Ultra rapid in vivo screening for anti-Alzheimer anti-amyloid drugs

被引:42
|
作者
Espargaro, Alba [1 ,2 ]
Medina, Aina [1 ,2 ]
Di Pietro, Ornella [3 ,4 ]
Munoz-Torrero, Diego [3 ,4 ]
Sabate, Raimon [1 ,2 ]
机构
[1] Univ Barcelona, Sch Pharm, Dept Phys Chem, E-08007 Barcelona, Spain
[2] Univ Barcelona, Inst Nanosci & Nanotechnol IN2UB, E-08007 Barcelona, Spain
[3] Univ Barcelona, Sch Pharm, CSIC Associated Unit, Lab Pharmaceut Chem, E-08007 Barcelona, Spain
[4] Univ Barcelona, Inst Biomed IBUB, E-08007 Barcelona, Spain
来源
SCIENTIFIC REPORTS | 2016年 / 6卷
关键词
NUCLEATED POLYMERIZATION; BETA; AGGREGATION; KINETICS; DISEASE; MECHANISM; TOXICITY; PEPTIDE; GROWTH; FIBRILLOGENESIS;
D O I
10.1038/srep23349
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
More than 46 million people worldwide suffer from Alzheimer's disease. A large number of potential treatments have been proposed; among these, the inhibition of the aggregation of amyloid beta-peptide (A beta), considered one of the main culprits in Alzheimer's disease. Limitations in monitoring the aggregation of A beta in cells and tissues restrict the screening of anti-amyloid drugs to in vitro studies in most cases. We have developed a simple but powerful method to track A beta aggregation in vivo in real-time, using bacteria as in vivo amyloid reservoir. We use the specific amyloid dye Thioflavin-S (Th-S) to stain bacterial inclusion bodies (IBs), in this case mainly formed of A beta in amyloid conformation. Th-S binding to amyloids leads to an increment of fluorescence that can be monitored. The quantification of the Th-S fluorescence along the time allows tracking A beta aggregation and the effect of potential anti-aggregating agents.
引用
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页数:8
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