Radibratović, Milica

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  • Radibratović, Milica (20)
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Teorijsko proučavanje konformacionih promena albumina prilikom vezivanja bioaktivnih liganada iz hrane

Radibratović, Milica

(Универзитет у Београду, Хемијски факултет, 2019)

TY  - BOOK
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  - http://cherry.chem.bg.ac.rs/handle/123456789/4379
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
ER  - 
@phdthesis{
author = "Radibratović, Milica",
year = "2019",
url = "http://eteze.bg.ac.rs/application/showtheses?thesesId=7671, https://fedorabg.bg.ac.rs/fedora/get/o:22849/bdef:Content/download, http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=23507977, https://nardus.mpn.gov.rs/handle/123456789/17610, http://cherry.chem.bg.ac.rs/handle/123456789/4379",
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"
}
Radibratović, M. (2019). Teorijsko proučavanje konformacionih promena albumina prilikom vezivanja bioaktivnih liganada iz hrane.
Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
Radibratović M. Teorijsko proučavanje konformacionih promena albumina prilikom vezivanja bioaktivnih liganada iz hrane. Универзитет у Београду. 2019;
Radibratović Milica, "Teorijsko proučavanje konformacionih promena albumina prilikom vezivanja bioaktivnih liganada iz hrane" Универзитет у Београду (2019)

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/123456789/3733
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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3733",
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.
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. Food Chemistry. 2019;278:388-395
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" Food Chemistry, 278 (2019):388-395,
https://doi.org/10.1016/j.foodchem.2018.11.038 .
3
3
4

Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.; Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099. https://doi.org/10.1016/j.foodchem.2017.07.066

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

(Elsevier, 2018)

TY  - BOOK
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana Ž.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3139
PB  - Elsevier
T2  - Food Chemistry
T1  - Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066
ER  - 
@book{
author = "Minić, Simeon L. and Stanić-Vučinić, Dragana and Radomirović, Mirjana Ž. and Radibratović, Milica and Milčić, Miloš K. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3139",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066"
}
Minić, S. L., Stanić-Vučinić, D., Radomirović, M. Ž., Radibratović, M., Milčić, M. K., Nikolić, M.,& Ćirković-Veličković, T. (2018). Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066.
Food Chemistry
Elsevier..
Minić SL, Stanić-Vučinić D, Radomirović MŽ, Radibratović M, Milčić MK, Nikolić M, Ćirković-Veličković T. Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066. Food Chemistry. 2018;
Minić Simeon L., Stanić-Vučinić Dragana, Radomirović Mirjana Ž., Radibratović Milica, Milčić Miloš K., Nikolić Milan, Ćirković-Veličković Tanja, "Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066" Food Chemistry (2018)

Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions

Minić, Simeon L.; Radomirović, Mirjana Ž.; Savković, Nina; Radibratović, Milica; Mihailović-Vesić, Jelena; Vasović, Tamara; Nikolić, Milan; Milčić, Miloš K.; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2018)

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Savković, Nina
AU  - Radibratović, Milica
AU  - Mihailović-Vesić, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3186
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 L. and Radomirović, Mirjana Ž. and Savković, Nina and Radibratović, Milica and Mihailović-Vesić, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3186",
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. L., Radomirović, M. Ž., Savković, N., Radibratović, M., Mihailović-Vesić, J., Vasović, T., Nikolić, M., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2018). Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions.
Food Chemistry
Elsevier Sci Ltd, Oxford., 269, 43-52.
https://doi.org/10.1016/j.foodchem.2018.06.138
Minić SL, Radomirović MŽ, Savković N, Radibratović M, Mihailović-Vesić J, Vasović T, Nikolić M, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. Food Chemistry. 2018;269:43-52
Minić Simeon L., Radomirović Mirjana Ž., Savković Nina, Radibratović Milica, Mihailović-Vesić Jelena, Vasović Tamara, Nikolić Milan, Milčić Miloš K., Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions" Food Chemistry, 269 (2018):43-52,
https://doi.org/10.1016/j.foodchem.2018.06.138 .
1
3
2
2

Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138

Minić, Simeon L.; Radomirović, Mirjana Ž.; Savković, Nina; Radibratović, Milica; Mihailović-Vesić, Jelena; Vasović, Tamara; Nikolić, Milan; Milčić, Miloš K.; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2018)

