Inhibitory effect of TA9902 on amyloid ?-peptide 1-42 aggregation by Fourier-transform infrared spectroscopy study / 中国病理生理杂志

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.