Cited by 45Protein Interaction Studies and Fluorescence AnalysisProteins in Food SystemsHemoglobin structure and function

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

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Minic, Simeon, Stanic-Vucinic, Dragana, Radomirovic, Mirjana, Radibratovic, Milica, Milcic, Milos, Nikolic, Milan, Cirkovic Velickovic, Tanja·2018·Food Chemistry

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=2×10 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.

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Crossref · 10.1016/j.foodchem.2017.07.066

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Authors
Minic, S., Stanic-Vucinic, D., Radomirovic, M., Radibratovic, M., Milcic, M., Nikolic, M., & Cirkovic Velickovic, T.
Affiliations
University of Belgrade (RS)
Venue
Food Chemistry
Publisher
Elsevier BV
Published
2018-01
Volume
239
Pages
1090-1099
ISSN
0308-8146 (ISSN-L)
OpenAlex
W2735839599
Cited by
45
References
43
Citations by year
2026: 5 · 2025: 4 · 2024: 4 · 2023: 7 · 2022: 5 · 2021: 4 · 2020: 6 · 2019: 2 · 2018: 8
FWCI
1.79
Type
journal article
Language
en
Open access
Locations
  • Food Chemistry (publishedVersion)
  • PubMed (publishedVersion)
  • Ghent University Academic Bibliography (Ghent University) (submittedVersion, other-oa)
  • CER (University of Belgrade, Institute of Chemistry, Technology and Metallurgy) (submittedVersion, other-oa)
  • CER (University of Belgrade, Institute of Chemistry, Technology and Metallurgy) (submittedVersion)
  • CER (University of Belgrade, Institute of Chemistry, Technology and Metallurgy) (submittedVersion, cc-by-nc-nd)
  • Cherry (Univesrity of Belgrade, Faculty of Chemistry) (submittedVersion)
  • Cherry (Univesrity of Belgrade, Faculty of Chemistry) (submittedVersion, cc-by-nc-nd)
Funders
  • European Commission (256716)
  • Ministarstvo Prosvete, Nauke i Tehnološkog Razvoja (172024)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
Keywords
phycocyanobilin, bovine serum albumin, protein-ligand binding, C-phycocyanin, Spirulina, tetrapyrrole chromophore, binding sites, protein thermal stability, antioxidant activity, free radical oxidation, food colorants, binding affinity
MeSH terms
Animals, Binding Sites, Cattle, Humans, Phycocyanin, Protein Binding, Serum Albumin, Bovine, Spectrometry, Fluorescence, Phycobilins, Molecular Docking Simulation

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