TY  - BOOK
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Savković, Nina
AU  - Radibratović, Milica
AU  - Mihailović-Vesić, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3187
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138
ER  - 
@book{
author = "Minić, Simeon L. and Radomirović, Mirjana Ž. and Savković, Nina and Radibratović, Milica and Mihailović-Vesić, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3187",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138"
}
Minić, S. L., Radomirović, M. Ž., Savković, N., Radibratović, M., Mihailović-Vesić, J., Vasović, T., Nikolić, M., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2018). Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138.
Food Chemistry
Elsevier Sci Ltd, Oxford..
Minić SL, Radomirović MŽ, Savković N, Radibratović M, Mihailović-Vesić J, Vasović T, Nikolić M, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138. Food Chemistry. 2018;
Minić Simeon L., Radomirović Mirjana Ž., Savković Nina, Radibratović Milica, Mihailović-Vesić Jelena, Vasović Tamara, Nikolić Milan, Milčić Miloš K., Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138" Food Chemistry (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

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović-Vesić, Jelena; Radibratović, Milica; Radosavljević, Jelena; Burazer, Lidija M.; Milčić, Miloš K.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3224
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, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3224",
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., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, 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.
Clinical and Experimental Allergy
Wiley, Hoboken., 48(6), 731-740.
https://doi.org/10.1111/cea.13113
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, 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. Clinical and Experimental Allergy. 2018;48(6):731-740
Prodić Ivana, Stanić-Vučinić Dragana, Apostolović Danijela, Mihailović-Vesić Jelena, Radibratović Milica, Radosavljević Jelena, Burazer Lidija M., Milčić Miloš K., Smiljanić Katarina, van Hage Marianne, 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" Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 .
3
21
18
19

Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. 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. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović-Vesić, Jelena; Radibratović, Milica; Radosavljević, Jelena; Burazer, Lidija M.; Milčić, Miloš K.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - BOOK
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3225
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. 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. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113
ER  - 
@book{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3225",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. 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. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T. (2018). Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. 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. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113.
Clinical and Experimental Allergy
Wiley, Hoboken..
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, Ćirković-Veličković T. Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. 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. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113. Clinical and Experimental Allergy. 2018;
Prodić Ivana, Stanić-Vučinić Dragana, Apostolović Danijela, Mihailović-Vesić Jelena, Radibratović Milica, Radosavljević Jelena, Burazer Lidija M., Milčić Miloš K., Smiljanić Katarina, van Hage Marianne, Ćirković-Veličković Tanja, "Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. 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. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113" Clinical and Experimental Allergy (2018)

Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions

Minić, Simeon L.; Radomirović, Mirjana Ž.; Savković, Nina; Radibratović, Milica; Mihailović-Vesić, Jelena; Vasović, Tamara; Nikolić, Milan; Milčić, Miloš K.; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2018)

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Savković, Nina
AU  - Radibratović, Milica
AU  - Mihailović-Vesić, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2197
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 L. and Radomirović, Mirjana Ž. and Savković, Nina and Radibratović, Milica and Mihailović-Vesić, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2197",
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. L., Radomirović, M. Ž., Savković, N., Radibratović, M., Mihailović-Vesić, J., Vasović, T., Nikolić, M., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2018). Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions.
Food Chemistry
Elsevier Sci Ltd, Oxford., 269, 43-52.
https://doi.org/10.1016/j.foodchem.2018.06.138
Minić SL, Radomirović MŽ, Savković N, Radibratović M, Mihailović-Vesić J, Vasović T, Nikolić M, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. Food Chemistry. 2018;269:43-52
Minić Simeon L., Radomirović Mirjana Ž., Savković Nina, Radibratović Milica, Mihailović-Vesić Jelena, Vasović Tamara, Nikolić Milan, Milčić Miloš K., Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions" Food Chemistry, 269 (2018):43-52,
https://doi.org/10.1016/j.foodchem.2018.06.138 .
1
3
2
2

Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin

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

(Elsevier, 2018)

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana Ž.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2515
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. (C) 2017 Elsevier Ltd. All rights reserved.
PB  - Elsevier
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 L. and Stanić-Vučinić, Dragana and Radomirović, Mirjana Ž. and Radibratović, Milica and Milčić, Miloš K. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2515",
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. (C) 2017 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier",
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. L., Stanić-Vučinić, D., Radomirović, M. Ž., Radibratović, M., Milčić, M. K., Nikolić, M.,& Ćirković-Veličković, T. (2018). Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin.
Food Chemistry
Elsevier., 239, 1090-1099.
https://doi.org/10.1016/j.foodchem.2017.07.066
Minić SL, Stanić-Vučinić D, Radomirović MŽ, Radibratović M, Milčić MK, Nikolić M, Ćirković-Veličković T. Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. Food Chemistry. 2018;239:1090-1099
Minić Simeon L., Stanić-Vučinić Dragana, Radomirović Mirjana Ž., Radibratović Milica, Milčić Miloš K., Nikolić Milan, Ćirković-Veličković Tanja, "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin" Food Chemistry, 239 (2018):1090-1099,
https://doi.org/10.1016/j.foodchem.2017.07.066 .
18
17
19

