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  - https://cer.ihtm.bg.ac.rs/handle/123456789/5555
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
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"
}

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

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 .

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 . .

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  - https://cer.ihtm.bg.ac.rs/handle/123456789/5556
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
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"
}

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

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 .

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 . .

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Radibratović, Milica
AU  - Papadimitriou, Vassiliki
AU  - Nedić, Olgica
AU  - Sotiroudis, Theodore G.
AU  - Nikolić, Milan
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4226
AB  - Phycocyanobilin is a dark blue linear tetrapyrrole chromophore covalently attached to protein subunits of phycobiliproteins present in the light-harvesting complexes of the cyanobacteria Arthrospira platensis (Spirulina “superfood”). It shows exceptional health-promoting properties and emerging use in various fields of bioscience and industry. This study aims to examine the mutual impact of phycocyanobilin interactions with catalase, a life-essential antioxidant enzyme. Fluorescence quenching experiments demonstrated moderate binding (Ka of 3.9 × 104 M−1 at 25 °C; n = 0.89) (static type), while van't Hoff plot points to an enthalpically driven ligand binding (ΔG = −28.2 kJ mol−1; ΔH = −41.9 kJ mol−1). No significant changes in protein secondary structures (α-helix content ~22%) and thermal protein stability in terms of enzyme tetramer subunits (Tm ~ 64 °C) were detected upon ligand binding. Alterations in the tertiary catalase structure were found without adverse effects on enzyme activity (~2 × 106 IU/mL). The docking study results indicated that the ligand most likely binds to amino acid residues (Asn141, Arg 362, Tyr369 and Asn384) near the cavity between the enzyme homotetramer subunits not related to the active site. Finally, complex formation protects the pigment from free-radical induced oxidation (bleaching), suggesting possible prolongation of its half-life and bioactivity in vivo if bound to catalase.
PB  - Elsevier
T2  - Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
T1  - Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity
VL  - 251
SP  - 119483
DO  - 10.1016/j.saa.2021.119483
ER  - 

@article{
author = "Gligorijević, Nikola and Minić, Simeon and Radibratović, Milica and Papadimitriou, Vassiliki and Nedić, Olgica and Sotiroudis, Theodore G. and Nikolić, Milan",
year = "2021",
abstract = "Phycocyanobilin is a dark blue linear tetrapyrrole chromophore covalently attached to protein subunits of phycobiliproteins present in the light-harvesting complexes of the cyanobacteria Arthrospira platensis (Spirulina “superfood”). It shows exceptional health-promoting properties and emerging use in various fields of bioscience and industry. This study aims to examine the mutual impact of phycocyanobilin interactions with catalase, a life-essential antioxidant enzyme. Fluorescence quenching experiments demonstrated moderate binding (Ka of 3.9 × 104 M−1 at 25 °C; n = 0.89) (static type), while van't Hoff plot points to an enthalpically driven ligand binding (ΔG = −28.2 kJ mol−1; ΔH = −41.9 kJ mol−1). No significant changes in protein secondary structures (α-helix content ~22%) and thermal protein stability in terms of enzyme tetramer subunits (Tm ~ 64 °C) were detected upon ligand binding. Alterations in the tertiary catalase structure were found without adverse effects on enzyme activity (~2 × 106 IU/mL). The docking study results indicated that the ligand most likely binds to amino acid residues (Asn141, Arg 362, Tyr369 and Asn384) near the cavity between the enzyme homotetramer subunits not related to the active site. Finally, complex formation protects the pigment from free-radical induced oxidation (bleaching), suggesting possible prolongation of its half-life and bioactivity in vivo if bound to catalase.",
publisher = "Elsevier",
journal = "Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy",
title = "Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity",
volume = "251",
pages = "119483",
doi = "10.1016/j.saa.2021.119483"
}

Gligorijević, N., Minić, S., Radibratović, M., Papadimitriou, V., Nedić, O., Sotiroudis, T. G.,& Nikolić, M.. (2021). Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity. in Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
Elsevier., 251, 119483.
https://doi.org/10.1016/j.saa.2021.119483

Gligorijević N, Minić S, Radibratović M, Papadimitriou V, Nedić O, Sotiroudis TG, Nikolić M. Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity. in Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy. 2021;251:119483.
doi:10.1016/j.saa.2021.119483 .

Gligorijević, Nikola, Minić, Simeon, Radibratović, Milica, Papadimitriou, Vassiliki, Nedić, Olgica, Sotiroudis, Theodore G., Nikolić, Milan, "Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity" in Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy, 251 (2021):119483,
https://doi.org/10.1016/j.saa.2021.119483 . .

TY  - JOUR
AU  - Radibratović, Milica
AU  - Al-Hanish, Ayah
AU  - Minić, Simeon
AU  - Radomirović, Mirjana
AU  - Milčić, Miloš
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković Veličković, Tanja
PY  - 2019
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3212
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 epigallocatechin-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 α-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 and Radomirović, Mirjana and Milčić, Miloš 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 epigallocatechin-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 α-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., Radomirović, M., Milčić, M., Stanić-Vučinić, D.,& Ćirković Veličković, T.. (2019). Stabilization of apo α-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 S, Radomirović M, Milčić M, Stanić-Vučinić D, Ćirković Veličković T. Stabilization of apo α-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, Radomirović, Mirjana, Milčić, Miloš, Stanić-Vučinić, Dragana, Ćirković Veličković, Tanja, "Stabilization of apo α-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study" in Food Chemistry, 278 (2019):388-395,
https://doi.org/10.1016/j.foodchem.2018.11.038 . .

