摘要
目的研究异丙酚和咪唑安定对β-淀粉样蛋白1-40(Aβ1-40)的促寡聚化和纤维形成的影响。方法对照组Aβ1-40用PBS配制。P组由预先溶解了3μg/ml异丙酚的PBS配制。M组由预先溶解了100 ng/ml咪唑安定的PBS配制。在30 min、1、2、3、4、5、6、7 d时各组进行荧光分析;对照组在30 min和7 d,其余各组4、7 d时进行透射电镜分析。结果与对照组比较,P组在30 min时荧光强度明显增强(P<0.05);与对照组及P组比较,M组在各时点的荧光强度均明显增强(P<0.05)。P组老化4 d时Aβ1-40以无定形结构存在,老化7 d时仅仅有少量纤维状聚集。M组老化4 d时可见密集的纤维状聚集物,老化7 d时聚集更加明显。结论异丙酚不促进Aβ聚集而咪唑安定对Aβ有促寡聚化和纤维形成的作用。
Objective To investigate the enhancement of amyloid-beta proteinl-40 （Aβ1-40） in oligomerization and fibril formation by propofol and midazolam. Methods Control group： Aβ1-40 incubated in PBS. Group P： Aβ1-40 incubated in PBS with 3 μg/ml propofol. Group M ： Aβ1-40 incubated in PBS with 100 ng/ml midazolam. The concentration of Aβ1-40 fibril was measured by thioflavine fluorimetric analysis at 30 min, 1,2, 3, 4, 5, 6, 7 d in all groups. The structure of Aβ1-40 fibril was observed by transmission electron microscope analysis at 30 min, 7 d in control group and 4 d, 7 d in group P and group M. Results Compared with control group, fluorescence intensity in group P was not remarkably increased at all time points except 30 min （ P 〈 0. 05 ）. Compared with control group and group P, fluorescence intensity was remarkable increased at all time points in group M （P 〈 0. 05 ）. Aβ1-40 at 4 d in group P showed amorphous aggregation, while at 7 d in group P showed a little fibrillar aggregation. A higher density of fibrillar Aβ1-40 aggregation was observed at 4 d in group M and a massive aggregation was observed at 7 d in group M. Conclusion Propofol does not enhance amyloid-beta protein in oligomerization but midazolam enhance amyloid-beta protein in oligomerization and fibril formation.
出处
《山东医药》
CAS
北大核心
2008年第9期30-31,共2页
Shandong Medical Journal
基金
国家自然科学基金资助项目(30571792)
