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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:
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.
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页数:8
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