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

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović-Vesić, Jelena; Radibratović, Milica; Radosavljević, Jelena; Burazer, Lidija M.; Milčić, Miloš K.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2155
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, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2155",
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., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, 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.
Clinical and Experimental Allergy
Wiley, Hoboken., 48(6), 731-740.
https://doi.org/10.1111/cea.13113
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, 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. Clinical and Experimental Allergy. 2018;48(6):731-740
Prodić Ivana, Stanić-Vučinić Dragana, Apostolović Danijela, Mihailović-Vesić Jelena, Radibratović Milica, Radosavljević Jelena, Burazer Lidija M., Milčić Miloš K., Smiljanić Katarina, van Hage Marianne, 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" Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 .
3
21
18
19

Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin

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

(Elsevier, 2017)

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana Ž.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3035
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 (Ka = 2 × 106 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
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 L. and Stanić-Vučinić, Dragana and Radomirović, Mirjana Ž. and Radibratović, Milica and Milčić, Miloš K. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3035",
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 (Ka = 2 × 106 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",
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. L., Stanić-Vučinić, D., Radomirović, M. Ž., Radibratović, M., Milčić, M. K., Nikolić, M.,& Ćirković-Veličković, T. (2017). Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin.
Food Chemistry
Elsevier., 239, 1090-1099.
https://doi.org/10.1016/j.foodchem.2017.07.066
Minić SL, Stanić-Vučinić D, Radomirović MŽ, Radibratović M, Milčić MK, Nikolić M, Ćirković-Veličković T. Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. Food Chemistry. 2017;239:1090-1099
Minić Simeon L., Stanić-Vučinić Dragana, Radomirović Mirjana Ž., Radibratović Milica, Milčić Miloš K., Nikolić Milan, Ćirković-Veličković Tanja, "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin" Food Chemistry, 239 (2017):1090-1099,
https://doi.org/10.1016/j.foodchem.2017.07.066 .
18
19

Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin

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

(Wiley, Hoboken, 2017)

TY  - CONF
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2408
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 (Ka = 2 × 106 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  - Wiley, Hoboken
C3  - FEBS Journal / Federation of European of Biochemical Societies
T1  - Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin
VL  - 284
SP  - 189
EP  - 190
DO  - 10.1016/j.foodchem.2017.07.066
ER  - 
@conference{
author = "Minić, Simeon L. and Radomirović, Mirjana Ž. and Radibratović, Milica and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2408",
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 (Ka = 2 × 106 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 = "Wiley, Hoboken",
journal = "FEBS Journal / Federation of European of Biochemical Societies",
title = "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin",
volume = "284",
pages = "189-190",
doi = "10.1016/j.foodchem.2017.07.066"
}
Minić, S. L., Radomirović, M. Ž., Radibratović, M., Milčić, M. K., Stanić-Vučinić, D., Nikolić, M.,& Ćirković-Veličković, T. (2017). Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin.
FEBS Journal / Federation of European of Biochemical Societies
Wiley, Hoboken., 284, 189-190.
https://doi.org/10.1016/j.foodchem.2017.07.066
Minić SL, Radomirović MŽ, Radibratović M, Milčić MK, Stanić-Vučinić D, Nikolić M, Ćirković-Veličković T. Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. FEBS Journal / Federation of European of Biochemical Societies. 2017;284:189-190
Minić Simeon L., Radomirović Mirjana Ž., Radibratović Milica, Milčić Miloš K., Stanić-Vučinić Dragana, Nikolić Milan, Ćirković-Veličković Tanja, "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin" FEBS Journal / Federation of European of Biochemical Societies, 284 (2017):189-190,
https://doi.org/10.1016/j.foodchem.2017.07.066 .
18
19

Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249

Apostolović, Danijela; Stanić-Vučinić, Dragana; de Jongh, Harmen H. J.; de Jong, Govardus A. H.; Mihailović-Vesić, Jelena; Radosavljević, Jelena; Radibratović, Milica; Nordlee, Julie A.; Baumert, Joseph L.; Milčić, Miloš K.; Taylor, Steve L.; Clua, Nuria Garrido; Ćirković-Veličković, Tanja; Koppelman, Stef J.

