Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/118270
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Type: Journal article
Title: C-Phycocyanin from Spirulina Inhibits α-synuclein and amyloid-β fibril formation but not amorphous aggregation
Other Titles: C-Phycocyanin from Spirulina Inhibits alpha-synuclein and amyloid-beta fibril formation but not amorphous aggregation
Author: Liu, Y.
Jovcevski, B.
Pukala, T.
Citation: Journal of Natural Products, 2019; 82(1):66-73
Publisher: American Chemical Society
Issue Date: 2019
ISSN: 0163-3864
1520-6025
Statement of
Responsibility: 
Yanqin Liu, Blagojce Jovcevski and Tara L. Pukala
Abstract: Proteinopathies including cataracts and neurodegenerative diseases, such as Alzheimer's and Parkinson's disease, are characterized by a series of aberrant protein folding events, resulting in amorphous aggregate or amyloid fibril formation. In the latter case, research has heavily focused on the development of small-molecule inhibitors with limited success during clinical trials. However, very few studies have focused on utilizing exogenous proteins as potential aggregation inhibitors. C-Phycocyanin, derived from Spirulina sp., has been known to exert anti-inflammatory properties; however, the ability of C-phycocyanin to inhibit protein aggregation has yet to be investigated. We have demonstrated that C-phycocyanin is an effective inhibitor of A53Tα-synuclein at extremely low substoichiometric ratios (200-fold excess of α-synuclein) and Aβ40/42 fibril formation. However, C-phycocyanin is relatively ineffective in inhibiting the reduction-induced amorphous aggregation of ADH and heat-induced aggregation of catalase. In addition, 2D NMR, ion mobility-mass spectrometry, and analytical-SEC demonstrate that the interaction between C-phycocyanin and α-synuclein is through nonstable interactions, indicating that transient interactions are likely to be responsible for preventing fibril formation. Overall, this work highlights how biomolecules from natural sources could be used to aid in the development of therapeutics to combat protein misfolding diseases.
Rights: © 2019 American Chemical Society and American Society of Pharmacognosy
RMID: 0030106502
DOI: 10.1021/acs.jnatprod.8b00610
Grant ID: http://purl.org/au-research/grants/arc/DP1093143
http://purl.org/au-research/grants/arc/DP170102033
Appears in Collections:Biochemistry publications

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