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Molecular Interaction of Protein-Pigment C-Phycocyanin with Bovine Serum Albumin in a Gomphosis Structure Inhibiting Amyloid Formation

by and *
Shanghai Food Safety and Engineering Technology Research Center, Bor S. Luh Food Safety Research Center, Key Lab of Urban Agriculture (South), School of Agriculture & Biology, Shanghai Jiao Tong University, Shanghai 200240, China
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Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(21), 8207; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21218207
Received: 29 August 2020 / Revised: 20 October 2020 / Accepted: 20 October 2020 / Published: 2 November 2020
(This article belongs to the Section Molecular Biology)
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. View Full-Text
Keywords: C-phycocyanin; blue food pigment; secondary interaction; fibrillation; non-covalent interaction C-phycocyanin; blue food pigment; secondary interaction; fibrillation; non-covalent interaction
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MDPI and ACS Style

Luo, Y.-C.; Jing, P. Molecular Interaction of Protein-Pigment C-Phycocyanin with Bovine Serum Albumin in a Gomphosis Structure Inhibiting Amyloid Formation. Int. J. Mol. Sci. 2020, 21, 8207. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21218207

AMA Style

Luo Y-C, Jing P. Molecular Interaction of Protein-Pigment C-Phycocyanin with Bovine Serum Albumin in a Gomphosis Structure Inhibiting Amyloid Formation. International Journal of Molecular Sciences. 2020; 21(21):8207. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21218207

Chicago/Turabian Style

Luo, Yi-Cong, and Pu Jing. 2020. "Molecular Interaction of Protein-Pigment C-Phycocyanin with Bovine Serum Albumin in a Gomphosis Structure Inhibiting Amyloid Formation" International Journal of Molecular Sciences 21, no. 21: 8207. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21218207

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