TY  - THES
AU  - Radibratović, Milica
PY  - 2019
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=7671
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:22849/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=23507977
UR  - https://nardus.mpn.gov.rs/handle/123456789/17610
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3741
AB  - Humani serum albumin (HSA), usled velikog kapaciteta vezivanja različitih liganada, imaprimenu u medicini i biotehnologiji. Protein mleka, -laktalbumin (ALA), takođe pokazujevisok afinitet vezivanja za bioaktivne ligande i privlači veliku pažnju kao model-protein zaispitivanje struktura sličnih konformaciji “stopljene globule”. Bioaktivne komponentehrane su neesencijalni molekuli, koji imaju blagotvorne efekte po zdravlje. Stoga suinterakcije albumina sa bioaktivnim molekulima hrane poslednjih godina u fokusuistraživanja.U ovoj disertaciji teorijskim pristupom su izučavani efekti vezivanja bioaktivnih liganada izhrane, fikocijanobilina (PCB) iz alge Spiruline i epigalokatehin-3-galata (EGCG), izzelenog čaja, na konformaciju i stabilnost HSA i ALA. Molekulsko-dinamičkim (MD)simulacijama pokazano je da vezivanje PCB za bilo koje od dva vezujuća mesta na HSA,povećava njegovu stabilnost, čineći strukturu HSA manje fleksibilnom, kao i da vezivanjePCB za HSA utiče i na vezivanje drugih fiziološki relevantnih liganada/lekova.Molekulskim dokingom je pokazano da se EGCG vezuje za apo ALA na istom mestu kao iza holo formu. MD simulacijom je pokazano da uklanjanje Ca2+-jona smanjujekonformacionu stabilnost ALA. Međutim, vezivanje EGCG povećava stabilnost ALAvraćanjem njene konformacije u konformaciju sličnu kao kod holo forme i na taj načinmože odložiti prelaz nativnog apo ALA u konformaciju ‘’stopljene globule’’. Obe formeALA mogu služiti kao nosači EGCG.Temeljnim teorijskim pristupom dobijeni su rezultati od značaja za biodostupnost itransport bioaktivnih liganada, kao i povećanu stabilnost albumina pri vezivanju ovihliganada. Objašnjeni su i mehanizmi bazirani na konformacionim promenama proteina, kojise samo eksperimentalnim pristupom teško mogu uočiti.
AB  - Human serum albumin (HSA) is widely used in medical applications and biotechnologydue to its extraordinary ligand binding properties. Small milk protein α-lactalbumin (ALA),used as a model-protein for the investigation of molten globule-like states, is known to bindbioactive ligands with high affinity. Bioactive food components are nonessential moleculeswith a variety of benefits for human health. Recently, there is a growing interest ininvestigating interactions of albumins and bioactive food molecules.The aim of this thesis was to investigate the effects of bioactive food ligands binding,phycocyanobilin (PCB), from algae Spirulina and green tea catechin, epigallocatechin-3-gallate, on stability and conformation of HSA and ALA, by theoretical methods. Moleculardynamics (MD) simulations revealed that binding of PCB at either subdomain IB or IIA,results in higher HSA stability, making its structure more rigid. Also, the binding of PCBmay affect the binding of other physiologically relevant ligands/drugs of HSA.The docking simulation indicated the same binding site for EGCG to both ALA forms. MDresults demonstrated that removal of Ca2+ resulted in higher flexibility of ALA. However,EGCG binding improves ALA stability by reverting its conformation similar to that ofholoALA and delaying the transition of the native apoALA in molten-globuleconformation. These results demonstrate that both ALA forms can be used as a vehicle forthe delivery of EGCG.A thorough theoretical approach provides insight into the bioavailability and transport ofbioactive ligands, as well as the influence of PCB and EGCG binding on the higherstability of albumins. The mechanisms based on the protein conformational changes thatare difficult to observe only experimentally are explained.
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Teorijsko proučavanje konformacionih promena albumina prilikom vezivanja bioaktivnih liganada iz hrane
UR  - https://hdl.handle.net/21.15107/rcub_nardus_17610
ER  - 

@phdthesis{
author = "Radibratović, Milica",
year = "2019",
abstract = "Humani serum albumin (HSA), usled velikog kapaciteta vezivanja različitih liganada, imaprimenu u medicini i biotehnologiji. Protein mleka, -laktalbumin (ALA), takođe pokazujevisok afinitet vezivanja za bioaktivne ligande i privlači veliku pažnju kao model-protein zaispitivanje struktura sličnih konformaciji “stopljene globule”. Bioaktivne komponentehrane su neesencijalni molekuli, koji imaju blagotvorne efekte po zdravlje. Stoga suinterakcije albumina sa bioaktivnim molekulima hrane poslednjih godina u fokusuistraživanja.U ovoj disertaciji teorijskim pristupom su izučavani efekti vezivanja bioaktivnih liganada izhrane, fikocijanobilina (PCB) iz alge Spiruline i epigalokatehin-3-galata (EGCG), izzelenog čaja, na konformaciju i stabilnost HSA i ALA. Molekulsko-dinamičkim (MD)simulacijama pokazano je da vezivanje PCB za bilo koje od dva vezujuća mesta na HSA,povećava njegovu stabilnost, čineći strukturu HSA manje fleksibilnom, kao i da vezivanjePCB za HSA utiče i na vezivanje drugih fiziološki relevantnih liganada/lekova.Molekulskim dokingom je pokazano da se EGCG vezuje za apo ALA na istom mestu kao iza holo formu. MD simulacijom je pokazano da uklanjanje Ca2+-jona smanjujekonformacionu stabilnost ALA. Međutim, vezivanje EGCG povećava stabilnost ALAvraćanjem njene konformacije u konformaciju sličnu kao kod holo forme i na taj načinmože odložiti prelaz nativnog apo ALA u konformaciju ‘’stopljene globule’’. Obe formeALA mogu služiti kao nosači EGCG.Temeljnim teorijskim pristupom dobijeni su rezultati od značaja za biodostupnost itransport bioaktivnih liganada, kao i povećanu stabilnost albumina pri vezivanju ovihliganada. Objašnjeni su i mehanizmi bazirani na konformacionim promenama proteina, kojise samo eksperimentalnim pristupom teško mogu uočiti., Human serum albumin (HSA) is widely used in medical applications and biotechnologydue to its extraordinary ligand binding properties. Small milk protein α-lactalbumin (ALA),used as a model-protein for the investigation of molten globule-like states, is known to bindbioactive ligands with high affinity. Bioactive food components are nonessential moleculeswith a variety of benefits for human health. Recently, there is a growing interest ininvestigating interactions of albumins and bioactive food molecules.The aim of this thesis was to investigate the effects of bioactive food ligands binding,phycocyanobilin (PCB), from algae Spirulina and green tea catechin, epigallocatechin-3-gallate, on stability and conformation of HSA and ALA, by theoretical methods. Moleculardynamics (MD) simulations revealed that binding of PCB at either subdomain IB or IIA,results in higher HSA stability, making its structure more rigid. Also, the binding of PCBmay affect the binding of other physiologically relevant ligands/drugs of HSA.The docking simulation indicated the same binding site for EGCG to both ALA forms. MDresults demonstrated that removal of Ca2+ resulted in higher flexibility of ALA. However,EGCG binding improves ALA stability by reverting its conformation similar to that ofholoALA and delaying the transition of the native apoALA in molten-globuleconformation. These results demonstrate that both ALA forms can be used as a vehicle forthe delivery of EGCG.A thorough theoretical approach provides insight into the bioavailability and transport ofbioactive ligands, as well as the influence of PCB and EGCG binding on the higherstability of albumins. The mechanisms based on the protein conformational changes thatare difficult to observe only experimentally are explained.",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Teorijsko proučavanje konformacionih promena albumina prilikom vezivanja bioaktivnih liganada iz hrane",
url = "https://hdl.handle.net/21.15107/rcub_nardus_17610"
}

