| Title |
Exploring the formation of polymers with anti-amyloid properties within the 2'3'-dihydroxyflavone autoxidation process / |
| Authors |
Sakalauskas, Andrius ; Janonienė, Agnė ; Žvinys, Gediminas ; Mikalauskaitė, Kamilė ; Žiaunys, Mantas ; Smirnovas, Vytautas |
| DOI |
10.3390/antiox11091711 |
| Full Text |
|
| Is Part of |
Antioxidants.. Basel : MDPI. 2022, vol. 11, iss. 9, art. no. 1711, p. [1-12].. eISSN 2076-3921 |
| Keywords [eng] |
aggregation ; alpha-synuclein ; amyloid-beta ; autoxidation ; flavone ; inhibition ; polymers |
| Abstract [eng] |
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. |
| Published |
Basel : MDPI |
| Type |
Journal article |
| Language |
English |
| Publication date |
2022 |
| CC license |
|