(Nature Publishing Group, London, 2016)

TY  - BOOK
AU  - Apostolović, Danijela
AU  - Stanić-Vučinić, Dragana
AU  - de Jongh, Harmen H. J.
AU  - de Jong, Govardus A. H.
AU  - Mihailović-Vesić, Jelena
AU  - Radosavljević, Jelena
AU  - Radibratović, Milica
AU  - Nordlee, Julie A.
AU  - Baumert, Joseph L.
AU  - Milčić, Miloš K.
AU  - Taylor, Steve L.
AU  - Clua, Nuria Garrido
AU  - Ćirković-Veličković, Tanja
AU  - Koppelman, Stef J.
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3415
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249
ER  - 
@book{
author = "Apostolović, Danijela and Stanić-Vučinić, Dragana and de Jongh, Harmen H. J. and de Jong, Govardus A. H. and Mihailović-Vesić, Jelena and Radosavljević, Jelena and Radibratović, Milica and Nordlee, Julie A. and Baumert, Joseph L. and Milčić, Miloš K. and Taylor, Steve L. and Clua, Nuria Garrido and Ćirković-Veličković, Tanja and Koppelman, Stef J.",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3415",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249"
}
Apostolović, D., Stanić-Vučinić, D., de Jongh, H. H. J., de Jong, G. A. H., Mihailović-Vesić, J., Radosavljević, J., Radibratović, M., Nordlee, J. A., Baumert, J. L., Milčić, M. K., Taylor, S. L., Clua, N. G., Ćirković-Veličković, T.,& Koppelman, S. J. (2016). Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249.
Scientific Reports
Nature Publishing Group, London..
Apostolović D, Stanić-Vučinić D, de Jongh HHJ, de Jong GAH, Mihailović-Vesić J, Radosavljević J, Radibratović M, Nordlee JA, Baumert JL, Milčić MK, Taylor SL, Clua NG, Ćirković-Veličković T, Koppelman SJ. Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249. Scientific Reports. 2016;
Apostolović Danijela, Stanić-Vučinić Dragana, de Jongh Harmen H. J., de Jong Govardus A. H., Mihailović-Vesić Jelena, Radosavljević Jelena, Radibratović Milica, Nordlee Julie A., Baumert Joseph L., Milčić Miloš K., Taylor Steve L., Clua Nuria Garrido, Ćirković-Veličković Tanja, Koppelman Stef J., "Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249" Scientific Reports (2016)

Supplementary material for the article: Al-Hanish, A.; Stanic-Vucinic, D.; Mihailovic, J.; Prodic, I.; Minic, S.; Stojadinovic, M.; Radibratovic, M.; Milcic, M.; Cirkovic Velickovic, T. Noncovalent Interactions of Bovine α-Lactalbumin with Green Tea Polyphenol, Epigalocatechin-3-Gallate. Food Hydrocolloids 2016, 61, 241–250. https://doi.org/10.1016/j.foodhyd.2016.05.012

Al-Hanish, Ayah; Stanić-Vučinić, Dragana; Mihailović-Vesić, Jelena; Prodić, Ivana; Minić, Simeon L.; Stojadinović, Marija M.; Radibratović, Milica; Milčić, Miloš K.; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2016)

TY  - BOOK
AU  - Al-Hanish, Ayah
AU  - Stanić-Vučinić, Dragana
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Minić, Simeon L.
AU  - Stojadinović, Marija M.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3585
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Hydrocolloids
T1  - Supplementary material for the article: Al-Hanish, A.; Stanic-Vucinic, D.; Mihailovic, J.; Prodic, I.; Minic, S.; Stojadinovic, M.; Radibratovic, M.; Milcic, M.; Cirkovic Velickovic, T. Noncovalent Interactions of Bovine α-Lactalbumin with Green Tea Polyphenol, Epigalocatechin-3-Gallate. Food Hydrocolloids 2016, 61, 241–250. https://doi.org/10.1016/j.foodhyd.2016.05.012
ER  - 
@book{
author = "Al-Hanish, Ayah and Stanić-Vučinić, Dragana and Mihailović-Vesić, Jelena and Prodić, Ivana and Minić, Simeon L. and Stojadinović, Marija M. and Radibratović, Milica and Milčić, Miloš K. and Ćirković-Veličković, Tanja",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3585",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Hydrocolloids",
title = "Supplementary material for the article: Al-Hanish, A.; Stanic-Vucinic, D.; Mihailovic, J.; Prodic, I.; Minic, S.; Stojadinovic, M.; Radibratovic, M.; Milcic, M.; Cirkovic Velickovic, T. Noncovalent Interactions of Bovine α-Lactalbumin with Green Tea Polyphenol, Epigalocatechin-3-Gallate. Food Hydrocolloids 2016, 61, 241–250. https://doi.org/10.1016/j.foodhyd.2016.05.012"
}
Al-Hanish, A., Stanić-Vučinić, D., Mihailović-Vesić, J., Prodić, I., Minić, S. L., Stojadinović, M. M., Radibratović, M., Milčić, M. K.,& Ćirković-Veličković, T. (2016). Supplementary material for the article: Al-Hanish, A.; Stanic-Vucinic, D.; Mihailovic, J.; Prodic, I.; Minic, S.; Stojadinovic, M.; Radibratovic, M.; Milcic, M.; Cirkovic Velickovic, T. Noncovalent Interactions of Bovine α-Lactalbumin with Green Tea Polyphenol, Epigalocatechin-3-Gallate. Food Hydrocolloids 2016, 61, 241–250. https://doi.org/10.1016/j.foodhyd.2016.05.012.
Food Hydrocolloids
Elsevier Sci Ltd, Oxford..
Al-Hanish A, Stanić-Vučinić D, Mihailović-Vesić J, Prodić I, Minić SL, Stojadinović MM, Radibratović M, Milčić MK, Ćirković-Veličković T. Supplementary material for the article: Al-Hanish, A.; Stanic-Vucinic, D.; Mihailovic, J.; Prodic, I.; Minic, S.; Stojadinovic, M.; Radibratovic, M.; Milcic, M.; Cirkovic Velickovic, T. Noncovalent Interactions of Bovine α-Lactalbumin with Green Tea Polyphenol, Epigalocatechin-3-Gallate. Food Hydrocolloids 2016, 61, 241–250. https://doi.org/10.1016/j.foodhyd.2016.05.012. Food Hydrocolloids. 2016;
Al-Hanish Ayah, Stanić-Vučinić Dragana, Mihailović-Vesić Jelena, Prodić Ivana, Minić Simeon L., Stojadinović Marija M., Radibratović Milica, Milčić Miloš K., Ćirković-Veličković Tanja, "Supplementary material for the article: Al-Hanish, A.; Stanic-Vucinic, D.; Mihailovic, J.; Prodic, I.; Minic, S.; Stojadinovic, M.; Radibratovic, M.; Milcic, M.; Cirkovic Velickovic, T. Noncovalent Interactions of Bovine α-Lactalbumin with Green Tea Polyphenol, Epigalocatechin-3-Gallate. Food Hydrocolloids 2016, 61, 241–250. https://doi.org/10.1016/j.foodhyd.2016.05.012" Food Hydrocolloids (2016)

