques, fluorescence spectroscopy, and inhibition of S–PCB and RBD–PCB covalent adduct formation using iodoacetamide and N-ethylmaleimide, were employed to examine interactions of PCB with S protein and RBD, while the effects of PCB binding on RBD structure were studied by CD spectroscopy. SDS-PAGE with Zn2+ staining has revealed that PCB covalently binds to both S protein and RBD, via free cysteine residues. Binding constants determined by the fluorescence quenching method were: 2.1×107 M–1 for PCB and S protein and 8.4×104 M–1 for PCB and RBD. Far-UV circular dichroism spectra showed that the binding of PCB influences RBD structure by decreasing the disordered structure content. Due to moderately strong noncovalent interactions of PCB with S protein and RBD, as well as covalent adducts formation, it may exert one of its many bioactive effects via impact on S protein binding to ACE2 receptor.",
publisher = "Faculty of Chemistry, Serbian Biochemical Society",
journal = "Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia",
title = "Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain",
pages = "130-131",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5520"
}
Simović, A., Radomirović, M., Gligorijević, N., Stanić Vučinić, D., Minić, S., Nikolić, M.,& Ćirković-Veličković, T.. (2022). Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain. in Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia
Faculty of Chemistry, Serbian Biochemical Society., 130-131.
https://hdl.handle.net/21.15107/rcub_cherry_5520
Simović A, Radomirović M, Gligorijević N, Stanić Vučinić D, Minić S, Nikolić M, Ćirković-Veličković T. Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain. in Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia. 2022;:130-131.
https://hdl.handle.net/21.15107/rcub_cherry_5520 .
Simović, Ana, Radomirović, Mirjana, Gligorijević, Nikola, Stanić Vučinić, Dragana, Minić, Simeon, Nikolić, Milan, Ćirković-Veličković, Tanja, "Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain" in Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia (2022):130-131,
https://hdl.handle.net/21.15107/rcub_cherry_5520 .

Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein

Radomirović, Mirjana Z.; Simović, Ana S.; Udovički, Božidar D.; Krstić-Ristivojević, Maja V.; Sabljić, Ljiljana Z.; Lukić, Ivana D.; Glamočlija, Sofija Đ.; Ćujić, Danica R.; Gnjatović, Marija Lj.; Stojanović, Marijana M.; Stanić-Vučinić, Dragana; Radosavljević, Jelena; Ćirković-Veličković, Tanja

(Beograd : Srpsko hemijsko društvo, 2022)

TY  - CONF
AU  - Radomirović, Mirjana Z.
AU  - Simović, Ana S.
AU  - Udovički, Božidar D.
AU  - Krstić-Ristivojević, Maja V.
AU  - Sabljić, Ljiljana Z.
AU  - Lukić, Ivana D.
AU  - Glamočlija, Sofija Đ.
AU  - Ćujić, Danica R.
AU  - Gnjatović, Marija Lj.
AU  - Stojanović, Marijana M.
AU  - Stanić-Vučinić, Dragana
AU  - Radosavljević, Jelena
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5362
AB  - Ta na dijagnoza ljudi sa sumnjom na infekciju SARS-CoV-2 je od suštinskog zna aja zasuzbijanje globalnog širenja COVID-19. Prisustvo SARS-CoV-2 može se otkriti RT-PCRom (otkriva RNK virusa) ili detekcijom prisustva virusnih antigena u biološkim te nostimaELISA-om ili sli nom tehnikom koje koriste antitela razvijena u životinjama. Cilj studijeje bio uspostavljanje kvantitativnog testa koji se zasniva na koriš enju poliklonskih serumaza rutinsko odre ivanje koncentracije SARS-CoV-2 nukleokapsidnog proteina merenjamapsorbancije u standardnoj mikrotitarskoj plo ici sa 96 bunara. Za potrebe razvoja testaproizveden je rekombinantni N-protein i koriš en za proizvodnju antiseruma u miševima ize evima. Proizvedeni antiserumi su pre iš eni i odre en im je titar. Poliklonskiantiserumivisokog afiniteta specifi ni za N-protein koriš eni su za razvoj ELISA testa specifi nog zaovaj protein. Test se zasniva na koriš enju poliklonskih seruma miševa koji su adheriranina dno bunara mikrotitarske plo ice za hvatanje N-proteina iz uzorka. Razli itekoncentracije rekombinantnog N-proteina su koriš ene za standardnu krivu zakvantifikaciju proteina. N-protein vezan za antitela miševa je detektovan ze jimpoliklonskim serumom i anti-ze jim antitelom povezanim sa enzimom koji obezbe ujespektrofotometrijsko merenje. Uspešno smo razvili prototip ELISA testa za kvantifikacijuN-proteina sa granicom detekcije u opsegu od ng/mL. Prose na vrednost LOD za prototipELISA testa za detekciju N-proteina je 9,2 ng/mL, dok je prose na vrednost LOQ10,2 ng/mL. Pokazali smo da su proizvedeni poliklonski antiserumi pogodni za detekcijuN-proteina sa sli nim ili boljim afinitetom i specifi noš u od komercijalnih antitela.Štaviše, prototip ELISA testa se može koristiti sa zadovoljavaju om pouzdanoš u zakvantifikaciju N-proteina u uzorcima bogatim proteinima, poput ljudskih seruma.
AB  - The accurate diagnosis of people with suspected infection with the SARS-CoV-2 isessential to curb the global spread of COVID-19. The presence of SARS-CoV-2 can bedetected by RT-PCR (it detects RNA of the virus) or by the presence of viral antigens inbiological fluids in ELISA or similar techniques using antibodies developed in animals.The aim of the study was the establishment of a quantitative polyclonal sera-based test forroutine measurement of the concentration of SARS CoV-2 nucleocapsid protein usingabsorbance measurement in a standard 96-well microtiter plate. For the purposes of the testdevelopment, recombinant N protein was produced and used for the production of miceand rabbit antisera. Produced antisera were purified and titer was determined. High-affinitypolyclonal N-protein specific antisera were used for N-protein specific ELISA testdevelopment. The test is based on mice polyclonal sera adhered to microtiter plate bottomfor the capture of the N protein from the specimen. Various concentrations of therecombinant N-protein were used to generate a standard curve for protein quantification.The N-protein bound to the mice antibodies was detected with rabbit polyclonal sera andanti-rabbit antibody coupled to an enzyme that provides spectrophotometric measurement.We have successfully developed the prototype ELISA for the quantification of N-proteinwith the detection limit being in the range of ng/mL. The average LOD value for theprototype ELISA was determined to be 9.2 ng/mL, while the average LOQ value was10.2 ng/mL. We have demonstrated that produced polyclonal antisera are suitable for thedetection of N-protein with affinity and specificity similar to, or better than commercialantibodies. Furthermore, the prototype ELISA can be used with satisfactory confidence forquantification of the N-protein in protein-rich samples, similar to human sera.
PB  - Beograd : Srpsko hemijsko društvo
C3  - 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine
T1  - Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein
T1  - Development of SARS-CoV-2 N-protein specific capture ELISA
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5362
ER  - 
@conference{
author = "Radomirović, Mirjana Z. and Simović, Ana S. and Udovički, Božidar D. and Krstić-Ristivojević, Maja V. and Sabljić, Ljiljana Z. and Lukić, Ivana D. and Glamočlija, Sofija Đ. and Ćujić, Danica R. and Gnjatović, Marija Lj. and Stojanović, Marijana M. and Stanić-Vučinić, Dragana and Radosavljević, Jelena and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Ta na dijagnoza ljudi sa sumnjom na infekciju SARS-CoV-2 je od suštinskog zna aja zasuzbijanje globalnog širenja COVID-19. Prisustvo SARS-CoV-2 može se otkriti RT-PCRom (otkriva RNK virusa) ili detekcijom prisustva virusnih antigena u biološkim te nostimaELISA-om ili sli nom tehnikom koje koriste antitela razvijena u životinjama. Cilj studijeje bio uspostavljanje kvantitativnog testa koji se zasniva na koriš enju poliklonskih serumaza rutinsko odre ivanje koncentracije SARS-CoV-2 nukleokapsidnog proteina merenjamapsorbancije u standardnoj mikrotitarskoj plo ici sa 96 bunara. Za potrebe razvoja testaproizveden je rekombinantni N-protein i koriš en za proizvodnju antiseruma u miševima ize evima. Proizvedeni antiserumi su pre iš eni i odre en im je titar. Poliklonskiantiserumivisokog afiniteta specifi ni za N-protein koriš eni su za razvoj ELISA testa specifi nog zaovaj protein. Test se zasniva na koriš enju poliklonskih seruma miševa koji su adheriranina dno bunara mikrotitarske plo ice za hvatanje N-proteina iz uzorka. Razli itekoncentracije rekombinantnog N-proteina su koriš ene za standardnu krivu zakvantifikaciju proteina. N-protein vezan za antitela miševa je detektovan ze jimpoliklonskim serumom i anti-ze jim antitelom povezanim sa enzimom koji obezbe ujespektrofotometrijsko merenje. Uspešno smo razvili prototip ELISA testa za kvantifikacijuN-proteina sa granicom detekcije u opsegu od ng/mL. Prose na vrednost LOD za prototipELISA testa za detekciju N-proteina je 9,2 ng/mL, dok je prose na vrednost LOQ10,2 ng/mL. Pokazali smo da su proizvedeni poliklonski antiserumi pogodni za detekcijuN-proteina sa sli nim ili boljim afinitetom i specifi noš u od komercijalnih antitela.Štaviše, prototip ELISA testa se može koristiti sa zadovoljavaju om pouzdanoš u zakvantifikaciju N-proteina u uzorcima bogatim proteinima, poput ljudskih seruma., The accurate diagnosis of people with suspected infection with the SARS-CoV-2 isessential to curb the global spread of COVID-19. The presence of SARS-CoV-2 can bedetected by RT-PCR (it detects RNA of the virus) or by the presence of viral antigens inbiological fluids in ELISA or similar techniques using antibodies developed in animals.The aim of the study was the establishment of a quantitative polyclonal sera-based test forroutine measurement of the concentration of SARS CoV-2 nucleocapsid protein usingabsorbance measurement in a standard 96-well microtiter plate. For the purposes of the testdevelopment, recombinant N protein was produced and used for the production of miceand rabbit antisera. Produced antisera were purified and titer was determined. High-affinitypolyclonal N-protein specific antisera were used for N-protein specific ELISA testdevelopment. The test is based on mice polyclonal sera adhered to microtiter plate bottomfor the capture of the N protein from the specimen. Various concentrations of therecombinant N-protein were used to generate a standard curve for protein quantification.The N-protein bound to the mice antibodies was detected with rabbit polyclonal sera andanti-rabbit antibody coupled to an enzyme that provides spectrophotometric measurement.We have successfully developed the prototype ELISA for the quantification of N-proteinwith the detection limit being in the range of ng/mL. The average LOD value for theprototype ELISA was determined to be 9.2 ng/mL, while the average LOQ value was10.2 ng/mL. We have demonstrated that produced polyclonal antisera are suitable for thedetection of N-protein with affinity and specificity similar to, or better than commercialantibodies. Furthermore, the prototype ELISA can be used with satisfactory confidence forquantification of the N-protein in protein-rich samples, similar to human sera.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine",
title = "Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein, Development of SARS-CoV-2 N-protein specific capture ELISA",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5362"
}
Radomirović, M. Z., Simović, A. S., Udovički, B. D., Krstić-Ristivojević, M. V., Sabljić, L. Z., Lukić, I. D., Glamočlija, S. Đ., Ćujić, D. R., Gnjatović, M. Lj., Stojanović, M. M., Stanić-Vučinić, D., Radosavljević, J.,& Ćirković-Veličković, T.. (2022). Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein. in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine
Beograd : Srpsko hemijsko društvo..
https://hdl.handle.net/21.15107/rcub_cherry_5362
Radomirović MZ, Simović AS, Udovički BD, Krstić-Ristivojević MV, Sabljić LZ, Lukić ID, Glamočlija SĐ, Ćujić DR, Gnjatović ML, Stojanović MM, Stanić-Vučinić D, Radosavljević J, Ćirković-Veličković T. Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein. in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine. 2022;.
https://hdl.handle.net/21.15107/rcub_cherry_5362 .
Radomirović, Mirjana Z., Simović, Ana S., Udovički, Božidar D., Krstić-Ristivojević, Maja V., Sabljić, Ljiljana Z., Lukić, Ivana D., Glamočlija, Sofija Đ., Ćujić, Danica R., Gnjatović, Marija Lj., Stojanović, Marijana M., Stanić-Vučinić, Dragana, Radosavljević, Jelena, Ćirković-Veličković, Tanja, "Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein" in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine (2022),
https://hdl.handle.net/21.15107/rcub_cherry_5362 .

Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein

Radomirović, Mirjana Z.; Simović, Ana S.; Udovički, Božidar D.; Krstić-Ristivojević, Maja V.; Sabljić, Ljiljana Z.; Lukić, Ivana D.; Glamočlija, Sofija Đ.; Ćujić, Danica R.; Gnjatović, Marija Lj.; Stojanović, Marijana M.; Stanić-Vučinić, Dragana; Radosavljević, Jelena; Ćirković-Veličković, Tanja

(Beograd : Srpsko hemijsko društvo, 2022)

TY  - CONF
AU  - Radomirović, Mirjana Z.
AU  - Simović, Ana S.
AU  - Udovički, Božidar D.
AU  - Krstić-Ristivojević, Maja V.
AU  - Sabljić, Ljiljana Z.
AU  - Lukić, Ivana D.
AU  - Glamočlija, Sofija Đ.
AU  - Ćujić, Danica R.
AU  - Gnjatović, Marija Lj.
AU  - Stojanović, Marijana M.
AU  - Stanić-Vučinić, Dragana
AU  - Radosavljević, Jelena
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5361
AB  - Ta na dijagnoza ljudi sa sumnjom na infekciju SARS-CoV-2 je od suštinskog zna aja za
suzbijanje globalnog širenja COVID-19. Prisustvo SARS-CoV-2 može se otkriti RT-PCRom (otkriva RNK virusa) ili detekcijom prisustva virusnih antigena u biološkim te nostima
ELISA-om ili sli nom tehnikom koje koriste antitela razvijena u životinjama. Cilj studije
je bio uspostavljanje kvantitativnog testa koji se zasniva na koriš enju poliklonskih seruma
za rutinsko odre ivanje koncentracije SARS-CoV-2 nukleokapsidnog proteina merenjam
apsorbancije u standardnoj mikrotitarskoj plo ici sa 96 bunara. Za potrebe razvoja testa
proizveden je rekombinantni N-protein i koriš en za proizvodnju antiseruma u miševima i
ze evima. Proizvedeni antiserumi su pre iš eni i odre en im je titar. Poliklonskiantiserumi
visokog afiniteta specifi ni za N-protein koriš eni su za razvoj ELISA testa specifi nog za
ovaj protein. Test se zasniva na koriš enju poliklonskih seruma miševa koji su adherirani
na dno bunara mikrotitarske plo ice za hvatanje N-proteina iz uzorka. Razli ite
koncentracije rekombinantnog N-proteina su koriš ene za standardnu krivu za
kvantifikaciju proteina. N-protein vezan za antitela miševa je detektovan ze jim
poliklonskim serumom i anti-ze jim antitelom povezanim sa enzimom koji obezbe uje
spektrofotometrijsko merenje. Uspešno smo razvili prototip ELISA testa za kvantifikaciju
N-proteina sa granicom detekcije u opsegu od ng/mL. Prose na vrednost LOD za prototip
ELISA testa za detekciju N-proteina je 9,2 ng/mL, dok je prose na vrednost LOQ
10,2 ng/mL. Pokazali smo da su proizvedeni poliklonski antiserumi pogodni za detekciju
N-proteina sa sli nim ili boljim afinitetom i specifi noš u od komercijalnih antitela.
Štaviše, prototip ELISA testa se može koristiti sa zadovoljavaju om pouzdanoš u za
kvantifikaciju N-proteina u uzorcima bogatim proteinima, poput ljudskih seruma.
AB  - The accurate diagnosis of people with suspected infection with the SARS-CoV-2 is
essential to curb the global spread of COVID-19. The presence of SARS-CoV-2 can be
detected by RT-PCR (it detects RNA of the virus) or by the presence of viral antigens in
biological fluids in ELISA or similar techniques using antibodies developed in animals.
The aim of the study was the establishment of a quantitative polyclonal sera-based test for
routine measurement of the concentration of SARS CoV-2 nucleocapsid protein using
absorbance measurement in a standard 96-well microtiter plate. For the purposes of the test
development, recombinant N protein was produced and used for the production of mice
and rabbit antisera. Produced antisera were purified and titer was determined. High-affinity
polyclonal N-protein specific antisera were used for N-protein specific ELISA test
development. The test is based on mice polyclonal sera adhered to microtiter plate bottom
for the capture of the N protein from the specimen. Various concentrations of the
recombinant N-protein were used to generate a standard curve for protein quantification.
The N-protein bound to the mice antibodies was detected with rabbit polyclonal sera and
anti-rabbit antibody coupled to an enzyme that provides spectrophotometric measurement.
We have successfully developed the prototype ELISA for the quantification of N-protein
with the detection limit being in the range of ng/mL. The average LOD value for the
prototype ELISA was determined to be 9.2 ng/mL, while the average LOQ value was
10.2 ng/mL. We have demonstrated that produced polyclonal antisera are suitable for the
detection of N-protein with affinity and specificity similar to, or better than commercial
antibodies. Furthermore, the prototype ELISA can be used with satisfactory confidence for
quantification of the N-protein in protein-rich samples, similar to human sera.
PB  - Beograd : Srpsko hemijsko društvo
C3  - 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine
T1  - Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein
T1  - Development of SARS-CoV-2 N-protein specific capture ELISA
SP  - 65
EP  - 66
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5361
ER  - 
@conference{
author = "Radomirović, Mirjana Z. and Simović, Ana S. and Udovički, Božidar D. and Krstić-Ristivojević, Maja V. and Sabljić, Ljiljana Z. and Lukić, Ivana D. and Glamočlija, Sofija Đ. and Ćujić, Danica R. and Gnjatović, Marija Lj. and Stojanović, Marijana M. and Stanić-Vučinić, Dragana and Radosavljević, Jelena and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Ta na dijagnoza ljudi sa sumnjom na infekciju SARS-CoV-2 je od suštinskog zna aja za
suzbijanje globalnog širenja COVID-19. Prisustvo SARS-CoV-2 može se otkriti RT-PCRom (otkriva RNK virusa) ili detekcijom prisustva virusnih antigena u biološkim te nostima
ELISA-om ili sli nom tehnikom koje koriste antitela razvijena u životinjama. Cilj studije
je bio uspostavljanje kvantitativnog testa koji se zasniva na koriš enju poliklonskih seruma
za rutinsko odre ivanje koncentracije SARS-CoV-2 nukleokapsidnog proteina merenjam
apsorbancije u standardnoj mikrotitarskoj plo ici sa 96 bunara. Za potrebe razvoja testa
proizveden je rekombinantni N-protein i koriš en za proizvodnju antiseruma u miševima i
ze evima. Proizvedeni antiserumi su pre iš eni i odre en im je titar. Poliklonskiantiserumi
visokog afiniteta specifi ni za N-protein koriš eni su za razvoj ELISA testa specifi nog za
ovaj protein. Test se zasniva na koriš enju poliklonskih seruma miševa koji su adherirani
na dno bunara mikrotitarske plo ice za hvatanje N-proteina iz uzorka. Razli ite
koncentracije rekombinantnog N-proteina su koriš ene za standardnu krivu za
kvantifikaciju proteina. N-protein vezan za antitela miševa je detektovan ze jim
poliklonskim serumom i anti-ze jim antitelom povezanim sa enzimom koji obezbe uje
spektrofotometrijsko merenje. Uspešno smo razvili prototip ELISA testa za kvantifikaciju
N-proteina sa granicom detekcije u opsegu od ng/mL. Prose na vrednost LOD za prototip
ELISA testa za detekciju N-proteina je 9,2 ng/mL, dok je prose na vrednost LOQ
10,2 ng/mL. Pokazali smo da su proizvedeni poliklonski antiserumi pogodni za detekciju
N-proteina sa sli nim ili boljim afinitetom i specifi noš u od komercijalnih antitela.
Štaviše, prototip ELISA testa se može koristiti sa zadovoljavaju om pouzdanoš u za
kvantifikaciju N-proteina u uzorcima bogatim proteinima, poput ljudskih seruma., The accurate diagnosis of people with suspected infection with the SARS-CoV-2 is
essential to curb the global spread of COVID-19. The presence of SARS-CoV-2 can be