Radibratović, M.. (2019). Teorijsko proučavanje konformacionih promena albumina prilikom vezivanja bioaktivnih liganada iz hrane. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
https://hdl.handle.net/21.15107/rcub_nardus_17610

Radibratović M. Teorijsko proučavanje konformacionih promena albumina prilikom vezivanja bioaktivnih liganada iz hrane. in Универзитет у Београду. 2019;.
https://hdl.handle.net/21.15107/rcub_nardus_17610 .

Radibratović, Milica, "Teorijsko proučavanje konformacionih promena albumina prilikom vezivanja bioaktivnih liganada iz hrane" in Универзитет у Београду (2019),
https://hdl.handle.net/21.15107/rcub_nardus_17610 .

TY  - JOUR
AU  - Minić, Simeon
AU  - Radomirović, Mirjana
AU  - Savkovic, Nina
AU  - Radibratović, Milica
AU  - Mihailović, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković Veličković, Tanja
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2420
AB  - In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions
VL  - 269
SP  - 43
EP  - 52
DO  - 10.1016/j.foodchem.2018.06.138
ER  - 

@article{
author = "Minić, Simeon and Radomirović, Mirjana and Savkovic, Nina and Radibratović, Milica and Mihailović, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš and Stanić-Vučinić, Dragana and Ćirković Veličković, Tanja",
year = "2018",
abstract = "In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions",
volume = "269",
pages = "43-52",
doi = "10.1016/j.foodchem.2018.06.138"
}

Minić, S., Radomirović, M., Savkovic, N., Radibratović, M., Mihailović, J., Vasović, T., Nikolić, M., Milčić, M., Stanić-Vučinić, D.,& Ćirković Veličković, T.. (2018). Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. in Food Chemistry
Elsevier Sci Ltd, Oxford., 269, 43-52.
https://doi.org/10.1016/j.foodchem.2018.06.138

Minić S, Radomirović M, Savkovic N, Radibratović M, Mihailović J, Vasović T, Nikolić M, Milčić M, Stanić-Vučinić D, Ćirković Veličković T. Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. in Food Chemistry. 2018;269:43-52.
doi:10.1016/j.foodchem.2018.06.138 .

Minić, Simeon, Radomirović, Mirjana, Savkovic, Nina, Radibratović, Milica, Mihailović, Jelena, Vasović, Tamara, Nikolić, Milan, Milčić, Miloš, Stanić-Vučinić, Dragana, Ćirković Veličković, Tanja, "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions" in Food Chemistry, 269 (2018):43-52,
https://doi.org/10.1016/j.foodchem.2018.06.138 . .

TY  - JOUR
AU  - Minić, Simeon
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana
AU  - Radibratović, Milica
AU  - Milčić, Miloš
AU  - Nikolić, Milan
AU  - Ćirković Veličković, Tanja
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2478
AB  - Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (K-a = 2 x 10(6) M-1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin
VL  - 239
SP  - 1090
EP  - 1099
DO  - 10.1016/j.foodchem.2017.07.066
ER  - 

@article{
author = "Minić, Simeon and Stanić-Vučinić, Dragana and Radomirović, Mirjana and Radibratović, Milica and Milčić, Miloš and Nikolić, Milan and Ćirković Veličković, Tanja",
year = "2018",
abstract = "Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (K-a = 2 x 10(6) M-1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin",
volume = "239",
pages = "1090-1099",
doi = "10.1016/j.foodchem.2017.07.066"
}

Minić, S., Stanić-Vučinić, D., Radomirović, M., Radibratović, M., Milčić, M., Nikolić, M.,& Ćirković Veličković, T.. (2018). Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. in Food Chemistry
Elsevier Sci Ltd, Oxford., 239, 1090-1099.
https://doi.org/10.1016/j.foodchem.2017.07.066

Minić S, Stanić-Vučinić D, Radomirović M, Radibratović M, Milčić M, Nikolić M, Ćirković Veličković T. Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. in Food Chemistry. 2018;239:1090-1099.
doi:10.1016/j.foodchem.2017.07.066 .

Minić, Simeon, Stanić-Vučinić, Dragana, Radomirović, Mirjana, Radibratović, Milica, Milčić, Miloš, Nikolić, Milan, Ćirković Veličković, Tanja, "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin" in Food Chemistry, 239 (2018):1090-1099,
https://doi.org/10.1016/j.foodchem.2017.07.066 . .

TY  - JOUR
AU  - Minić, Simeon
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana
AU  - Radibratović, Milica
AU  - Milčić, Miloš
AU  - Nikolić, Milan
AU  - Ćirković Veličković, Tanja
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2984
AB  - Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (K-a = 2 x 10(6) M-1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin
VL  - 239
SP  - 1090
EP  - 1099
DO  - 10.1016/j.foodchem.2017.07.066
ER  - 

@article{
author = "Minić, Simeon and Stanić-Vučinić, Dragana and Radomirović, Mirjana and Radibratović, Milica and Milčić, Miloš and Nikolić, Milan and Ćirković Veličković, Tanja",
year = "2018",
abstract = "Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (K-a = 2 x 10(6) M-1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin",
volume = "239",
pages = "1090-1099",
doi = "10.1016/j.foodchem.2017.07.066"
}

Minić, S., Stanić-Vučinić, D., Radomirović, M., Radibratović, M., Milčić, M., Nikolić, M.,& Ćirković Veličković, T.. (2018). Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. in Food Chemistry
Elsevier Sci Ltd, Oxford., 239, 1090-1099.
https://doi.org/10.1016/j.foodchem.2017.07.066

Minić S, Stanić-Vučinić D, Radomirović M, Radibratović M, Milčić M, Nikolić M, Ćirković Veličković T. Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. in Food Chemistry. 2018;239:1090-1099.
doi:10.1016/j.foodchem.2017.07.066 .