Supplementary material for the article: Radibratovic, M.; Minic, S.; Stanic-Vucinic, D.; Nikolic, M.; Milcic, M.; Velickovic, T. C. Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study. PLoS ONE 2016, 11 (12). https://doi.org/10.1371/journal.pone.0167973

Radibratović, Milica; Minić, Simeon L.; Stanić-Vučinić, Dragana; Nikolić, Milan; Milčić, Miloš K.; Ćirković-Veličković, Tanja

(Public Library Science, San Francisco, 2016)

TY  - BOOK
AU  - Radibratović, Milica
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3614
PB  - Public Library Science, San Francisco
T2  - PLoS One / Public Library of Science
T1  - Supplementary material for the article: Radibratovic, M.; Minic, S.; Stanic-Vucinic, D.; Nikolic, M.; Milcic, M.; Velickovic, T. C. Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study. PLoS ONE 2016, 11 (12). https://doi.org/10.1371/journal.pone.0167973
ER  - 
@book{
author = "Radibratović, Milica and Minić, Simeon L. and Stanić-Vučinić, Dragana and Nikolić, Milan and Milčić, Miloš K. and Ćirković-Veličković, Tanja",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3614",
publisher = "Public Library Science, San Francisco",
journal = "PLoS One / Public Library of Science",
title = "Supplementary material for the article: Radibratovic, M.; Minic, S.; Stanic-Vucinic, D.; Nikolic, M.; Milcic, M.; Velickovic, T. C. Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study. PLoS ONE 2016, 11 (12). https://doi.org/10.1371/journal.pone.0167973"
}
Radibratović, M., Minić, S. L., Stanić-Vučinić, D., Nikolić, M., Milčić, M. K.,& Ćirković-Veličković, T. (2016). Supplementary material for the article: Radibratovic, M.; Minic, S.; Stanic-Vucinic, D.; Nikolic, M.; Milcic, M.; Velickovic, T. C. Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study. PLoS ONE 2016, 11 (12). https://doi.org/10.1371/journal.pone.0167973.
PLoS One / Public Library of Science
Public Library Science, San Francisco..
Radibratović M, Minić SL, Stanić-Vučinić D, Nikolić M, Milčić MK, Ćirković-Veličković T. Supplementary material for the article: Radibratovic, M.; Minic, S.; Stanic-Vucinic, D.; Nikolic, M.; Milcic, M.; Velickovic, T. C. Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study. PLoS ONE 2016, 11 (12). https://doi.org/10.1371/journal.pone.0167973. PLoS One / Public Library of Science. 2016;
Radibratović Milica, Minić Simeon L., Stanić-Vučinić Dragana, Nikolić Milan, Milčić Miloš K., Ćirković-Veličković Tanja, "Supplementary material for the article: Radibratovic, M.; Minic, S.; Stanic-Vucinic, D.; Nikolic, M.; Milcic, M.; Velickovic, T. C. Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study. PLoS ONE 2016, 11 (12). https://doi.org/10.1371/journal.pone.0167973" PLoS One / Public Library of Science (2016)

Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity

Apostolović, Danijela; Stanić-Vučinić, Dragana; de Jongh, Harmen H. J.; de Jong, Govardus A. H.; Mihailović-Vesić, Jelena; Radosavljević, Jelena; Radibratović, Milica; Nordlee, Julie A.; Baumert, Joseph L.; Milčić, Miloš K.; Taylor, Steve L.; Clua, Nuria Garrido; Ćirković-Veličković, Tanja; Koppelman, Stef J.

(Nature Publishing Group, London, 2016)

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Stanić-Vučinić, Dragana
AU  - de Jongh, Harmen H. J.
AU  - de Jong, Govardus A. H.
AU  - Mihailović-Vesić, Jelena
AU  - Radosavljević, Jelena
AU  - Radibratović, Milica
AU  - Nordlee, Julie A.
AU  - Baumert, Joseph L.
AU  - Milčić, Miloš K.
AU  - Taylor, Steve L.
AU  - Clua, Nuria Garrido
AU  - Ćirković-Veličković, Tanja
AU  - Koppelman, Stef J.
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2273
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 = "Apostolović, Danijela and Stanić-Vučinić, Dragana and de Jongh, Harmen H. J. and de Jong, Govardus A. H. and Mihailović-Vesić, Jelena and Radosavljević, Jelena and Radibratović, Milica and Nordlee, Julie A. and Baumert, Joseph L. and Milčić, Miloš K. and Taylor, Steve L. and Clua, Nuria Garrido and Ćirković-Veličković, Tanja and Koppelman, Stef J.",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2273",
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"
}
Apostolović, D., Stanić-Vučinić, D., de Jongh, H. H. J., de Jong, G. A. H., Mihailović-Vesić, J., Radosavljević, J., Radibratović, M., Nordlee, J. A., Baumert, J. L., Milčić, M. K., 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.
Scientific Reports
Nature Publishing Group, London., 6.
https://doi.org/10.1038/srep29249
Apostolović D, Stanić-Vučinić D, de Jongh HHJ, de Jong GAH, Mihailović-Vesić J, Radosavljević J, Radibratović M, Nordlee JA, Baumert JL, Milčić MK, 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. Scientific Reports. 2016;6
Apostolović Danijela, Stanić-Vučinić Dragana, de Jongh Harmen H. J., de Jong Govardus A. H., Mihailović-Vesić Jelena, Radosavljević Jelena, Radibratović Milica, Nordlee Julie A., Baumert Joseph L., Milčić Miloš K., 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" Scientific Reports, 6 (2016),
https://doi.org/10.1038/srep29249 .
9
43
39
41

Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate

Al-Hanish, Ayah; Stanić-Vučinić, Dragana; Mihailović-Vesić, Jelena; Prodić, Ivana; Minić, Simeon L.; Stojadinović, Marija M.; Radibratović, Milica; Milčić, Miloš K.; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2016)