detected by RT-PCR (it detects RNA of the virus) or by the presence of viral antigens in
biological fluids in ELISA or similar techniques using antibodies developed in animals.
The aim of the study was the establishment of a quantitative polyclonal sera-based test for
routine measurement of the concentration of SARS CoV-2 nucleocapsid protein using
absorbance measurement in a standard 96-well microtiter plate. For the purposes of the test
development, recombinant N protein was produced and used for the production of mice
and rabbit antisera. Produced antisera were purified and titer was determined. High-affinity
polyclonal N-protein specific antisera were used for N-protein specific ELISA test
development. The test is based on mice polyclonal sera adhered to microtiter plate bottom
for the capture of the N protein from the specimen. Various concentrations of the
recombinant N-protein were used to generate a standard curve for protein quantification.
The N-protein bound to the mice antibodies was detected with rabbit polyclonal sera and
anti-rabbit antibody coupled to an enzyme that provides spectrophotometric measurement.
We have successfully developed the prototype ELISA for the quantification of N-protein
with the detection limit being in the range of ng/mL. The average LOD value for the
prototype ELISA was determined to be 9.2 ng/mL, while the average LOQ value was
10.2 ng/mL. We have demonstrated that produced polyclonal antisera are suitable for the
detection of N-protein with affinity and specificity similar to, or better than commercial
antibodies. Furthermore, the prototype ELISA can be used with satisfactory confidence for
quantification of the N-protein in protein-rich samples, similar to human sera.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine",
title = "Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein, Development of SARS-CoV-2 N-protein specific capture ELISA",
pages = "65-66",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5361"
}
Radomirović, M. Z., Simović, A. S., Udovički, B. D., Krstić-Ristivojević, M. V., Sabljić, L. Z., Lukić, I. D., Glamočlija, S. Đ., Ćujić, D. R., Gnjatović, M. Lj., Stojanović, M. M., Stanić-Vučinić, D., Radosavljević, J.,& Ćirković-Veličković, T.. (2022). Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein. in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine
Beograd : Srpsko hemijsko društvo., 65-66.
https://hdl.handle.net/21.15107/rcub_cherry_5361
Radomirović MZ, Simović AS, Udovički BD, Krstić-Ristivojević MV, Sabljić LZ, Lukić ID, Glamočlija SĐ, Ćujić DR, Gnjatović ML, Stojanović MM, Stanić-Vučinić D, Radosavljević J, Ćirković-Veličković T. Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein. in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine. 2022;:65-66.
https://hdl.handle.net/21.15107/rcub_cherry_5361 .
Radomirović, Mirjana Z., Simović, Ana S., Udovički, Božidar D., Krstić-Ristivojević, Maja V., Sabljić, Ljiljana Z., Lukić, Ivana D., Glamočlija, Sofija Đ., Ćujić, Danica R., Gnjatović, Marija Lj., Stojanović, Marijana M., Stanić-Vučinić, Dragana, Radosavljević, Jelena, Ćirković-Veličković, Tanja, "Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein" in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine (2022):65-66,
https://hdl.handle.net/21.15107/rcub_cherry_5361 .

Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating

Radomirović, Mirjana Ž.; Minić, Simeon L.; Stanić-Vučinić, Dragana; Nikolić, Milan; Van Haute, Sam; Rajković, Andreja; Ćirković-Veličković, Tanja

(Elsevier, 2022)

TY  - JOUR
AU  - Radomirović, Mirjana Ž.
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Van Haute, Sam
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4863
AB  - β-lactoglobulin (BLG) is a major whey protein with numerous techno-functional properties desirable for the food industry. Phycocyanobilin (PCB), a bioactive pigment of Arthrospira platensis with health-promoting effects, covalently binds to BLG at physiological pH. This study investigated the effects of this covalent modification on BLG functional properties. The BLG–PCB adduct possesses enhanced antioxidant properties, and bound PCB protects BLG against free radical-induced oxidation. Despite the similar thermal stabilities of BLG and BLG–PCB, BLG–PCB is less susceptible to covalent and noncovalent aggregation under moderate heat treatment (63 °C, 30 min). Blocked thiol group and reduced hydrophobicity due to hindering of hydrophobic residues by bound PCB, as well as the heat-induced transition of β-sheet to α-helix, contributed to the low susceptibility of BLG–PCB to aggregation. BLG–PCB has a higher resistance to pepsin and pancreatin digestion than BLG and unaltered IgE-binding properties. The improved functional properties of BLG–PCB make it a useful ingredient in the food industry.
PB  - Elsevier
T2  - Food Hydrocolloids
T1  - Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating
VL  - 123
SP  - 107169
DO  - 10.1016/j.foodhyd.2021.107169
ER  - 
@article{
author = "Radomirović, Mirjana Ž. and Minić, Simeon L. and Stanić-Vučinić, Dragana and Nikolić, Milan and Van Haute, Sam and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "β-lactoglobulin (BLG) is a major whey protein with numerous techno-functional properties desirable for the food industry. Phycocyanobilin (PCB), a bioactive pigment of Arthrospira platensis with health-promoting effects, covalently binds to BLG at physiological pH. This study investigated the effects of this covalent modification on BLG functional properties. The BLG–PCB adduct possesses enhanced antioxidant properties, and bound PCB protects BLG against free radical-induced oxidation. Despite the similar thermal stabilities of BLG and BLG–PCB, BLG–PCB is less susceptible to covalent and noncovalent aggregation under moderate heat treatment (63 °C, 30 min). Blocked thiol group and reduced hydrophobicity due to hindering of hydrophobic residues by bound PCB, as well as the heat-induced transition of β-sheet to α-helix, contributed to the low susceptibility of BLG–PCB to aggregation. BLG–PCB has a higher resistance to pepsin and pancreatin digestion than BLG and unaltered IgE-binding properties. The improved functional properties of BLG–PCB make it a useful ingredient in the food industry.",
publisher = "Elsevier",
journal = "Food Hydrocolloids",
title = "Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating",
volume = "123",
pages = "107169",
doi = "10.1016/j.foodhyd.2021.107169"
}
Radomirović, M. Ž., Minić, S. L., Stanić-Vučinić, D., Nikolić, M., Van Haute, S., Rajković, A.,& Ćirković-Veličković, T.. (2022). Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating. in Food Hydrocolloids
Elsevier., 123, 107169.
https://doi.org/10.1016/j.foodhyd.2021.107169
Radomirović MŽ, Minić SL, Stanić-Vučinić D, Nikolić M, Van Haute S, Rajković A, Ćirković-Veličković T. Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating. in Food Hydrocolloids. 2022;123:107169.
doi:10.1016/j.foodhyd.2021.107169 .
Radomirović, Mirjana Ž., Minić, Simeon L., Stanić-Vučinić, Dragana, Nikolić, Milan, Van Haute, Sam, Rajković, Andreja, Ćirković-Veličković, Tanja, "Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating" in Food Hydrocolloids, 123 (2022):107169,
https://doi.org/10.1016/j.foodhyd.2021.107169 . .
2
6
4

