Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions
Autori
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
Članak u časopisu (Recenzirana verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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 th...is adduct can serve as delivery system of bioactive PCB.
Ključne reči:
beta-lactoglobulin / Phycocyanobilin / Phycocyanin / Covalent / Binding / Spirulina / Fluorescence / Molecular dockingIzvor:
Food Chemistry, 2018, 269, 43-52Izdavač:
- Elsevier Sci Ltd, Oxford
Finansiranje / projekti:
- Molekularne osobine i modifikacije nekih respiratornih i nutritivnih alergena (RS-MESTD-Basic Research (BR or ON)-172024)
- Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-FP7-256716)
Napomena:
- This is peer-reviewed version of the following 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
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3187
DOI: 10.1016/j.foodchem.2018.06.138
ISSN: 0308-8146
PubMed: 30100456
WoS: 000441142100006
Scopus: 2-s2.0-85049319228
Kolekcije
Institucija/grupa
Hemijski fakultet / Faculty of ChemistryTY - 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 - https://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", 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. in 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. in Food Chemistry. 2018;269:43-52. doi: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, "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions" in Food Chemistry, 269 (2018):43-52, https://doi.org/10.1016/j.foodchem.2018.06.138 . .