Minić, Simeon, Stanić-Vučinić, Dragana, Radomirović, Mirjana, Radibratović, Milica, Milčić, Miloš, Nikolić, Milan, Ćirković Veličković, Tanja, "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin" in Food Chemistry, 239 (2018):1090-1099,
https://doi.org/10.1016/j.foodchem.2017.07.066 . .

TY  - JOUR
AU  - Minić, Simeon
AU  - Radomirović, Mirjana
AU  - Savkovic, Nina
AU  - Radibratović, Milica
AU  - Mihailović, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković Veličković, Tanja
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3022
AB  - In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions
VL  - 269
SP  - 43
EP  - 52
DO  - 10.1016/j.foodchem.2018.06.138
ER  - 

@article{
author = "Minić, Simeon and Radomirović, Mirjana and Savkovic, Nina and Radibratović, Milica and Mihailović, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš and Stanić-Vučinić, Dragana and Ćirković Veličković, Tanja",
year = "2018",
abstract = "In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions",
volume = "269",
pages = "43-52",
doi = "10.1016/j.foodchem.2018.06.138"
}

Minić, S., Radomirović, M., Savkovic, N., Radibratović, M., Mihailović, J., Vasović, T., Nikolić, M., Milčić, M., Stanić-Vučinić, D.,& Ćirković Veličković, T.. (2018). Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. in Food Chemistry
Elsevier Sci Ltd, Oxford., 269, 43-52.
https://doi.org/10.1016/j.foodchem.2018.06.138

Minić S, Radomirović M, Savkovic N, Radibratović M, Mihailović J, Vasović T, Nikolić M, Milčić M, Stanić-Vučinić D, Ćirković Veličković T. Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. in Food Chemistry. 2018;269:43-52.
doi:10.1016/j.foodchem.2018.06.138 .

Minić, Simeon, Radomirović, Mirjana, Savkovic, Nina, Radibratović, Milica, Mihailović, Jelena, Vasović, Tamara, Nikolić, Milan, Milčić, Miloš, Stanić-Vučinić, Dragana, Ćirković Veličković, Tanja, "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions" in Food Chemistry, 269 (2018):43-52,
https://doi.org/10.1016/j.foodchem.2018.06.138 . .

TY  - CONF
AU  - Radibratović, Milica
AU  - Al-Hanish, Ayah
AU  - Minić, Simeon
AU  - Radomirović, Mirjana Ž.
AU  - Milčić, Miloš
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7462
AB  - α-Lactalbumin (ALA) is a small, acidic, Ca2+-binding protein that might constitute up to 20% of whey protein. ALA has several partially folded intermediate states. It is very attractive for studies of the properties and structure of intermediate molten globule-like states since at acidic pH and in the apo-state at elevated temperatures ALA is the classic ‘molten globule’.The aim of our study was to examine if epi-gallo-catechin-3-gallate (EGCG) binds to ALA in its Ca-depleted (apo-ALA) and less ordered states. Moreover we examined if the polyphenol binding can stabilize protein structure. The experimental investigation of EGCG binding and protein’s stability were supported by molecular dynamics data.Green tea catechin binds to apo-ALA in neutral and acidic conditions. Binding affinity determined by intrinsic fluorescence quenching is of a similar magnitude as to the holo form of the protein. The complex of EGCG and ALA at neutral conditions is more stable to thermal denaturation then protein alone. The stabilizing effect is more pronounced for apo-ALA than for the holo-ALA.The docking analysis and molecular dynamic simulation (MDS) showed that EGCG binds to apoALA at the same site as to holoALA, in the hydrophobic pocket at the entrance of cleft between α and β subdomains, remaining bound during MDS. Ca2+ removal results in decreased conformational stability of ALA, where local destabilization of Ca2+-binding region propagates to cleft, with its slight opening. EGCG binding to apo-ALA increases stability of ALA by reverting of conformation and stability of disturbed Ca2+-binding region, which is transmitted to cleft, resulting in rejoining of α and β subdomains and slight cleft closing by the same mechanism. EGCG binding could retard transition of apo-ALA to less ordered states under conditions favoring its formation.Therefore, non-covalent binding of EGCG can stabilize structural fold of calcium-depleted ALA.
PB  - Univerzitet u Beogradu
C3  - UNIFOOD Conference, Belgrade, Serbia, 5th–6th October, 2018. In: UNIFOOD Conference - Programme and Book of Abstracts
T1  - Stabilization of apo-alpha-lactalbumin by binding of epigallocatechin-3-gallate: experimental and molecular dynamics study
SP  - 268
EP  - 268
UR  - https://hdl.handle.net/21.15107/rcub_cer_7462
ER  - 

@conference{
author = "Radibratović, Milica and Al-Hanish, Ayah and Minić, Simeon and Radomirović, Mirjana Ž. and Milčić, Miloš and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "α-Lactalbumin (ALA) is a small, acidic, Ca2+-binding protein that might constitute up to 20% of whey protein. ALA has several partially folded intermediate states. It is very attractive for studies of the properties and structure of intermediate molten globule-like states since at acidic pH and in the apo-state at elevated temperatures ALA is the classic ‘molten globule’.The aim of our study was to examine if epi-gallo-catechin-3-gallate (EGCG) binds to ALA in its Ca-depleted (apo-ALA) and less ordered states. Moreover we examined if the polyphenol binding can stabilize protein structure. The experimental investigation of EGCG binding and protein’s stability were supported by molecular dynamics data.Green tea catechin binds to apo-ALA in neutral and acidic conditions. Binding affinity determined by intrinsic fluorescence quenching is of a similar magnitude as to the holo form of the protein. The complex of EGCG and ALA at neutral conditions is more stable to thermal denaturation then protein alone. The stabilizing effect is more pronounced for apo-ALA than for the holo-ALA.The docking analysis and molecular dynamic simulation (MDS) showed that EGCG binds to apoALA at the same site as to holoALA, in the hydrophobic pocket at the entrance of cleft between α and β subdomains, remaining bound during MDS. Ca2+ removal results in decreased conformational stability of ALA, where local destabilization of Ca2+-binding region propagates to cleft, with its slight opening. EGCG binding to apo-ALA increases stability of ALA by reverting of conformation and stability of disturbed Ca2+-binding region, which is transmitted to cleft, resulting in rejoining of α and β subdomains and slight cleft closing by the same mechanism. EGCG binding could retard transition of apo-ALA to less ordered states under conditions favoring its formation.Therefore, non-covalent binding of EGCG can stabilize structural fold of calcium-depleted ALA.",
publisher = "Univerzitet u Beogradu",
journal = "UNIFOOD Conference, Belgrade, Serbia, 5th–6th October, 2018. In: UNIFOOD Conference - Programme and Book of Abstracts",
title = "Stabilization of apo-alpha-lactalbumin by binding of epigallocatechin-3-gallate: experimental and molecular dynamics study",
pages = "268-268",
url = "https://hdl.handle.net/21.15107/rcub_cer_7462"
}

