期刊
SMALL
卷 9, 期 20, 页码 3455-3461出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/smll.201202612
关键词
self-assembly; nanoparticles; peptide inhibitors; amyloids; polyoxometalates; alzheimer's disease
类别
资金
- 973 Project [2011CB936004, 2012CB720602]
- NSFC [21210002, 91213302]
Amyloid fibril formation is a critical step in Alzheimer's disease (AD) pathogenesis. Inhibition of A aggregation has shown promising against AD and has been used in clinic trials. Here, a novel strategy is reported for the self-assembly of polyoxometalate-peptide (POM@P) hybrid particles as bifunctional A inhibitors. The two-in-one bifunctional POM@P nanoparticles show an enhanced inhibition effect on amyloid aggregation in mice cerebrospinal fluid. Incorporating a clinically used A fibril-staining dye, congo red (CR), into the hybrid colloidal spheres, the nanoparticles can also act as an effective fluorescent probe to monitor the inhibition process of POM@P via CR fluorescence change in real time. It is believed that such flexible organic-inorganic hybrid systems may prompt the design of new multifunctional materials for AD treatment.
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