Abstract
The inhibition of fibril formation of amyloid β proteins (Aβ) would be attractive therapeutic targets for the treatment of Alzheimer's disease (AD). Dopamine (DA) and other catechol derivatives were used as inhibitory factors for Aβ fibril formation. The fibril formation of Aβ was monitored by Thioflavin T fluorescence, a transmission electron microscopy (TEM) and a total internal reflection fluorescence microscopy (TIRFM). Catechol and its derivatives showed the dose-dependent inhibitory effects on the spontaneous Aβ fibril formation. The inhibitory activity depended on the chemical structure of catechol derivatives both in the presence and absence of the liposome a model of biomembrane. Formation of catechol quinone-conjugated-Aβ adduct by a Schiff-base is a key step for the inhibition effect of Aβ fibril formation.
Original language | English |
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Pages (from-to) | 629-634 |
Number of pages | 6 |
Journal | Journal of Bioscience and Bioengineering |
Volume | 109 |
Issue number | 6 |
DOIs | |
Publication status | Published - Jun 2010 |
Externally published | Yes |
Keywords
- Alzheimer's disease
- Amyloid beta
- Catechol derivatives
- Fibril formation
- Inhibitor
- Liposome
ASJC Scopus subject areas
- Biotechnology
- Bioengineering
- Applied Microbiology and Biotechnology