Radibratović, M., Al-Hanish, A., Minić, S., Radomirović, M. Ž., Milčić, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2018). Stabilization of apo-alpha-lactalbumin by binding of epigallocatechin-3-gallate: experimental and molecular dynamics study. in UNIFOOD Conference, Belgrade, Serbia, 5th–6th October, 2018. In: UNIFOOD Conference - Programme and Book of Abstracts
Univerzitet u Beogradu., 268-268.
https://hdl.handle.net/21.15107/rcub_cer_7462

Radibratović M, Al-Hanish A, Minić S, Radomirović MŽ, Milčić M, Stanić-Vučinić D, Ćirković-Veličković T. Stabilization of apo-alpha-lactalbumin by binding of epigallocatechin-3-gallate: experimental and molecular dynamics study. in UNIFOOD Conference, Belgrade, Serbia, 5th–6th October, 2018. In: UNIFOOD Conference - Programme and Book of Abstracts. 2018;:268-268.
https://hdl.handle.net/21.15107/rcub_cer_7462 .

Radibratović, Milica, Al-Hanish, Ayah, Minić, Simeon, Radomirović, Mirjana Ž., Milčić, Miloš, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Stabilization of apo-alpha-lactalbumin by binding of epigallocatechin-3-gallate: experimental and molecular dynamics study" in UNIFOOD Conference, Belgrade, Serbia, 5th–6th October, 2018. In: UNIFOOD Conference - Programme and Book of Abstracts (2018):268-268,
https://hdl.handle.net/21.15107/rcub_cer_7462 .

TY  - JOUR
AU  - Prodić, I.
AU  - Stanić-Vučinić, Dragana
AU  - Apostolovic, D.
AU  - Mihailović, Jelena
AU  - Radibratović, Milica
AU  - Radosavljevic, J.
AU  - Burazer, L.
AU  - Milčić, Miloš
AU  - Smiljanic, K.
AU  - van, Hage M.
AU  - Ćirković Veličković, Tanja
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2299
AB  - BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  LT 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
VL  - 48
IS  - 6
SP  - 731
EP  - 740
DO  - 10.1111/cea.13113
ER  - 

@article{
author = "Prodić, I. and Stanić-Vučinić, Dragana and Apostolovic, D. and Mihailović, Jelena and Radibratović, Milica and Radosavljevic, J. and Burazer, L. and Milčić, Miloš and Smiljanic, K. and van, Hage M. and Ćirković Veličković, Tanja",
year = "2018",
abstract = "BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  LT 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
volume = "48",
number = "6",
pages = "731-740",
doi = "10.1111/cea.13113"
}

Prodić, I., Stanić-Vučinić, D., Apostolovic, D., Mihailović, J., Radibratović, M., Radosavljevic, J., Burazer, L., Milčić, M., Smiljanic, K., van, H. M.,& Ćirković Veličković, T.. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy
Wiley, Hoboken., 48(6), 731-740.
https://doi.org/10.1111/cea.13113

Prodić I, Stanić-Vučinić D, Apostolovic D, Mihailović J, Radibratović M, Radosavljevic J, Burazer L, Milčić M, Smiljanic K, van HM, Ćirković Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy. 2018;48(6):731-740.
doi:10.1111/cea.13113 .

Prodić, I., Stanić-Vučinić, Dragana, Apostolovic, D., Mihailović, Jelena, Radibratović, Milica, Radosavljevic, J., Burazer, L., Milčić, Miloš, Smiljanic, K., van, Hage M., Ćirković Veličković, Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" in Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 . .

TY  - JOUR
AU  - Prodić, I.
AU  - Stanić-Vučinić, Dragana
AU  - Apostolovic, D.
AU  - Mihailović, Jelena
AU  - Radibratović, Milica
AU  - Radosavljevic, J.
AU  - Burazer, L.
AU  - Milčić, Miloš
AU  - Smiljanic, K.
AU  - van, Hage M.
AU  - Ćirković Veličković, Tanja
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3340
AB  - BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  LT 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
VL  - 48
IS  - 6
SP  - 731
EP  - 740
DO  - 10.1111/cea.13113
ER  - 

@article{
author = "Prodić, I. and Stanić-Vučinić, Dragana and Apostolovic, D. and Mihailović, Jelena and Radibratović, Milica and Radosavljevic, J. and Burazer, L. and Milčić, Miloš and Smiljanic, K. and van, Hage M. and Ćirković Veličković, Tanja",
year = "2018",
abstract = "BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  LT 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
volume = "48",
number = "6",
pages = "731-740",
doi = "10.1111/cea.13113"
}

Prodić, I., Stanić-Vučinić, D., Apostolovic, D., Mihailović, J., Radibratović, M., Radosavljevic, J., Burazer, L., Milčić, M., Smiljanic, K., van, H. M.,& Ćirković Veličković, T.. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy
Wiley, Hoboken., 48(6), 731-740.
https://doi.org/10.1111/cea.13113

Prodić I, Stanić-Vučinić D, Apostolovic D, Mihailović J, Radibratović M, Radosavljevic J, Burazer L, Milčić M, Smiljanic K, van HM, Ćirković Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy. 2018;48(6):731-740.
doi:10.1111/cea.13113 .

Prodić, I., Stanić-Vučinić, Dragana, Apostolovic, D., Mihailović, Jelena, Radibratović, Milica, Radosavljevic, J., Burazer, L., Milčić, Miloš, Smiljanic, K., van, Hage M., Ćirković Veličković, Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" in Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 . .

