H102衍生物对β淀粉样蛋白聚集的抑制作用

Inhibitiory activities of H102 derivatives on aggregation of β-amyloid protein

目的:比较6种β片层阻断肽(H102、H102-1、H102-2、H102-3、DH102、LD-7)对β淀粉样蛋白(Aβ)聚集及纤维形成的影响,并进行药物筛选。方法:运用硫磺素T(ThT)荧光法以及傅里叶变换红外光谱法(FT-IR)分析6种β片层阻断肽对Aβ1-42聚集的影响。结果:6种β片层阻断肽及对照组维生素E对Aβ1-42聚集和纤维抑制率分别为:(14.168±0.038)%、(9.725±0.023)%、(22.535±0.013)%、(8.586±0.035)%、(5.37±0.019)%、(9.599±0.012)%、(12.736±0.026)%,提示H102-2的效果最佳;FT-IR结果也以H102-2的效果最佳。结论:H102-2对β淀粉样蛋白聚集和纤维抑制效果最佳。

Objective： To compare the effects of six β-sheet breaker （H102, H102-1, H102-2, H102-3, DH102, LD-7） on β-amyloid protein （Aβ） fibrous formation. Methods： The inhibitory effects of β-sheet breakers on Aβ1-42 fibrous formation were determined by using fluorescence analysis with Thioflavin T （ThT） and Fourier- transform infrared spectroscopy was used to study the secondary structure changes on aging Aβ in vitro. Results： β-sheet breakers and vitamin E inhibited the Aβ-42 aggregation and formation of amyloid fibrosis with the percentage inhibitory as follows： （ 14.168±0.038 ）%, （9.725±0.023）%, （22.535±0.013）%, （ 8.586±0.035 ）%, （5.37±0.019）%, （9.599±0.012 ）%, （ 12.736±0.026）%. FT-IR also revealed the best effect of H 102-2 than others. Conclusion： H 102-2 is much more ef- ficient than the others β-sheet breskers in inhibiting Aβ-42 aggregation.