TY  - JOUR
AU  - Al-Hanish, Ayah
AU  - Stanić-Vučinić, Dragana
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Minić, Simeon L.
AU  - Stojadinović, Marija M.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2299
AB  - Bovine alpha-lactalbumin (ALA) is an important Ca-binding protein of milk. Epigallocatechin-3-gallate (EGCG) is the major and the most biologically active catechin of green tea, which has the highest binding affinity to whey proteins due to galloyl functional group. In this study experimental and computational methods were used to investigate noncovalent interactions of EGCG and ALA. Binding affinity of EGCG for ALA, determined by fluorescence quenching analysis, was in the range described for complexes of EGCG and other dietary proteins, and lower than affinity of some phenolic compounds to ALA. Based on circular dichroism and Fourier transform infrared spectroscopy spectra, binding of EGCG change ALA conformation inducing alpha-helix to beta-structures transition. The isothermal titration calorimetry results suggest that the binding of EGCG to ALA is enthalpically favorable. The docking analysis shows that EGCG binds in the hydrophobic pocket at the entrance of cleft between alpha-helical and beta-sheetrich domains and includes residues of aromatic cluster II. Uptake of ALA by monocytes proceeds at a slower rate in the presence of EGCG suggesting that EGCG binding may impair uptake of ALA by antigen-presenting cells. ALA, being of low cost and widely available protein, can serve as suitable delivery system for EGCG, as well as for food fortification with this bioactive catechin. (C) 2016 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Hydrocolloids
T1  - Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate
VL  - 61
SP  - 241
EP  - 250
DO  - 10.1016/j.foodhyd.2016.05.012
ER  - 
@article{
author = "Al-Hanish, Ayah and Stanić-Vučinić, Dragana and Mihailović-Vesić, Jelena and Prodić, Ivana and Minić, Simeon L. and Stojadinović, Marija M. and Radibratović, Milica and Milčić, Miloš K. and Ćirković-Veličković, Tanja",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2299",
abstract = "Bovine alpha-lactalbumin (ALA) is an important Ca-binding protein of milk. Epigallocatechin-3-gallate (EGCG) is the major and the most biologically active catechin of green tea, which has the highest binding affinity to whey proteins due to galloyl functional group. In this study experimental and computational methods were used to investigate noncovalent interactions of EGCG and ALA. Binding affinity of EGCG for ALA, determined by fluorescence quenching analysis, was in the range described for complexes of EGCG and other dietary proteins, and lower than affinity of some phenolic compounds to ALA. Based on circular dichroism and Fourier transform infrared spectroscopy spectra, binding of EGCG change ALA conformation inducing alpha-helix to beta-structures transition. The isothermal titration calorimetry results suggest that the binding of EGCG to ALA is enthalpically favorable. The docking analysis shows that EGCG binds in the hydrophobic pocket at the entrance of cleft between alpha-helical and beta-sheetrich domains and includes residues of aromatic cluster II. Uptake of ALA by monocytes proceeds at a slower rate in the presence of EGCG suggesting that EGCG binding may impair uptake of ALA by antigen-presenting cells. ALA, being of low cost and widely available protein, can serve as suitable delivery system for EGCG, as well as for food fortification with this bioactive catechin. (C) 2016 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Hydrocolloids",
title = "Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate",
volume = "61",
pages = "241-250",
doi = "10.1016/j.foodhyd.2016.05.012"
}
Al-Hanish, A., Stanić-Vučinić, D., Mihailović-Vesić, J., Prodić, I., Minić, S. L., Stojadinović, M. M., Radibratović, M., Milčić, M. K.,& Ćirković-Veličković, T. (2016). Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate.
Food Hydrocolloids
Elsevier Sci Ltd, Oxford., 61, 241-250.
https://doi.org/10.1016/j.foodhyd.2016.05.012
Al-Hanish A, Stanić-Vučinić D, Mihailović-Vesić J, Prodić I, Minić SL, Stojadinović MM, Radibratović M, Milčić MK, Ćirković-Veličković T. Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate. Food Hydrocolloids. 2016;61:241-250
Al-Hanish Ayah, Stanić-Vučinić Dragana, Mihailović-Vesić Jelena, Prodić Ivana, Minić Simeon L., Stojadinović Marija M., Radibratović Milica, Milčić Miloš K., Ćirković-Veličković Tanja, "Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate" Food Hydrocolloids, 61 (2016):241-250,
https://doi.org/10.1016/j.foodhyd.2016.05.012 .
2
57
44
56

Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study

Radibratović, Milica; Minić, Simeon L.; Stanić-Vučinić, Dragana; Nikolić, Milan; Milčić, Miloš K.; Ćirković-Veličković, Tanja

(Public Library Science, San Francisco, 2016)

TY  - JOUR
AU  - Radibratović, Milica
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1948
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 / Public Library of Science
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 L. and Stanić-Vučinić, Dragana and Nikolić, Milan and Milčić, Miloš K. and Ćirković-Veličković, Tanja",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1948",
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 / Public Library of Science",
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. L., Stanić-Vučinić, D., Nikolić, M., Milčić, M. K.,& 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.
PLoS One / Public Library of Science
Public Library Science, San Francisco., 11(12).
https://doi.org/10.1371/journal.pone.0167973
Radibratović M, Minić SL, Stanić-Vučinić D, Nikolić M, Milčić MK, 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. PLoS One / Public Library of Science. 2016;11(12)
Radibratović Milica, Minić Simeon L., Stanić-Vučinić Dragana, Nikolić Milan, Milčić Miloš K., 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" PLoS One / Public Library of Science, 11, no. 12 (2016),
https://doi.org/10.1371/journal.pone.0167973 .
4
16
9
10

Supplementary data for article: Minic, S. L.; Milcic, M.; Stanic-Vucinic, D.; Radibratovic, M.; Sotiroudis, T. G.; Nikolic, M. R.; Velickovic, T. C. Phycocyanobilin, a Bioactive Tetrapyrrolic Compound of Blue-Green Alga Spirulina, Binds with High Affinity and Competes with Bilirubin for Binding on Human Serum Albumin. RSC Advances 2015, 5 (76), 61787–61798. https://doi.org/10.1039/c5ra05534b

