Exploring the Formation of Polymers with Anti-Amyloid Properties within the 2'3'-Dihydroxyflavone Autoxidation Process.
Antioxidants (Basel, Switzerland)(2022)
Abstract
Amyloid-β and α-synuclein aggregation into amyloid fibrils is linked to the onset and progression of Alzheimer's and Parkinson's diseases. While there are only a few disease-modifying drugs, it is essential to search for new, more effective ways to encounter these neurodegenerative diseases. Multiple research articles have shown that the autoxidation of flavone is a critical factor for activating the inhibitory potential against the protein aggregation. Despite this, the structure of the newly-formed inhibitors is unknown. In this research, we examined the autoxidation products of 2',3'-dihydroxyflavone that were previously shown to possess one of the most prominent inhibitory effects against amyloid-β aggregation. Their analysis using HPLC suggested the formation of polymeric molecules that were isolated using a 3 kDa cut-off. These polymeric structures were indicated as the most potent inhibitors based on protein aggregation kinetics and AFM studies. This revelation was confirmed using MALDI-TOF and NMR. We also show that active molecules have a tendency to reduce the Amyloid-β and α-synuclein aggregates toxicity to SH-SY5Y cells.
MoreTranslated text
Key words
aggregation,alpha-synuclein,amyloid-beta,autoxidation,flavone,inhibition,polymers
AI Read Science
Must-Reading Tree
Example
![](https://originalfileserver.aminer.cn/sys/aminer/pubs/mrt_preview.jpeg)
Generate MRT to find the research sequence of this paper
Chat Paper
Summary is being generated by the instructions you defined