TY  - CONF
AU  - Minic, S.
AU  - Radomirović, Mirjana
AU  - Radibratović, Milica
AU  - Milčić, Miloš
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Ćirković Veličković, Tanja
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2167
UR  - https://doi.org/10.1111/febs.14174
PB  - Wiley, Hoboken
C3  - FEBS Journal
T1  - Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin
VL  - 284
IS  - S1
SP  - 189
EP  - 190
UR  - https://hdl.handle.net/21.15107/rcub_cer_2167
ER  - 

@conference{
author = "Minic, S. and Radomirović, Mirjana and Radibratović, Milica and Milčić, Miloš and Stanić-Vučinić, Dragana and Nikolić, Milan and Ćirković Veličković, Tanja",
year = "2017",
publisher = "Wiley, Hoboken",
journal = "FEBS Journal",
title = "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin",
volume = "284",
number = "S1",
pages = "189-190",
url = "https://hdl.handle.net/21.15107/rcub_cer_2167"
}

Minic, S., Radomirović, M., Radibratović, M., Milčić, M., Stanić-Vučinić, D., Nikolić, M.,& Ćirković Veličković, T.. (2017). Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. in FEBS Journal
Wiley, Hoboken., 284(S1), 189-190.
https://hdl.handle.net/21.15107/rcub_cer_2167

Minic S, Radomirović M, Radibratović M, Milčić M, Stanić-Vučinić D, Nikolić M, Ćirković Veličković T. Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. in FEBS Journal. 2017;284(S1):189-190.
https://hdl.handle.net/21.15107/rcub_cer_2167 .

Minic, S., Radomirović, Mirjana, Radibratović, Milica, Milčić, Miloš, Stanić-Vučinić, Dragana, Nikolić, Milan, Ćirković Veličković, Tanja, "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin" in FEBS Journal, 284, no. S1 (2017):189-190,
https://hdl.handle.net/21.15107/rcub_cer_2167 .

TY  - JOUR
AU  - Radibratović, Milica
AU  - Minić, Simeon
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Milčić, Miloš
AU  - Ćirković Veličković, Tanja
PY  - 2016
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1891
AB  - Phycocyanobilin (PCB) binds with high affinity (2.2 x 10 6 M-1 at 25 degrees C) to human serum albumin (HSA) at sites located in IB and IIA subdomains. The aim of this study was to examine effects of PCB binding on protein conformation and stability. Using 300 ns molecular dynamics (MD) simulations, UV-VIS spectrophotometry, CD, FT-IR, spectrofluorimetry, thermal denaturation and susceptibility to trypsin digestion, we studied the effects of PCB binding on the stability and rigidity of HSA, as well as the conformational changes in PCB itself upon binding to the protein. MD simulation results demonstrated that HSA with PCB bound at any of the two sites showed greater rigidity and lower overall and individual domain flexibility compared to free HSA. Experimental data demonstrated an increase in the a-helical content of the protein and thermal and proteolytic stability upon ligand binding. PCB bound to HSA undergoes a conformational change to a more elongated conformation in the binding pockets of HSA. PCB binding to HSA stabilizes the structure of this flexible transport protein, making it more thermostable and resistant to proteolysis. The results from this work explain at molecular level, conformational changes and stabilization of HSA structure upon ligand binding. The resultant increased thermal and proteolytic stability of HSA may provide greater longevity to HSA in plasma.
PB  - Public Library Science, San Francisco
T2  - Plos One
T1  - Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study
VL  - 11
IS  - 12
DO  - 10.1371/journal.pone.0167973
ER  - 

@article{
author = "Radibratović, Milica and Minić, Simeon and Stanić-Vučinić, Dragana and Nikolić, Milan and Milčić, Miloš and Ćirković Veličković, Tanja",
year = "2016",
abstract = "Phycocyanobilin (PCB) binds with high affinity (2.2 x 10 6 M-1 at 25 degrees C) to human serum albumin (HSA) at sites located in IB and IIA subdomains. The aim of this study was to examine effects of PCB binding on protein conformation and stability. Using 300 ns molecular dynamics (MD) simulations, UV-VIS spectrophotometry, CD, FT-IR, spectrofluorimetry, thermal denaturation and susceptibility to trypsin digestion, we studied the effects of PCB binding on the stability and rigidity of HSA, as well as the conformational changes in PCB itself upon binding to the protein. MD simulation results demonstrated that HSA with PCB bound at any of the two sites showed greater rigidity and lower overall and individual domain flexibility compared to free HSA. Experimental data demonstrated an increase in the a-helical content of the protein and thermal and proteolytic stability upon ligand binding. PCB bound to HSA undergoes a conformational change to a more elongated conformation in the binding pockets of HSA. PCB binding to HSA stabilizes the structure of this flexible transport protein, making it more thermostable and resistant to proteolysis. The results from this work explain at molecular level, conformational changes and stabilization of HSA structure upon ligand binding. The resultant increased thermal and proteolytic stability of HSA may provide greater longevity to HSA in plasma.",
publisher = "Public Library Science, San Francisco",
journal = "Plos One",
title = "Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study",
volume = "11",
number = "12",
doi = "10.1371/journal.pone.0167973"
}

Radibratović, M., Minić, S., Stanić-Vučinić, D., Nikolić, M., Milčić, M.,& Ćirković Veličković, T.. (2016). Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study. in Plos One
Public Library Science, San Francisco., 11(12).
https://doi.org/10.1371/journal.pone.0167973

Radibratović M, Minić S, Stanić-Vučinić D, Nikolić M, Milčić M, Ćirković Veličković T. Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study. in Plos One. 2016;11(12).
doi:10.1371/journal.pone.0167973 .

Radibratović, Milica, Minić, Simeon, Stanić-Vučinić, Dragana, Nikolić, Milan, Milčić, Miloš, Ćirković Veličković, Tanja, "Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study" in Plos One, 11, no. 12 (2016),
https://doi.org/10.1371/journal.pone.0167973 . .

