Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 182, Issue -, Pages 91-97Publisher
ELSEVIER
DOI: 10.1016/j.ijbiomac.2021.03.186
Keywords
Calycosin; alpha-Synuclein; Amyloid fibrils; Antioxidant activity; Spectroscopy; Neurotoxicity; Parkinson's diseases
Funding
- China Postdoctoral Science Foundation [2020M672291]
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The study demonstrated that calycosin significantly inhibits the fibril formation of α-syn in a concentration-dependent manner, preventing α-syn amyloid-triggered neurotoxicity. By modifying the aggregation pathway, calycosin promotes the formation of non-toxic species, restoring SOD/CAT activity and GSH content while reducing ROS levels and caspase-3 activity. This research provides valuable insights into the mechanism of α-syn amyloid inhibition by calycosin and suggests the development of small molecules-based therapeutic platforms for Parkinson's disease.
Protein misfolding and aggregation result in induction of a number of neurodegenerative diseases. In the present study, the anti-fibrillation activity of calycosin and its influence on the amyloid formation of alpha-synuclein (alpha-syn) and associated cytotoxicity on neuron-like cells (PC-12) as a model of Parkinson's disease were explored. Therefore, in combination with ThT and ANS fluorescence assay, CD, Congo red absorbance, TEM and cytotoxicity assays (MTT, ROS, SOD activity, CAT activity, GSH content, and caspase-3 activity assays), we showed that calycosin remarkably inhibits alpha-syn fibril formation through a concentration-dependent manner. The experimental analysis indicated that calycosin exert its antioxidant effects against alpha-syn amyloid-triggered neurotoxicity by modifying the aggregation pathway toward formation of nontoxic spices via recovering the activity of SOD/CAT and GSH content and reducing the ROS content and caspase-3 activity. This work may provide useful information about the mechanism of alpha-syn amyloid inhibition by calycosin and pave the way for developing some small molecules-based therapeutic platforms against Parkinson's disease. (c) 2021 Published by Elsevier B.V.
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