Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin
Open accessAbstract
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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- 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
- bronze
- doi.org
- 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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Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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