TY  - JOUR
AU  - Apostolovic, Danijela
AU  - Stanić-Vučinić, Dragana
AU  - de, Jongh Harmen H J
AU  - de, Jong Govardus A H
AU  - Mihailović, Jelena
AU  - Radosavljević, Jelena
AU  - Radibratović, Milica
AU  - Nordlee, Julie A
AU  - Baumert, Joseph L
AU  - Milčić, Miloš
AU  - Taylor, Steve L
AU  - Clua, Nuria Garrido
AU  - Ćirković Veličković, Tanja
AU  - Koppelman, Stef J
PY  - 2016
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1853
AB  - Conglutins represent the major peanut allergens and are renowned for their resistance to gastrointestinal digestion. Our aim was to characterize the digestion-resistant peptides (DRPs) of conglutins by biochemical and biophysical methods followed by a molecular dynamics simulation in order to better understand the molecular basis of food protein allergenicity. We have mapped proteolysis sites at the N- and C-termini and at a limited internal segment, while other potential proteolysis sites remained unaffected. Molecular dynamics simulation showed that proteolysis only occurred in the vibrant regions of the proteins. DRPs appeared to be conformationally stable as intact conglutins. Also, the overall secondary structure and IgE-binding potency of DRPs was comparable to that of intact conglutins. The stability of conglutins toward gastro-intestinal digestion, combined with the conformational stability of the resulting DRPs provide conditions for optimal exposure to the intestinal immune system, providing an explanation for the extraordinary allergenicity of peanut conglutins.
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity
VL  - 6
DO  - 10.1038/srep29249
ER  - 

@article{
author = "Apostolovic, Danijela and Stanić-Vučinić, Dragana and de, Jongh Harmen H J and de, Jong Govardus A H and Mihailović, Jelena and Radosavljević, Jelena and Radibratović, Milica and Nordlee, Julie A and Baumert, Joseph L and Milčić, Miloš and Taylor, Steve L and Clua, Nuria Garrido and Ćirković Veličković, Tanja and Koppelman, Stef J",
year = "2016",
abstract = "Conglutins represent the major peanut allergens and are renowned for their resistance to gastrointestinal digestion. Our aim was to characterize the digestion-resistant peptides (DRPs) of conglutins by biochemical and biophysical methods followed by a molecular dynamics simulation in order to better understand the molecular basis of food protein allergenicity. We have mapped proteolysis sites at the N- and C-termini and at a limited internal segment, while other potential proteolysis sites remained unaffected. Molecular dynamics simulation showed that proteolysis only occurred in the vibrant regions of the proteins. DRPs appeared to be conformationally stable as intact conglutins. Also, the overall secondary structure and IgE-binding potency of DRPs was comparable to that of intact conglutins. The stability of conglutins toward gastro-intestinal digestion, combined with the conformational stability of the resulting DRPs provide conditions for optimal exposure to the intestinal immune system, providing an explanation for the extraordinary allergenicity of peanut conglutins.",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity",
volume = "6",
doi = "10.1038/srep29249"
}

Apostolovic, D., Stanić-Vučinić, D., de, J. H. H. J., de, J. G. A. H., Mihailović, J., Radosavljević, J., Radibratović, M., Nordlee, J. A., Baumert, J. L., Milčić, M., Taylor, S. L., Clua, N. G., Ćirković Veličković, T.,& Koppelman, S. J.. (2016). Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity. in Scientific Reports
Nature Publishing Group, London., 6.
https://doi.org/10.1038/srep29249

Apostolovic D, Stanić-Vučinić D, de JHHJ, de JGAH, Mihailović J, Radosavljević J, Radibratović M, Nordlee JA, Baumert JL, Milčić M, Taylor SL, Clua NG, Ćirković Veličković T, Koppelman SJ. Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity. in Scientific Reports. 2016;6.
doi:10.1038/srep29249 .

Apostolovic, Danijela, Stanić-Vučinić, Dragana, de, Jongh Harmen H J, de, Jong Govardus A H, Mihailović, Jelena, Radosavljević, Jelena, Radibratović, Milica, Nordlee, Julie A, Baumert, Joseph L, Milčić, Miloš, Taylor, Steve L, Clua, Nuria Garrido, Ćirković Veličković, Tanja, Koppelman, Stef J, "Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity" in Scientific Reports, 6 (2016),
https://doi.org/10.1038/srep29249 . .

TY  - JOUR
AU  - Minić, Simeon
AU  - Milčić, Miloš
AU  - Stanić-Vučinić, Dragana
AU  - Radibratović, Milica
AU  - Sotiroudis, Theodore G.
AU  - Nikolić, Milan
AU  - Ćirković Veličković, Tanja
PY  - 2015
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1624
AB  - Human serum albumin (HSA) is an important regulator of the pharmacokinetic properties of bioactive compounds. Phycocyanobilin is a blue tetrapyrrole chromophore of C-phycocyanin with proven health-promoting activities. Despite its structural similarity to bilirubin, the conformation it adopts in aqueous solution is different and the pigment is more soluble than bilirubin. The aim of our study was to examine binding of phycocyanobilin for HSA and to investigate its competition with bilirubin. Based on a computational approach, we demonstrated two putative high-affinity binding pockets on HSA of virtually identical energies for the neutral and anion forms of bilirubin, but with slightly favorable predictions for anion forms of phycocyanobilin. Computational prediction of phycocyanobilin pK(a) values suggested a monoanion form to be the most stable form at physiological conditions. The computationally predicted binding sites for phycocyanobilin were identical to the two previously identified binding sites for bilirubin (subdomains IB and IIA). Results obtained by protein and pigment fluorescence measurements, circular dichroism, and competition experiments confirmed high affinity (binding constant of 2.2 x 10(6) M-1 at 25 degrees C), stereo-selective binding of phycocyanobilin M-conformer to HSA and its competition with bilirubin, warfarin and hemin. Our experimental data confirm that phycocyanobilin binds to IB and IIA binding site of HSA with an affinity similar to bilirubin. In conditions characterized by an increased bilirubin plasma concentration, or intake of drugs binding to IB or IIA binding site, pharmacokinetics of phycocyanobilin may also be changed.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin
VL  - 5
IS  - 76
SP  - 61787
EP  - 61798
DO  - 10.1039/c5ra05534b
ER  - 