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

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

(Elsevier, 2021)

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

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

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

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

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

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

Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection.",
publisher = "Elsevier",
journal = "Virology journal",
title = "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2",
volume = "557",
pages = "15-22",
doi = "10.1016/j.virol.2021.01.004"
}
Đukić, T., Mladenović, M., Stanić-Vučinić, D., Radosavljević, J., Smiljanić, K., Sabljić, L., Dević, M., Ćujić, D., Vasović, T., Simović, A., Radomirović, M. Ž.,& Ćirković-Veličković, T.. (2021). Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2. in Virology journal
Elsevier., 557, 15-22.
https://doi.org/10.1016/j.virol.2021.01.004
Đukić T, Mladenović M, Stanić-Vučinić D, Radosavljević J, Smiljanić K, Sabljić L, Dević M, Ćujić D, Vasović T, Simović A, Radomirović MŽ, Ćirković-Veličković T. Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2. in Virology journal. 2021;557:15-22.
doi:10.1016/j.virol.2021.01.004 .
Đukić, Teodora, Mladenović, Maja, Stanić-Vučinić, Dragana, Radosavljević, Jelena, Smiljanić, Katarina, Sabljić, Ljiljana, Dević, Marija, Ćujić, Danica, Vasović, Tamara, Simović, Ana, Radomirović, Mirjana Ž., Ćirković-Veličković, Tanja, "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2" in Virology journal, 557 (2021):15-22,
https://doi.org/10.1016/j.virol.2021.01.004 . .
5
10
8
8

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

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

(Elsevier, 2021)

TY  - JOUR
AU  - Đukić, Teodora
AU  - Mladenović, Maja
AU  - Stanić-Vučinić, Dragana
AU  - Radosavljević, Jelena
AU  - Smiljanić, Katarina
AU  - Sabljić, Ljiljana
AU  - Dević, Marija
AU  - Ćujić, Danica
AU  - Vasović, Tamara
AU  - Simović, Ana
AU  - Radomirović, Mirjana Ž.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4331
AB  - Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production.SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified and characterized biochemically and immunologically.Purified rfNP has secondary structure of full-length recombinant N protein, with high percentage of disordered structure (34.2%) and of β-sheet (40.7%). rfNP was tested in immunoblot using sera of COVID-19 convalescent patients. ELISA was optimized with sera of RT-PCR confirmed positive symptomatic patients and healthy individuals. IgG detection sensitivity was 96% (47/50) and specificity 97% (67/68), while IgM detection was slightly lower (94% and 96.5%, respectively).Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection.
PB  - Elsevier
T2  - Virology journal
T1  - Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2
VL  - 557
SP  - 15
EP  - 22
DO  - 10.1016/j.virol.2021.01.004
ER  - 
@article{
author = "Đukić, Teodora and Mladenović, Maja and Stanić-Vučinić, Dragana and Radosavljević, Jelena and Smiljanić, Katarina and Sabljić, Ljiljana and Dević, Marija and Ćujić, Danica and Vasović, Tamara and Simović, Ana and Radomirović, Mirjana Ž. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production.SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified and characterized biochemically and immunologically.Purified rfNP has secondary structure of full-length recombinant N protein, with high percentage of disordered structure (34.2%) and of β-sheet (40.7%). rfNP was tested in immunoblot using sera of COVID-19 convalescent patients. ELISA was optimized with sera of RT-PCR confirmed positive symptomatic patients and healthy individuals. IgG detection sensitivity was 96% (47/50) and specificity 97% (67/68), while IgM detection was slightly lower (94% and 96.5%, respectively).Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection.",
publisher = "Elsevier",
journal = "Virology journal",
title = "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2",
volume = "557",
pages = "15-22",
doi = "10.1016/j.virol.2021.01.004"
}
Đukić, T., Mladenović, M., Stanić-Vučinić, D., Radosavljević, J., Smiljanić, K., Sabljić, L., Dević, M., Ćujić, D., Vasović, T., Simović, A., Radomirović, M. Ž.,& Ćirković-Veličković, T.. (2021). Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2. in Virology journal
Elsevier., 557, 15-22.
https://doi.org/10.1016/j.virol.2021.01.004
Đukić T, Mladenović M, Stanić-Vučinić D, Radosavljević J, Smiljanić K, Sabljić L, Dević M, Ćujić D, Vasović T, Simović A, Radomirović MŽ, Ćirković-Veličković T. Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2. in Virology journal. 2021;557:15-22.
doi:10.1016/j.virol.2021.01.004 .
Đukić, Teodora, Mladenović, Maja, Stanić-Vučinić, Dragana, Radosavljević, Jelena, Smiljanić, Katarina, Sabljić, Ljiljana, Dević, Marija, Ćujić, Danica, Vasović, Tamara, Simović, Ana, Radomirović, Mirjana Ž., Ćirković-Veličković, Tanja, "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2" in Virology journal, 557 (2021):15-22,
https://doi.org/10.1016/j.virol.2021.01.004 . .
5
10
8
8

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

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

(Elsevier, 2021)

TY  - JOUR
AU  - Peruško, Marija
AU  - Ghnimi, Sami
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Radomirović, Mirjana Ž.
AU  - Gharsallaoui, Adem
AU  - Smiljanić, Katarina
AU  - Van Haute, Sam
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4332
AB  - Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.
PB  - Elsevier
T2  - LWT
T1  - Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying
VL  - 143
SP  - 111091
DO  - 10.1016/j.lwt.2021.111091
ER  - 
@article{
author = "Peruško, Marija and Ghnimi, Sami and Simović, Ana and Stevanović, Nikola R. and Radomirović, Mirjana Ž. and Gharsallaoui, Adem and Smiljanić, Katarina and Van Haute, Sam and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.",
publisher = "Elsevier",
journal = "LWT",
title = "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying",
volume = "143",
pages = "111091",
doi = "10.1016/j.lwt.2021.111091"
}
Peruško, M., Ghnimi, S., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Gharsallaoui, A., Smiljanić, K., Van Haute, S., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT
Elsevier., 143, 111091.
https://doi.org/10.1016/j.lwt.2021.111091
Peruško M, Ghnimi S, Simović A, Stevanović NR, Radomirović MŽ, Gharsallaoui A, Smiljanić K, Van Haute S, Stanić-Vučinić D, Ćirković-Veličković T. Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT. 2021;143:111091.
doi:10.1016/j.lwt.2021.111091 .
Peruško, Marija, Ghnimi, Sami, Simović, Ana, Stevanović, Nikola R., Radomirović, Mirjana Ž., Gharsallaoui, Adem, Smiljanić, Katarina, Van Haute, Sam, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying" in LWT, 143 (2021):111091,
https://doi.org/10.1016/j.lwt.2021.111091 . .
1
10
2
9

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

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

(Elsevier, 2021)

TY  - JOUR
AU  - Peruško, Marija
AU  - Ghnimi, Sami
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Radomirović, Mirjana Ž.
AU  - Gharsallaoui, Adem
AU  - Smiljanić, Katarina
AU  - Van Haute, Sam
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4333
AB  - Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.
PB  - Elsevier
T2  - LWT
T1  - Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying
VL  - 143
SP  - 111091
DO  - 10.1016/j.lwt.2021.111091
ER  - 
@article{
author = "Peruško, Marija and Ghnimi, Sami and Simović, Ana and Stevanović, Nikola R. and Radomirović, Mirjana Ž. and Gharsallaoui, Adem and Smiljanić, Katarina and Van Haute, Sam and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.",
publisher = "Elsevier",
journal = "LWT",
title = "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying",
volume = "143",
pages = "111091",
doi = "10.1016/j.lwt.2021.111091"
}
Peruško, M., Ghnimi, S., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Gharsallaoui, A., Smiljanić, K., Van Haute, S., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT
Elsevier., 143, 111091.
https://doi.org/10.1016/j.lwt.2021.111091
Peruško M, Ghnimi S, Simović A, Stevanović NR, Radomirović MŽ, Gharsallaoui A, Smiljanić K, Van Haute S, Stanić-Vučinić D, Ćirković-Veličković T. Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT. 2021;143:111091.
doi:10.1016/j.lwt.2021.111091 .
Peruško, Marija, Ghnimi, Sami, Simović, Ana, Stevanović, Nikola R., Radomirović, Mirjana Ž., Gharsallaoui, Adem, Smiljanić, Katarina, Van Haute, Sam, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying" in LWT, 143 (2021):111091,
https://doi.org/10.1016/j.lwt.2021.111091 . .
1
10
2
9

