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

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2018
1_1007_10.1016j.foodchem.2018.06.138.pdf (1.489Mb)
Authors
Minic, Simeon
Radomirović, Mirjana
Savkovic, Nina
Radibratović, Milica
Mihailović, Jelena
Vasovic, Tamara
Nikolić, Milan
Milčić, Miloš
Stanić-Vučinić, Dragana
Ćirković Veličković, Tanja
Article (Accepted Version)
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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 th...is adduct can serve as delivery system of bioactive PCB.

Keywords:
beta-lactoglobulin / Phycocyanobilin / Phycocyanin / Covalent / Binding / Spirulina / Fluorescence / Molecular docking
Source:
Food Chemistry, 2018, 269, 43-52
Publisher:
  • Elsevier Sci Ltd, Oxford
Funding / projects:
  • Molecular properties and modifications of some respiratory and nutritional allergens (RS-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-256716)
Note:
  • This is peer-reviewed version of the article: Minic, S., Radomirovic, M., Savkovic, N., Radibratovic, M., Mihailovic, J., Vasovic, T., Nikolic, M., Milcic, M., Stanic-Vucinic, D., Velickovic, T.C., Covalent binding of food-derived blue pigment phycocyanobilin to bovine β-lactoglobulin under physiological conditions, Food Chemistry, 2018, 269, 43-52, doi: https://doi.org/10.1016/j.foodchem.2018.06.138
  • http://cer.ihtm.bg.ac.rs/handle/123456789/2420

DOI: 10.1016/j.foodchem.2018.06.138

ISSN: 0308-8146

PubMed: 30100456

WoS: 000441142100006

Scopus: 2-s2.0-85049319228
[ Google Scholar ]
6
5
URI
https://cer.ihtm.bg.ac.rs/handle/123456789/3022
Collections
  • Radovi istraživača / Researchers' publications
Institution/Community
IHTM
TY  - JOUR
AU  - Minic, Simeon
AU  - Radomirović, Mirjana
AU  - Savkovic, Nina
AU  - Radibratović, Milica
AU  - Mihailović, Jelena
AU  - Vasovic, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković Veličković, Tanja
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3022
AB  - In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions
VL  - 269
SP  - 43
EP  - 52
DO  - 10.1016/j.foodchem.2018.06.138
ER  - 
@article{
author = "Minic, Simeon and Radomirović, Mirjana and Savkovic, Nina and Radibratović, Milica and Mihailović, Jelena and Vasovic, Tamara and Nikolić, Milan and Milčić, Miloš and Stanić-Vučinić, Dragana and Ćirković Veličković, Tanja",
year = "2018",
abstract = "In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions",
volume = "269",
pages = "43-52",
doi = "10.1016/j.foodchem.2018.06.138"
}
Minic, S., Radomirović, M., Savkovic, N., Radibratović, M., Mihailović, J., Vasovic, T., Nikolić, M., Milčić, M., Stanić-Vučinić, D.,& Ćirković Veličković, T.. (2018). Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. in Food Chemistry
Elsevier Sci Ltd, Oxford., 269, 43-52.
https://doi.org/10.1016/j.foodchem.2018.06.138
Minic S, Radomirović M, Savkovic N, Radibratović M, Mihailović J, Vasovic T, Nikolić M, Milčić M, Stanić-Vučinić D, Ćirković Veličković T. Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. in Food Chemistry. 2018;269:43-52.
doi:10.1016/j.foodchem.2018.06.138 .
Minic, Simeon, Radomirović, Mirjana, Savkovic, Nina, Radibratović, Milica, Mihailović, Jelena, Vasovic, Tamara, Nikolić, Milan, Milčić, Miloš, Stanić-Vučinić, Dragana, Ćirković Veličković, Tanja, "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions" in Food Chemistry, 269 (2018):43-52,
https://doi.org/10.1016/j.foodchem.2018.06.138 . .

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