Molecular Interaction of Protein-Pigment C-Phycocyanin with Bovine Serum Albumin in a Gomphosis Structure Inhibiting Amyloid Formation
Open accessAbstract
Accumulation of amyloid fibrils in organisms accompanies many diseases. Natural extracts offer an alternative strategy to control the process with potentially fewer side effects. In this study, the inhibition of C-phycocyanin from Spirulina sp. on amyloid formation of bovine serum albumin (BSA) during a 21-day incubation was investigated using fluorescence and circular dichroism (CD), and mechanisms were explored via kinetic fitting and molecular docking. C-phycocyanin (0–50 µg/mL) hindered the amyloid formation process of BSA with increased half-lives (12.43–17.73 days) based on fluorescence intensity. A kinetic model was built and showed that the k1 decreased from 1.820 × 10−2 d−1 to 2.62 × 10−3 d−1 with the increase of C-phycocyanin, while k2 showed no changes, indicating that the inhibition of BSA fibrillation by C-phycocyanin occurred in a spontaneous process instead of self-catalyzed one. CD results show that C-phycocyanin inhibited conformational conversion (α-helices and β-sheets) of BSA from day 6 to day 18. Molecular docking suggested that C-phycocyanin may hinder BSA fibrillation by hydrogen-bonding > 6 of 27 α-helices of BSA in a gomphosis-like structure, but the unblocked BSA α-helices might follow the self-catalytic process subsequently.
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C-PC hinders the amyloid formation process of bovine serum albumin, inhibiting conformational conversion of α-helices and β-sheets of bovine serum albumin.
“Luo and Jing demonstrated that C-PC is able to hinder the amyloid formation process of bovine serum albumin (BSA), inhibiting conformational conversion (α-helices and β-sheets) of BSA [136].”
From Beneficial Effects of Spirulina Consumption on Brain Health (2022) · cites this paper as [136]
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Beneficial Effects of Spirulina Consumption on Brain Health
Trotta, T., Porro, C., Cianciulli, A., & Panaro, M. A. (2022) · Nutrients · doi:10.3390/nu14030676 · Cited by 98 · see citing works
- Authors
- Luo, Y.-C., & Jing, P.
- Affiliations
- Shanghai Jiao Tong University (CN)
- Corresponding author
- Jing, Pu
- ORCID
- Jing, Pu
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2020-11-02
- Volume
- 21
- Issue
- 21
- Pages
- 8207
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC7663302
- OpenAlex
- W3097474367
- Cited by
- 9
- References
- 42
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 4 · 2022: 2
- FWCI
- 0.49
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Natural Science Foundation of China (21978169)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- C-phycocyanin, bovine serum albumin, amyloid fibrillation inhibition, protein-protein interaction, Spirulina, protein conformational change, hydrogen bonding, amyloidosis
- MeSH terms
- Cyanobacteria, Amyloid, Animals, Catalysis, Cattle, Circular Dichroism, Hydrogen Bonding, Kinetics, Microscopy, Fluorescence, Phycocyanin, Pigmentation, Protein Binding, Serum Albumin, Bovine, Protein Structure, Secondary, Benzothiazoles, Spirulina, Molecular Docking Simulation
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