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

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

(Elsevier, 2021)

TY  - DATA
AU  - Peruško, Marija
AU  - Ghnimi, Sami
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Radomirović, Mirjana Ž.
AU  - Gharsallaoui, Adem
AU  - Smiljanić, Katarina
AU  - Van Haute, Sam
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4334
PB  - Elsevier
T2  - LWT
T1  - Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4334
ER  - 
@misc{
author = "Peruško, Marija and Ghnimi, Sami and Simović, Ana and Stevanović, Nikola R. and Radomirović, Mirjana Ž. and Gharsallaoui, Adem and Smiljanić, Katarina and Van Haute, Sam and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
publisher = "Elsevier",
journal = "LWT",
title = "Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4334"
}
Peruško, M., Ghnimi, S., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Gharsallaoui, A., Smiljanić, K., Van Haute, S., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.. in LWT
Elsevier..
https://hdl.handle.net/21.15107/rcub_cherry_4334
Peruško M, Ghnimi S, Simović A, Stevanović NR, Radomirović MŽ, Gharsallaoui A, Smiljanić K, Van Haute S, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.. in LWT. 2021;.
https://hdl.handle.net/21.15107/rcub_cherry_4334 .
Peruško, Marija, Ghnimi, Sami, Simović, Ana, Stevanović, Nikola R., Radomirović, Mirjana Ž., Gharsallaoui, Adem, Smiljanić, Katarina, Van Haute, Sam, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091." in LWT (2021),
https://hdl.handle.net/21.15107/rcub_cherry_4334 .

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

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

(MDPI, 2021)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana Ž.
AU  - Stojadinović, Marija M.
AU  - Khulal, Urmila
AU  - Nedić, Olgica
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://www.mdpi.com/1420-3049/26/10/2834
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4552
AB  - Resveratrol is a phytoalexin produced by many plants as a defense mechanism against stress-inducing conditions. The richest dietary sources of resveratrol are berries and grapes, their juices and wines. Good bioavailability of resveratrol is not reflected in its high biological activity in vivo because of resveratrol isomerization and its poor solubility in aqueous solutions. Proteins, cyclodextrins and nanomaterials have been explored as innovative delivery vehicles for resveratrol to overcome this limitation. Numerous in vitro and in vivo studies demonstrated beneficial effects of resveratrol in cardiovascular diseases (CVD). Main beneficial effects of resveratrol intake are cardioprotective, anti-hypertensive, vasodilatory, anti-diabetic, and improvement of lipid status. As resveratrol can alleviate the numerous factors associated with CVD, it has potential as a functional supplement to reduce COVID-19 illness severity in patients displaying poor prognosis due to cardio-vascular complications. Resveratrol was shown to mitigate the major pathways involved in the pathogenesis of SARS-CoV-2 including regulation of the renin-angiotensin system and expression of angiotensin-converting enzyme 2, stimulation of immune system and downregulation of pro-inflammatory cytokine release. Therefore, several studies already have anticipated potential implementation of resveratrol in COVID-19 treatment. Regular intake of a resveratrol rich diet, or resveratrol-based complementary medicaments, may contribute to a healthier cardio-vascular system, prevention and control of CVD, including COVID-19 disease related complications of CVD.
PB  - MDPI
T2  - Molecules
T1  - Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability
VL  - 26
IS  - 10
SP  - 2834
DO  - 10.3390/molecules26102834
ER  - 
@article{
author = "Gligorijević, Nikola and Stanić-Vučinić, Dragana and Radomirović, Mirjana Ž. and Stojadinović, Marija M. and Khulal, Urmila and Nedić, Olgica and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Resveratrol is a phytoalexin produced by many plants as a defense mechanism against stress-inducing conditions. The richest dietary sources of resveratrol are berries and grapes, their juices and wines. Good bioavailability of resveratrol is not reflected in its high biological activity in vivo because of resveratrol isomerization and its poor solubility in aqueous solutions. Proteins, cyclodextrins and nanomaterials have been explored as innovative delivery vehicles for resveratrol to overcome this limitation. Numerous in vitro and in vivo studies demonstrated beneficial effects of resveratrol in cardiovascular diseases (CVD). Main beneficial effects of resveratrol intake are cardioprotective, anti-hypertensive, vasodilatory, anti-diabetic, and improvement of lipid status. As resveratrol can alleviate the numerous factors associated with CVD, it has potential as a functional supplement to reduce COVID-19 illness severity in patients displaying poor prognosis due to cardio-vascular complications. Resveratrol was shown to mitigate the major pathways involved in the pathogenesis of SARS-CoV-2 including regulation of the renin-angiotensin system and expression of angiotensin-converting enzyme 2, stimulation of immune system and downregulation of pro-inflammatory cytokine release. Therefore, several studies already have anticipated potential implementation of resveratrol in COVID-19 treatment. Regular intake of a resveratrol rich diet, or resveratrol-based complementary medicaments, may contribute to a healthier cardio-vascular system, prevention and control of CVD, including COVID-19 disease related complications of CVD.",
publisher = "MDPI",
journal = "Molecules",
title = "Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability",
volume = "26",
number = "10",
pages = "2834",
doi = "10.3390/molecules26102834"
}
Gligorijević, N., Stanić-Vučinić, D., Radomirović, M. Ž., Stojadinović, M. M., Khulal, U., Nedić, O.,& Ćirković-Veličković, T.. (2021). Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability. in Molecules
MDPI., 26(10), 2834.
https://doi.org/10.3390/molecules26102834
Gligorijević N, Stanić-Vučinić D, Radomirović MŽ, Stojadinović MM, Khulal U, Nedić O, Ćirković-Veličković T. Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability. in Molecules. 2021;26(10):2834.
doi:10.3390/molecules26102834 .
Gligorijević, Nikola, Stanić-Vučinić, Dragana, Radomirović, Mirjana Ž., Stojadinović, Marija M., Khulal, Urmila, Nedić, Olgica, Ćirković-Veličković, Tanja, "Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability" in Molecules, 26, no. 10 (2021):2834,
https://doi.org/10.3390/molecules26102834 . .
10
5
9

Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention

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

(MDPI, 2021)

TY  - JOUR
AU  - Gligorijevic, Nikola
AU  - Radomirović, Mirjana Ž.
AU  - Nedić, Olgica
AU  - Stojadinović, Marija M.
AU  - Khulal, Urmila
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4784
AB  - The worldwide outbreak of COVID-19 was caused by a pathogenic virus called Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2). Therapies against SARS-CoV-2 target the virus or human cells or the immune system. However, therapies based on specific antibodies, such as vaccines and monoclonal antibodies, may become inefficient enough when the virus changes its antigenicity due to mutations. Polyphenols are the major class of bioactive compounds in nature, exerting diverse health effects based on their direct antioxidant activity and their effects in the modulation of intracellular signaling. There are currently numerous clinical trials investigating the effects of polyphenols in prophylaxis and the treatment of COVID-19, from symptomatic, via moderate and severe COVID-19 treatment, to anti-fibrotic treatment in discharged COVID-19 patients. Antiviral activities of polyphenols and their impact on immune system modulation could serve as a solid basis for developing polyphenol-based natural approaches for preventing and treating COVID-19.
PB  - MDPI
T2  - International Journal of Molecular Sciences
T1  - Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention
VL  - 22
IS  - 22
SP  - 12385
DO  - 10.3390/ijms222212385
ER  - 
@article{
author = "Gligorijevic, Nikola and Radomirović, Mirjana Ž. and Nedić, Olgica and Stojadinović, Marija M. and Khulal, Urmila and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "The worldwide outbreak of COVID-19 was caused by a pathogenic virus called Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2). Therapies against SARS-CoV-2 target the virus or human cells or the immune system. However, therapies based on specific antibodies, such as vaccines and monoclonal antibodies, may become inefficient enough when the virus changes its antigenicity due to mutations. Polyphenols are the major class of bioactive compounds in nature, exerting diverse health effects based on their direct antioxidant activity and their effects in the modulation of intracellular signaling. There are currently numerous clinical trials investigating the effects of polyphenols in prophylaxis and the treatment of COVID-19, from symptomatic, via moderate and severe COVID-19 treatment, to anti-fibrotic treatment in discharged COVID-19 patients. Antiviral activities of polyphenols and their impact on immune system modulation could serve as a solid basis for developing polyphenol-based natural approaches for preventing and treating COVID-19.",
publisher = "MDPI",
journal = "International Journal of Molecular Sciences",
title = "Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention",
volume = "22",
number = "22",
pages = "12385",
doi = "10.3390/ijms222212385"
}
Gligorijevic, N., Radomirović, M. Ž., Nedić, O., Stojadinović, M. M., Khulal, U., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention. in International Journal of Molecular Sciences
MDPI., 22(22), 12385.
https://doi.org/10.3390/ijms222212385
Gligorijevic N, Radomirović MŽ, Nedić O, Stojadinović MM, Khulal U, Stanić-Vučinić D, Ćirković-Veličković T. Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention. in International Journal of Molecular Sciences. 2021;22(22):12385.
doi:10.3390/ijms222212385 .
Gligorijevic, Nikola, Radomirović, Mirjana Ž., Nedić, Olgica, Stojadinović, Marija M., Khulal, Urmila, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention" in International Journal of Molecular Sciences, 22, no. 22 (2021):12385,
https://doi.org/10.3390/ijms222212385 . .
1
4
4

