Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin
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2018
Authors
Minić, Simeon L.
Stanić-Vučinić, Dragana

Radomirović, Mirjana Ž.

Radibratović, Milica

Milčić, Miloš K.

Nikolić, Milan

Ćirković-Veličković, Tanja

Article (Published version)

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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 PC...B binding to bovine vs. human serum albumin. (C) 2017 Elsevier Ltd. All rights reserved.
Keywords:
Spirulina / Phycocyanobilin / Bovine serum albumin / Binding / Stability / AntioxidantSource:
Food Chemistry, 2018, 239, 1090-1099Publisher:
- Elsevier
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:
- Peer-reviewed article: http://cherry.chem.bg.ac.rs/handle/123456789/3035
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3139
DOI: 10.1016/j.foodchem.2017.07.066
ISSN: 0308-8146
PubMed: 28873526
WoS: 000408740200129
Scopus: 2-s2.0-85024374977
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Institution/Community
Hemijski fakultet / Faculty of ChemistryTY - 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 - https://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", 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. in 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. in Food Chemistry. 2018;239:1090-1099. doi: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, "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin" in Food Chemistry, 239 (2018):1090-1099, https://doi.org/10.1016/j.foodchem.2017.07.066 . .