@article{
author = "Minić, Simeon and Milčić, Miloš and Stanić-Vučinić, Dragana and Radibratović, Milica and Sotiroudis, Theodore G. and Nikolić, Milan and Ćirković Veličković, Tanja",
year = "2015",
abstract = "Human serum albumin (HSA) is an important regulator of the pharmacokinetic properties of bioactive compounds. Phycocyanobilin is a blue tetrapyrrole chromophore of C-phycocyanin with proven health-promoting activities. Despite its structural similarity to bilirubin, the conformation it adopts in aqueous solution is different and the pigment is more soluble than bilirubin. The aim of our study was to examine binding of phycocyanobilin for HSA and to investigate its competition with bilirubin. Based on a computational approach, we demonstrated two putative high-affinity binding pockets on HSA of virtually identical energies for the neutral and anion forms of bilirubin, but with slightly favorable predictions for anion forms of phycocyanobilin. Computational prediction of phycocyanobilin pK(a) values suggested a monoanion form to be the most stable form at physiological conditions. The computationally predicted binding sites for phycocyanobilin were identical to the two previously identified binding sites for bilirubin (subdomains IB and IIA). Results obtained by protein and pigment fluorescence measurements, circular dichroism, and competition experiments confirmed high affinity (binding constant of 2.2 x 10(6) M-1 at 25 degrees C), stereo-selective binding of phycocyanobilin M-conformer to HSA and its competition with bilirubin, warfarin and hemin. Our experimental data confirm that phycocyanobilin binds to IB and IIA binding site of HSA with an affinity similar to bilirubin. In conditions characterized by an increased bilirubin plasma concentration, or intake of drugs binding to IB or IIA binding site, pharmacokinetics of phycocyanobilin may also be changed.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin",
volume = "5",
number = "76",
pages = "61787-61798",
doi = "10.1039/c5ra05534b"
}

Minić, S., Milčić, M., Stanić-Vučinić, D., Radibratović, M., Sotiroudis, T. G., Nikolić, M.,& Ćirković Veličković, T.. (2015). Phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin. in RSC Advances
Royal Soc Chemistry, Cambridge., 5(76), 61787-61798.
https://doi.org/10.1039/c5ra05534b

Minić S, Milčić M, Stanić-Vučinić D, Radibratović M, Sotiroudis TG, Nikolić M, Ćirković Veličković T. Phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin. in RSC Advances. 2015;5(76):61787-61798.
doi:10.1039/c5ra05534b .

Minić, Simeon, Milčić, Miloš, Stanić-Vučinić, Dragana, Radibratović, Milica, Sotiroudis, Theodore G., Nikolić, Milan, Ćirković Veličković, Tanja, "Phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin" in RSC Advances, 5, no. 76 (2015):61787-61798,
https://doi.org/10.1039/c5ra05534b . .

TY  - JOUR
AU  - Zarić, Božidarka
AU  - Bukorović, Milica
AU  - Stojanović, Srđan
PY  - 2013
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1210
AB  - The Sm and Sm-like (LSm) proteins are a widespread protein family with members in all kingdoms of life. Sm proteins form complexes engaging in various RNA-processing events. Sm proteins do form and act as oligomeric assemblies whose characteristic is their exceptional stability. This study compares strong and weak hydrogen bonds in the interior of monomers and at interfaces of Sm/LSm proteins in order to better understand the stability of oligomers. According to our results, the stability of oligomeric assemblies is achieved by CH center dot center dot center dot O, NH center dot center dot center dot O and CH center dot center dot center dot N interactions including, NH center dot center dot center dot N, OH center dot center dot center dot O, XH center dot center dot center dot pi interactions present in small percentages. Intrachain hydrogen bonds behave in respect to geometry, distances and angles, like interchain hydrogen bonds. It is also shown that amino acids Arg and Lys participate significantly as donors or acceptors in some of the strong or weak interactions at interfaces to a higher extent than in the monomers. There is a trend for most polar amino acids to cross into more solvent exposed position in interfaces, which is not the case for nonpolar or charged amino acids. There is no exclusive preference for particular secondary structure both for intrachains and for interfaces.
PB  - Inst Materials Physics, Bucharest
T2  - Digest Journal of Nanomaterials and Biostructures
T1  - Strong and weak hydrogen bonds in sm/lsm oligomeric assemblies: a comparison of intra- and interchain interaction
VL  - 8
IS  - 2
SP  - 639
EP  - 654
UR  - https://hdl.handle.net/21.15107/rcub_cer_1210
ER  - 

@article{
author = "Zarić, Božidarka and Bukorović, Milica and Stojanović, Srđan",
year = "2013",
abstract = "The Sm and Sm-like (LSm) proteins are a widespread protein family with members in all kingdoms of life. Sm proteins form complexes engaging in various RNA-processing events. Sm proteins do form and act as oligomeric assemblies whose characteristic is their exceptional stability. This study compares strong and weak hydrogen bonds in the interior of monomers and at interfaces of Sm/LSm proteins in order to better understand the stability of oligomers. According to our results, the stability of oligomeric assemblies is achieved by CH center dot center dot center dot O, NH center dot center dot center dot O and CH center dot center dot center dot N interactions including, NH center dot center dot center dot N, OH center dot center dot center dot O, XH center dot center dot center dot pi interactions present in small percentages. Intrachain hydrogen bonds behave in respect to geometry, distances and angles, like interchain hydrogen bonds. It is also shown that amino acids Arg and Lys participate significantly as donors or acceptors in some of the strong or weak interactions at interfaces to a higher extent than in the monomers. There is a trend for most polar amino acids to cross into more solvent exposed position in interfaces, which is not the case for nonpolar or charged amino acids. There is no exclusive preference for particular secondary structure both for intrachains and for interfaces.",
publisher = "Inst Materials Physics, Bucharest",
journal = "Digest Journal of Nanomaterials and Biostructures",
title = "Strong and weak hydrogen bonds in sm/lsm oligomeric assemblies: a comparison of intra- and interchain interaction",
volume = "8",
number = "2",
pages = "639-654",
url = "https://hdl.handle.net/21.15107/rcub_cer_1210"
}

Zarić, B., Bukorović, M.,& Stojanović, S.. (2013). Strong and weak hydrogen bonds in sm/lsm oligomeric assemblies: a comparison of intra- and interchain interaction. in Digest Journal of Nanomaterials and Biostructures
Inst Materials Physics, Bucharest., 8(2), 639-654.
https://hdl.handle.net/21.15107/rcub_cer_1210

Zarić B, Bukorović M, Stojanović S. Strong and weak hydrogen bonds in sm/lsm oligomeric assemblies: a comparison of intra- and interchain interaction. in Digest Journal of Nanomaterials and Biostructures. 2013;8(2):639-654.
https://hdl.handle.net/21.15107/rcub_cer_1210 .

Zarić, Božidarka, Bukorović, Milica, Stojanović, Srđan, "Strong and weak hydrogen bonds in sm/lsm oligomeric assemblies: a comparison of intra- and interchain interaction" in Digest Journal of Nanomaterials and Biostructures, 8, no. 2 (2013):639-654,
https://hdl.handle.net/21.15107/rcub_cer_1210 .