Interaction of SARS-CoV-2 Spike protein with phycocyanobilin

Simović, Ana; Radomirović, Mirjana Ž.; Gligorijević, Nikola; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Sociedade Portuguesa de Química, 2021)

TY  - CONF
AU  - Simović, Ana
AU  - Radomirović, Mirjana Ž.
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5132
AB  - Algae have been consumed as food and medicine for centuries. Their benefits are so pronounced, due to high concentrations of vitamins, minerals, antioxidants and proteins that they are commonly referred to as superfoods. Phycocyanobilin (PCB) is a bioactive compound of microalga Spirulina platensis. It is a blue tetrapyrrole chromophore of C-phycocyanin (C-PC), the major chromoprotein of this microalga. It is covalently attached to cysteine residues of C-PC via thioether bond. The outbreak of Coronavirus Disease 2019 (COVID-19) has posed a serious threat to global public health, calling for the development of safe and effective prophylactics and therapeutics against infection of its causative agent, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The SARS-CoV-2 spike (S) protein plays the most important roles in viral attachment, fusion and entry, and it serves as a target for development of antibodies, entry inhibitors and vaccines. It mediates viral entry into host cells by first binding to a host angiotensin-converting enzyme 2 (ACE2) receptor through the receptor-binding domain (RBD) and then fusing the viral and host membranes. This study aimed to investigate interaction of bioactive PCB with S protein and RBD respectively.
Combination of electrophoretic techniques and fluorescence spectroscopy was employed in order to examine interactions of PCB and S protein, as well as interactions of PCB and RBD, while the effects of PCB binding on RBD structure were studied by CD spectroscopy.
SDS-PAGE with Zn2+ staining has revealed that PCB covalently binds to both S protein and RBD, via free cysteine residues. Binding constants determined by fluorescence quenching method were: 2.1 x 107 M–1 for PCB and S protein, and 8.4 x 104 M–1 for PCB and RBD. Far-UV circular dichroism spectra showed that PCB influences RBD structure.
Our results support the importance of further research on covalent binding of PCB to S protein and RBD and its implications. Due to its interaction with S protein and RBD, PCB may exert one of its many bioactive effects via impact on S protein binding to ACE2 receptor.
Acknowledgments: This project has received funding from the European Union’s Horizon 2020 research and innovation program under grant agreement No. 810752.
References:
[1] S. Minic, M. Radomirovic, N. Savkovic et al., Food Chemistry, 269(2018) 43-52.
[2] W. Tai, L. He, X. Zhang et al., Cellular & Molecular Immunology, 17(2020) 613-620.
PB  - Sociedade Portuguesa de Química
C3  - Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference
T1  - Interaction of SARS-CoV-2 Spike protein with phycocyanobilin
SP  - 164
EP  - 164
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5132
ER  - 
@conference{
author = "Simović, Ana and Radomirović, Mirjana Ž. and Gligorijević, Nikola and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Algae have been consumed as food and medicine for centuries. Their benefits are so pronounced, due to high concentrations of vitamins, minerals, antioxidants and proteins that they are commonly referred to as superfoods. Phycocyanobilin (PCB) is a bioactive compound of microalga Spirulina platensis. It is a blue tetrapyrrole chromophore of C-phycocyanin (C-PC), the major chromoprotein of this microalga. It is covalently attached to cysteine residues of C-PC via thioether bond. The outbreak of Coronavirus Disease 2019 (COVID-19) has posed a serious threat to global public health, calling for the development of safe and effective prophylactics and therapeutics against infection of its causative agent, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The SARS-CoV-2 spike (S) protein plays the most important roles in viral attachment, fusion and entry, and it serves as a target for development of antibodies, entry inhibitors and vaccines. It mediates viral entry into host cells by first binding to a host angiotensin-converting enzyme 2 (ACE2) receptor through the receptor-binding domain (RBD) and then fusing the viral and host membranes. This study aimed to investigate interaction of bioactive PCB with S protein and RBD respectively.
Combination of electrophoretic techniques and fluorescence spectroscopy was employed in order to examine interactions of PCB and S protein, as well as interactions of PCB and RBD, while the effects of PCB binding on RBD structure were studied by CD spectroscopy.
SDS-PAGE with Zn2+ staining has revealed that PCB covalently binds to both S protein and RBD, via free cysteine residues. Binding constants determined by fluorescence quenching method were: 2.1 x 107 M–1 for PCB and S protein, and 8.4 x 104 M–1 for PCB and RBD. Far-UV circular dichroism spectra showed that PCB influences RBD structure.
Our results support the importance of further research on covalent binding of PCB to S protein and RBD and its implications. Due to its interaction with S protein and RBD, PCB may exert one of its many bioactive effects via impact on S protein binding to ACE2 receptor.
Acknowledgments: This project has received funding from the European Union’s Horizon 2020 research and innovation program under grant agreement No. 810752.
References:
[1] S. Minic, M. Radomirovic, N. Savkovic et al., Food Chemistry, 269(2018) 43-52.
[2] W. Tai, L. He, X. Zhang et al., Cellular & Molecular Immunology, 17(2020) 613-620.",
publisher = "Sociedade Portuguesa de Química",
journal = "Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference",
title = "Interaction of SARS-CoV-2 Spike protein with phycocyanobilin",
pages = "164-164",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5132"
}
Simović, A., Radomirović, M. Ž., Gligorijević, N., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Interaction of SARS-CoV-2 Spike protein with phycocyanobilin. in Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference
Sociedade Portuguesa de Química., 164-164.
https://hdl.handle.net/21.15107/rcub_cherry_5132
Simović A, Radomirović MŽ, Gligorijević N, Stanić-Vučinić D, Ćirković-Veličković T. Interaction of SARS-CoV-2 Spike protein with phycocyanobilin. in Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference. 2021;:164-164.
https://hdl.handle.net/21.15107/rcub_cherry_5132 .
Simović, Ana, Radomirović, Mirjana Ž., Gligorijević, Nikola, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Interaction of SARS-CoV-2 Spike protein with phycocyanobilin" in Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference (2021):164-164,
https://hdl.handle.net/21.15107/rcub_cherry_5132 .

Higher degree of Maillard reaction induced by spray drying at high temperatures increases antioxidant activity of camel milk proteins

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

(2020)

