Effect of antioxidants on secondary conformational transition of aged amyloid ?-peptide_( 1-40) by FT-IR quantitative study
- VernacularTitle:傅里叶变换红外光谱法定量研究抗氧化剂对?-淀粉样蛋白_(1-40)老化过程中二级结构变化的影响
- Author:
Zhaoxue YU
;
Zhibin YAO
- Publication Type:Journal Article
- Keywords:
Alzheimer's disease;
Amyloid beta-protein;
Antioxidants;
Spectra, Fourier transform infrared
- From:
Chinese Journal of Pathophysiology
1989;0(06):-
- CountryChina
- Language:Chinese
-
Abstract:
AIM: To investigate the mechanism that antioxidants TA9901, inhibit the formation of amyloid-?-protein(A?) fibril. METHODS: Fourier-transform infrared spectroscopy was used to study the secondary structure changes on aging A? in vitro. RESULTS: A? aged alone for 30 min, the content of ?-pleated sheet and ?-turn were 43.17% and 32.9% respectively. A? aged alone for 7 days, the content of ?-pleated sheet increased abuot 10% and produced a shift of random coil toward ?-pleated sheet. TA9901 induced a significant decrease of the content of ?-turn (23.5%) and ?-pleated sheet (26.4%). VE mainly decreased the ?-pleated sheet content (30.8%). The combination of TA9901 and VE promoted transition of ?-turn (16.7%) toward ?-helix and random coil. CONCLUSIONS: Both of TA9901 and VE can effectively diminish the ?-structural content. TA9901 showed more intensitive inhibition than VE. The effect of TA9901 on the secondary structure of aged A? was associated with the mechanism that TA9901 inhibited A? aggregation and fibril formation.
