Inhibitory effect of TA9902 on amyloid ?-peptide 1-42 aggregation by Fourier-transform infrared spectroscopy study
- VernacularTitle:FT-IR光谱法研究TA9902抑制A?_(1-42)聚集的分子机制
- Author:
Guangwu LI
;
Huaqiao WANG
;
Zhibin YAO
- Publication Type:Journal Article
- Keywords:
Alzheimer disease;
Amyloid beta-protein;
Spectroscopy, Fourier transform infrared
- From:
Chinese Journal of Pathophysiology
1986;0(01):-
- CountryChina
- Language:Chinese
-
Abstract:
AIM: To investigate the mechanism by which TA9902 inhibits the formation of amyloid ?-peptide (A?) fibrils. METHODS: Fourier-transform infrared spectroscopy was used to study the secondary structure changes on aging A? in vitro. RESULTS: The content of ?-pleated sheet were 46.53% in the condition of A? aged alone for 30 min. When A? aged alone for 72 h, the content of ?-pleated sheet increased about 19.4% and produced a shift of random coil toward ?-pleated sheet. TA9902 induced a significant decrease in the content of ?-pleated sheet (36.09%). CONCLUSION: TA9902 effectively diminishes the ?-pleated structural content. The effect of TA9902 on the secondary structure of aged A? is associated with inhibition of A? aggregation and fibril formation.