TY  - CONF
AU  - Peruško, Marija
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Radomirović, Mirjana Ž.
AU  - Smiljanić, Katarina
AU  - Stanić-Vučinić, Dragana
AU  - Ghnimi, Sami
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5130
AB  - Objective. Camel milk is highly nutritious food with many health benefits proposed. Demand for camel milk has increased worldwide. Production of camel milk powders facilitate its transport, prolonge shelf-life, and also offer an attractive additive for various food products. In this study we examined the effect of freeze/spray drying treatment for camel milk powder production, on physiochemical and functional properties of camel milk proteins.
Material and Methods. Whole camel milk powders were prepared by spray drying treatment at six different inlet temperatures (190°C - 250°C) or by freeze drying. The soluble protein fractions upon the treatments were analysed by combination of electrophoretic and spectroscopic techniques. Structural and functional properties of camel milk proteins such as Maillard reaction products formation, antioxidant activity and protein solubility were assessed.
Results. SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while native electrophoresis revealed non-uniform decrease in pI values with increased inlet temperature of spray drying. That indicated attachement of lactose moieties to NH2-group of proteins via non-enzymatic Maillard reaction. Spectrophotometric analysis showed formation of intermediate Maillard reaction products (increased absorbance at 294 nm) and no detectable late Maillard reaction products formation. Higher inlet temperatures (230°C - 250°C) resulted in higher protein carbonyls formation and lower content of free amino groups as a result of Maillard reaction. Far-UV circular dichroism spectra showed no differences in secondary structures between freeze and spray dried samples. Antioxidant activity and protein solubility were increased with increase in inlet temperature.
Conclusions. Our results showed that spray drying treatment promotes non-enzymatic glycation of camel milk proteins and exert significant effects on the techno-functional properties of CM powder such as nutritional value and shelf life. Thus, optimization of spray drying parametars is essential for production of high quality camel milk powders.
Acknowledgments: This work was supported by the Ministry of Education, Science and Technological Development of the Republic of Serbia, grant number 172024. The project leading to this application has received funding from the European Union's Horizon 2020 research and innovation programme under grant agreement No 810752.
C3  - 2nd FoodEnTwin Workshop Experimental anlimal models for food and environment, February 3-4, 2020, Vienna, Austria
T1  - Higher degree of Maillard reaction induced by spray drying at high temperatures increases antioxidant activity of camel milk proteins
SP  - 6
EP  - 7
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5130
ER  - 
@conference{
author = "Peruško, Marija and Simović, Ana and Stevanović, Nikola R. and Radomirović, Mirjana Ž. and Smiljanić, Katarina and Stanić-Vučinić, Dragana and Ghnimi, Sami and Ćirković-Veličković, Tanja",
year = "2020",
abstract = "Objective. Camel milk is highly nutritious food with many health benefits proposed. Demand for camel milk has increased worldwide. Production of camel milk powders facilitate its transport, prolonge shelf-life, and also offer an attractive additive for various food products. In this study we examined the effect of freeze/spray drying treatment for camel milk powder production, on physiochemical and functional properties of camel milk proteins.
Material and Methods. Whole camel milk powders were prepared by spray drying treatment at six different inlet temperatures (190°C - 250°C) or by freeze drying. The soluble protein fractions upon the treatments were analysed by combination of electrophoretic and spectroscopic techniques. Structural and functional properties of camel milk proteins such as Maillard reaction products formation, antioxidant activity and protein solubility were assessed.
Results. SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while native electrophoresis revealed non-uniform decrease in pI values with increased inlet temperature of spray drying. That indicated attachement of lactose moieties to NH2-group of proteins via non-enzymatic Maillard reaction. Spectrophotometric analysis showed formation of intermediate Maillard reaction products (increased absorbance at 294 nm) and no detectable late Maillard reaction products formation. Higher inlet temperatures (230°C - 250°C) resulted in higher protein carbonyls formation and lower content of free amino groups as a result of Maillard reaction. Far-UV circular dichroism spectra showed no differences in secondary structures between freeze and spray dried samples. Antioxidant activity and protein solubility were increased with increase in inlet temperature.
Conclusions. Our results showed that spray drying treatment promotes non-enzymatic glycation of camel milk proteins and exert significant effects on the techno-functional properties of CM powder such as nutritional value and shelf life. Thus, optimization of spray drying parametars is essential for production of high quality camel milk powders.
Acknowledgments: This work was supported by the Ministry of Education, Science and Technological Development of the Republic of Serbia, grant number 172024. The project leading to this application has received funding from the European Union's Horizon 2020 research and innovation programme under grant agreement No 810752.",
journal = "2nd FoodEnTwin Workshop Experimental anlimal models for food and environment, February 3-4, 2020, Vienna, Austria",
title = "Higher degree of Maillard reaction induced by spray drying at high temperatures increases antioxidant activity of camel milk proteins",
pages = "6-7",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5130"
}
Peruško, M., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Smiljanić, K., Stanić-Vučinić, D., Ghnimi, S.,& Ćirković-Veličković, T.. (2020). Higher degree of Maillard reaction induced by spray drying at high temperatures increases antioxidant activity of camel milk proteins. in 2nd FoodEnTwin Workshop Experimental anlimal models for food and environment, February 3-4, 2020, Vienna, Austria, 6-7.
https://hdl.handle.net/21.15107/rcub_cherry_5130
Peruško M, Simović A, Stevanović NR, Radomirović MŽ, Smiljanić K, Stanić-Vučinić D, Ghnimi S, Ćirković-Veličković T. Higher degree of Maillard reaction induced by spray drying at high temperatures increases antioxidant activity of camel milk proteins. in 2nd FoodEnTwin Workshop Experimental anlimal models for food and environment, February 3-4, 2020, Vienna, Austria. 2020;:6-7.
https://hdl.handle.net/21.15107/rcub_cherry_5130 .
Peruško, Marija, Simović, Ana, Stevanović, Nikola R., Radomirović, Mirjana Ž., Smiljanić, Katarina, Stanić-Vučinić, Dragana, Ghnimi, Sami, Ćirković-Veličković, Tanja, "Higher degree of Maillard reaction induced by spray drying at high temperatures increases antioxidant activity of camel milk proteins" in 2nd FoodEnTwin Workshop Experimental anlimal models for food and environment, February 3-4, 2020, Vienna, Austria (2020):6-7,
https://hdl.handle.net/21.15107/rcub_cherry_5130 .

Analytical Protocols in Phycobiliproteins Analysis

Nikolić, Milan; Minić, Simeon L.; Mačvanin, Mirjana T.; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja; Jacob-Lopes, Eduardo; Queiroz, Maria Isabel; Zepka, Leila Queiroz

(Springer International Publishing, 2020)

TY  - CHAP
AU  - Nikolić, Milan
AU  - Minić, Simeon L.
AU  - Mačvanin, Mirjana T.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
AU  - Jacob-Lopes, Eduardo
AU  - Queiroz, Maria Isabel
AU  - Zepka, Leila Queiroz
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4892
AB  - The aim of this chapter is to review and discuss methodology and protocols in the analysis of phycobiliproteins (phycocyanins, allophycocyanins, and phycoerythrins) and their chromophores. Due to the presence of multiple covalently bound open-chain tetrapyrrole chromophores, phycobiliproteins are colored and strongly fluorescent molecules, with high absorption coefficients (105 to 106) and excellent fluorescent quantum yield (0.51 up to 0.98). Therefore, a vast number of methods for phycobiliproteins analysis is based on these spectral characteristics, whereas assessment of their bioactivity is related to their exceptional redox and metal-chelating properties. This chapter is dedicated to methods used for isolation and purification, structure analysis, physicochemical properties and stability characterization, quantification, as well as in vitro and in vivo biological activities evaluation. In addition, emerging approaches related to phycobiliproteins analysis are also reviewed including interactions with other biomolecules and ions and identification of phycobiliprotein (chromo)peptides by mass spectrometry.
PB  - Springer International Publishing
T2  - Pigments from Microalgae Handbook
T1  - Analytical Protocols in Phycobiliproteins Analysis
SP  - 179
EP  - 201
DO  - 10.1007/978-3-030-50971-2_8
ER  - 
@inbook{
author = "Nikolić, Milan and Minić, Simeon L. and Mačvanin, Mirjana T. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja and Jacob-Lopes, Eduardo and Queiroz, Maria Isabel and Zepka, Leila Queiroz",
year = "2020",
abstract = "The aim of this chapter is to review and discuss methodology and protocols in the analysis of phycobiliproteins (phycocyanins, allophycocyanins, and phycoerythrins) and their chromophores. Due to the presence of multiple covalently bound open-chain tetrapyrrole chromophores, phycobiliproteins are colored and strongly fluorescent molecules, with high absorption coefficients (105 to 106) and excellent fluorescent quantum yield (0.51 up to 0.98). Therefore, a vast number of methods for phycobiliproteins analysis is based on these spectral characteristics, whereas assessment of their bioactivity is related to their exceptional redox and metal-chelating properties. This chapter is dedicated to methods used for isolation and purification, structure analysis, physicochemical properties and stability characterization, quantification, as well as in vitro and in vivo biological activities evaluation. In addition, emerging approaches related to phycobiliproteins analysis are also reviewed including interactions with other biomolecules and ions and identification of phycobiliprotein (chromo)peptides by mass spectrometry.",
publisher = "Springer International Publishing",
journal = "Pigments from Microalgae Handbook",
booktitle = "Analytical Protocols in Phycobiliproteins Analysis",
pages = "179-201",
doi = "10.1007/978-3-030-50971-2_8"
}
Nikolić, M., Minić, S. L., Mačvanin, M. T., Stanić-Vučinić, D., Ćirković-Veličković, T., Jacob-Lopes, E., Queiroz, M. I.,& Zepka, L. Q.. (2020). Analytical Protocols in Phycobiliproteins Analysis. in Pigments from Microalgae Handbook
Springer International Publishing., 179-201.
https://doi.org/10.1007/978-3-030-50971-2_8
Nikolić M, Minić SL, Mačvanin MT, Stanić-Vučinić D, Ćirković-Veličković T, Jacob-Lopes E, Queiroz MI, Zepka LQ. Analytical Protocols in Phycobiliproteins Analysis. in Pigments from Microalgae Handbook. 2020;:179-201.
doi:10.1007/978-3-030-50971-2_8 .
Nikolić, Milan, Minić, Simeon L., Mačvanin, Mirjana T., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, Jacob-Lopes, Eduardo, Queiroz, Maria Isabel, Zepka, Leila Queiroz, "Analytical Protocols in Phycobiliproteins Analysis" in Pigments from Microalgae Handbook (2020):179-201,
https://doi.org/10.1007/978-3-030-50971-2_8 . .
3

