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

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2018
1_k_jfoodchem.2017.07.066.pdf (936.8Kb)
Authors
Minic, Simeon
Stanić-Vučinić, Dragana
Radomirović, Mirjana
Radibratović, Milica
Milčić, Miloš
Nikolić, Milan
Ćirković Veličković, Tanja
Article (Accepted Version)
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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 PC...B binding to bovine vs. human serum albumin.

Keywords:
Spirulina / Phycocyanobilin / Bovine serum albumin / Binding / Stability / Antioxidant
Source:
Food Chemistry, 2018, 239, 1090-1099
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 following 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
  • http://cer.ihtm.bg.ac.rs/handle/123456789/2478

DOI: 10.1016/j.foodchem.2017.07.066

ISSN: 0308-8146

PubMed: 28873526

WoS: 000408740200129

Scopus: 2-s2.0-85024374977
[ Google Scholar ]
20
21
URI
https://cer.ihtm.bg.ac.rs/handle/123456789/2984
Collections
  • Radovi istraživača / Researchers' publications
Institution/Community
IHTM
TY  - JOUR
AU  - Minic, Simeon
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana
AU  - Radibratović, Milica
AU  - Milčić, Miloš
AU  - Nikolić, Milan
AU  - Ćirković Veličković, Tanja
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2984
AB  - Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (K-a = 2 x 10(6) M-1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin
VL  - 239
SP  - 1090
EP  - 1099
DO  - 10.1016/j.foodchem.2017.07.066
UR  - Conv_3779
ER  - 
@article{
author = "Minic, Simeon and Stanić-Vučinić, Dragana and Radomirović, Mirjana and Radibratović, Milica and Milčić, Miloš and Nikolić, Milan and Ćirković Veličković, Tanja",
year = "2018",
abstract = "Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (K-a = 2 x 10(6) M-1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin",
volume = "239",
pages = "1090-1099",
doi = "10.1016/j.foodchem.2017.07.066",
url = "Conv_3779"
}
Minic, S., Stanić-Vučinić, D., Radomirović, M., Radibratović, M., Milčić, M., Nikolić, M.,& Ćirković Veličković, T.. (2018). Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. in Food Chemistry
Elsevier Sci Ltd, Oxford., 239, 1090-1099.
https://doi.org/10.1016/j.foodchem.2017.07.066
Conv_3779
Minic S, Stanić-Vučinić D, Radomirović M, Radibratović M, Milčić M, Nikolić M, Ćirković Veličković T. Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. in Food Chemistry. 2018;239:1090-1099.
doi:10.1016/j.foodchem.2017.07.066
Conv_3779 .
Minic, Simeon, Stanić-Vučinić, Dragana, Radomirović, Mirjana, Radibratović, Milica, Milčić, Miloš, Nikolić, Milan, Ćirković Veličković, Tanja, "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin" in Food Chemistry, 239 (2018):1090-1099,
https://doi.org/10.1016/j.foodchem.2017.07.066 .,
Conv_3779 .

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