Minić, Simeon L.; Milčić, Miloš K.; Stanić-Vučinić, Dragana; Radibratović, Milica; Sotiroudis, Theodore G.; Nikolić, Milan; Ćirković-Veličković, Tanja

(Royal Soc Chemistry, Cambridge, 2015)

TY  - BOOK
AU  - Minić, Simeon L.
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Radibratović, Milica
AU  - Sotiroudis, Theodore G.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3403
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Supplementary data for article: Minic, S. L.; Milcic, M.; Stanic-Vucinic, D.; Radibratovic, M.; Sotiroudis, T. G.; Nikolic, M. R.; Velickovic, T. C. Phycocyanobilin, a Bioactive Tetrapyrrolic Compound of Blue-Green Alga Spirulina, Binds with High Affinity and Competes with Bilirubin for Binding on Human Serum Albumin. RSC Advances 2015, 5 (76), 61787–61798. https://doi.org/10.1039/c5ra05534b
ER  - 
@book{
author = "Minić, Simeon L. and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Radibratović, Milica and Sotiroudis, Theodore G. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2015",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3403",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Supplementary data for article: Minic, S. L.; Milcic, M.; Stanic-Vucinic, D.; Radibratovic, M.; Sotiroudis, T. G.; Nikolic, M. R.; Velickovic, T. C. Phycocyanobilin, a Bioactive Tetrapyrrolic Compound of Blue-Green Alga Spirulina, Binds with High Affinity and Competes with Bilirubin for Binding on Human Serum Albumin. RSC Advances 2015, 5 (76), 61787–61798. https://doi.org/10.1039/c5ra05534b"
}
Minić, S. L., Milčić, M. K., Stanić-Vučinić, D., Radibratović, M., Sotiroudis, T. G., Nikolić, M.,& Ćirković-Veličković, T. (2015). Supplementary data for article: Minic, S. L.; Milcic, M.; Stanic-Vucinic, D.; Radibratovic, M.; Sotiroudis, T. G.; Nikolic, M. R.; Velickovic, T. C. Phycocyanobilin, a Bioactive Tetrapyrrolic Compound of Blue-Green Alga Spirulina, Binds with High Affinity and Competes with Bilirubin for Binding on Human Serum Albumin. RSC Advances 2015, 5 (76), 61787–61798. https://doi.org/10.1039/c5ra05534b.
RSC Advances
Royal Soc Chemistry, Cambridge..
Minić SL, Milčić MK, Stanić-Vučinić D, Radibratović M, Sotiroudis TG, Nikolić M, Ćirković-Veličković T. Supplementary data for article: Minic, S. L.; Milcic, M.; Stanic-Vucinic, D.; Radibratovic, M.; Sotiroudis, T. G.; Nikolic, M. R.; Velickovic, T. C. Phycocyanobilin, a Bioactive Tetrapyrrolic Compound of Blue-Green Alga Spirulina, Binds with High Affinity and Competes with Bilirubin for Binding on Human Serum Albumin. RSC Advances 2015, 5 (76), 61787–61798. https://doi.org/10.1039/c5ra05534b. RSC Advances. 2015;
Minić Simeon L., Milčić Miloš K., Stanić-Vučinić Dragana, Radibratović Milica, Sotiroudis Theodore G., Nikolić Milan, Ćirković-Veličković Tanja, "Supplementary data for article: Minic, S. L.; Milcic, M.; Stanic-Vucinic, D.; Radibratovic, M.; Sotiroudis, T. G.; Nikolic, M. R.; Velickovic, T. C. Phycocyanobilin, a Bioactive Tetrapyrrolic Compound of Blue-Green Alga Spirulina, Binds with High Affinity and Competes with Bilirubin for Binding on Human Serum Albumin. RSC Advances 2015, 5 (76), 61787–61798. https://doi.org/10.1039/c5ra05534b" RSC Advances (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

Minić, Simeon L.; Milčić, Miloš K.; Stanić-Vučinić, Dragana; Radibratović, Milica; Sotiroudis, Theodore G.; Nikolić, Milan; Ćirković-Veličković, Tanja

(Royal Soc Chemistry, Cambridge, 2015)

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Radibratović, Milica
AU  - Sotiroudis, Theodore G.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1741
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 L. and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Radibratović, Milica and Sotiroudis, Theodore G. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2015",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1741",
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. L., Milčić, M. K., 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.
RSC Advances
Royal Soc Chemistry, Cambridge., 5(76), 61787-61798.
https://doi.org/10.1039/c5ra05534b
Minić SL, Milčić MK, 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. RSC Advances. 2015;5(76):61787-61798
Minić Simeon L., Milčić Miloš K., 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" RSC Advances, 5, no. 76 (2015):61787-61798,
https://doi.org/10.1039/c5ra05534b .
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