Analytical Protocols in Phycobiliproteins Analysis

Nikolić, Milan; Minić, Simeon L.; Mačvanin, Mirjana T.; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja; Jacob-Lopes, Eduardo; Queiroz, Maria Isabel; Zepka, Leila Queiroz

(Springer International Publishing, 2020)

TY  - CHAP
AU  - Nikolić, Milan
AU  - Minić, Simeon L.
AU  - Mačvanin, Mirjana T.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
AU  - Jacob-Lopes, Eduardo
AU  - Queiroz, Maria Isabel
AU  - Zepka, Leila Queiroz
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4893
AB  - The aim of this chapter is to review and discuss methodology and protocols in the analysis of phycobiliproteins (phycocyanins, allophycocyanins, and phycoerythrins) and their chromophores. Due to the presence of multiple covalently bound open-chain tetrapyrrole chromophores, phycobiliproteins are colored and strongly fluorescent molecules, with high absorption coefficients (105 to 106) and excellent fluorescent quantum yield (0.51 up to 0.98). Therefore, a vast number of methods for phycobiliproteins analysis is based on these spectral characteristics, whereas assessment of their bioactivity is related to their exceptional redox and metal-chelating properties. This chapter is dedicated to methods used for isolation and purification, structure analysis, physicochemical properties and stability characterization, quantification, as well as in vitro and in vivo biological activities evaluation. In addition, emerging approaches related to phycobiliproteins analysis are also reviewed including interactions with other biomolecules and ions and identification of phycobiliprotein (chromo)peptides by mass spectrometry.
PB  - Springer International Publishing
T2  - Pigments from Microalgae Handbook
T1  - Analytical Protocols in Phycobiliproteins Analysis
SP  - 179
EP  - 201
DO  - 10.1007/978-3-030-50971-2_8
ER  - 
@inbook{
author = "Nikolić, Milan and Minić, Simeon L. and Mačvanin, Mirjana T. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja and Jacob-Lopes, Eduardo and Queiroz, Maria Isabel and Zepka, Leila Queiroz",
year = "2020",
abstract = "The aim of this chapter is to review and discuss methodology and protocols in the analysis of phycobiliproteins (phycocyanins, allophycocyanins, and phycoerythrins) and their chromophores. Due to the presence of multiple covalently bound open-chain tetrapyrrole chromophores, phycobiliproteins are colored and strongly fluorescent molecules, with high absorption coefficients (105 to 106) and excellent fluorescent quantum yield (0.51 up to 0.98). Therefore, a vast number of methods for phycobiliproteins analysis is based on these spectral characteristics, whereas assessment of their bioactivity is related to their exceptional redox and metal-chelating properties. This chapter is dedicated to methods used for isolation and purification, structure analysis, physicochemical properties and stability characterization, quantification, as well as in vitro and in vivo biological activities evaluation. In addition, emerging approaches related to phycobiliproteins analysis are also reviewed including interactions with other biomolecules and ions and identification of phycobiliprotein (chromo)peptides by mass spectrometry.",
publisher = "Springer International Publishing",
journal = "Pigments from Microalgae Handbook",
booktitle = "Analytical Protocols in Phycobiliproteins Analysis",
pages = "179-201",
doi = "10.1007/978-3-030-50971-2_8"
}
Nikolić, M., Minić, S. L., Mačvanin, M. T., Stanić-Vučinić, D., Ćirković-Veličković, T., Jacob-Lopes, E., Queiroz, M. I.,& Zepka, L. Q.. (2020). Analytical Protocols in Phycobiliproteins Analysis. in Pigments from Microalgae Handbook
Springer International Publishing., 179-201.
https://doi.org/10.1007/978-3-030-50971-2_8
Nikolić M, Minić SL, Mačvanin MT, Stanić-Vučinić D, Ćirković-Veličković T, Jacob-Lopes E, Queiroz MI, Zepka LQ. Analytical Protocols in Phycobiliproteins Analysis. in Pigments from Microalgae Handbook. 2020;:179-201.
doi:10.1007/978-3-030-50971-2_8 .
Nikolić, Milan, Minić, Simeon L., Mačvanin, Mirjana T., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, Jacob-Lopes, Eduardo, Queiroz, Maria Isabel, Zepka, Leila Queiroz, "Analytical Protocols in Phycobiliproteins Analysis" in Pigments from Microalgae Handbook (2020):179-201,
https://doi.org/10.1007/978-3-030-50971-2_8 . .
3

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

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

(Springer, 2020)

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

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

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

(Springer, 2020)

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

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

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

(Springer, 2020)

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

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

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

(Elsevier, 2019)

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

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

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

(2019)

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

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

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

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

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

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

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

(Elsevier, 2019)

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

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

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

Supplementary data for the article: Radibratović, M.; Al-Hanish, A.; Minić, S. L.; Radomirović, M. Ž.; Milčić, M. K.; Stanić-Vučinić, D.; Ćirković-Veličković, T. Stabilization of Apo Alpha-Lactalbumin by Binding of Epigallocatechin-3-Gallate: Experimental and Molecular Dynamics Study. Food Chemistry 2019, 278, 388–395. https://doi.org/10.1016/j.foodchem.2018.11.038.

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

(Elsevier, 2019)

TY  - DATA
AU  - Radibratović, Milica
AU  - Al-Hanish, Ayah
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4849
PB  - Elsevier
T2  - Food Chemistry
T1  - Supplementary data for the article: Radibratović, M.; Al-Hanish, A.; Minić, S. L.; Radomirović, M. Ž.; Milčić, M. K.; Stanić-Vučinić, D.; Ćirković-Veličković, T. Stabilization of Apo Alpha-Lactalbumin by Binding of Epigallocatechin-3-Gallate: Experimental and Molecular Dynamics Study. Food Chemistry 2019, 278, 388–395. https://doi.org/10.1016/j.foodchem.2018.11.038.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4849
ER  - 
@misc{
author = "Radibratović, Milica and Al-Hanish, Ayah and Minić, Simeon L. and Radomirović, Mirjana Ž. and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2019",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Supplementary data for the article: Radibratović, M.; Al-Hanish, A.; Minić, S. L.; Radomirović, M. Ž.; Milčić, M. K.; Stanić-Vučinić, D.; Ćirković-Veličković, T. Stabilization of Apo Alpha-Lactalbumin by Binding of Epigallocatechin-3-Gallate: Experimental and Molecular Dynamics Study. Food Chemistry 2019, 278, 388–395. https://doi.org/10.1016/j.foodchem.2018.11.038.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4849"
}
Radibratović, M., Al-Hanish, A., Minić, S. L., Radomirović, M. Ž., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2019). Supplementary data for the article: Radibratović, M.; Al-Hanish, A.; Minić, S. L.; Radomirović, M. Ž.; Milčić, M. K.; Stanić-Vučinić, D.; Ćirković-Veličković, T. Stabilization of Apo Alpha-Lactalbumin by Binding of Epigallocatechin-3-Gallate: Experimental and Molecular Dynamics Study. Food Chemistry 2019, 278, 388–395. https://doi.org/10.1016/j.foodchem.2018.11.038.. in Food Chemistry
Elsevier..
https://hdl.handle.net/21.15107/rcub_cherry_4849
Radibratović M, Al-Hanish A, Minić SL, Radomirović MŽ, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary data for the article: Radibratović, M.; Al-Hanish, A.; Minić, S. L.; Radomirović, M. Ž.; Milčić, M. K.; Stanić-Vučinić, D.; Ćirković-Veličković, T. Stabilization of Apo Alpha-Lactalbumin by Binding of Epigallocatechin-3-Gallate: Experimental and Molecular Dynamics Study. Food Chemistry 2019, 278, 388–395. https://doi.org/10.1016/j.foodchem.2018.11.038.. in Food Chemistry. 2019;.
https://hdl.handle.net/21.15107/rcub_cherry_4849 .
Radibratović, Milica, Al-Hanish, Ayah, Minić, Simeon L., Radomirović, Mirjana Ž., Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Supplementary data for the article: Radibratović, M.; Al-Hanish, A.; Minić, S. L.; Radomirović, M. Ž.; Milčić, M. K.; Stanić-Vučinić, D.; Ćirković-Veličković, T. Stabilization of Apo Alpha-Lactalbumin by Binding of Epigallocatechin-3-Gallate: Experimental and Molecular Dynamics Study. Food Chemistry 2019, 278, 388–395. https://doi.org/10.1016/j.foodchem.2018.11.038." in Food Chemistry (2019),
https://hdl.handle.net/21.15107/rcub_cherry_4849 .