黄芩素对β-淀粉样蛋白纤维化及其细胞毒性的影响

摘要

Objective To investigate the effects of baicalein on the fibrillation and cytotoxicity of amyloid p-protein Aβ1-42. Methods The inhibitory effects of baicalein on Aβ1-42 fibril formation were determined by using thioflavin T fluorescence (Th-T). The protective effects against cytotoxicity induced by Aβ1-42 in PC12 cells were evaluated by MTT assay. Results The data from Th-T fluorescence assay showed that baicalein had a dose-dependent effect on inhibition of Aβ1-42 fibril formation and disaggregation of pre-formed Aβ1-42 fibril. It also reduced the neurotoxicity of Aβ1-42 on the cultured PC12 cells in (P< 0. 01) , as determined by the MTT method. Conclusion These findings provide evidence that baicalein can effectively inhibit Aβ1-42 fibril formation and aggregation and significantly lower the neurotoxicity on PC12 cell line, suggesting that baicalein may be a candidate for prevention or treatment of Alzheimer's disease.%目的 探讨黄芩素对致病性β-淀粉样蛋白(Aβ1-42)纤维形成及细胞毒性作用的影响.方法 采用硫黄素-T(Th-T)荧光分析法观察黄芩素对抗Aβ1-42纤维化效应；应用噻唑蓝(MTT)法,观察黄芩素对抗Aβ1-42对PC12细胞毒性的影响.结果 Th-T荧光分析显示:黄芩素对Aβ1-42纤维形成和聚集有浓度依赖性抑制作用,对预聚集的Aβ1-42纤维也有明显解聚作用(P＜0.01)；MTT法显示:黄芩素能显著降低Aβ1-42对PC12细胞的毒性作用(P＜0.01).结论 黄芩素在体外能有效抑制Aβ1-42纤维形成和聚集,并显著降低Aβ1-42对PC12细胞的毒性作用,提示黄芩素有可能成为防治阿尔茨海默病的药物之一.