期刊
MOLECULAR PHARMACEUTICS
卷 10, 期 3, 页码 1131-1137出版社
AMER CHEMICAL SOC
DOI: 10.1021/mp300636h
关键词
alpha-synuclein; viologen-phosphorus dendrimers; fibrillation; circular dichroism
资金
- COST Action [TD0802]
- CNRS
- MAScIR foundation
Inhibition of alpha-synuclein (ASN) fibril formation is a potential therapeutic strategy in Parkinson's disease and other synucleinopathies. The aim of this study was to examine the role of viologen-phosphorus dendrimers in the alpha-synuclein fibrillation process and to assess the structural changes in alpha-synuclein under the influence of dendrimers. ASN interactions with phosphonate and pegylated surface-reactive viologen-phosphorus dendrimers were examined by measuring the zeta potential, which allowed determining the number of dendrimer molecules that bind to the ASN molecule. The fibrillation kinetics and the structural changes were examined using ThT fluorescence and CD spectroscopy. Depending on the concentration of the used dendrimer and the nature of the reactive groups located on the surface, ASN fibrillation kinetics can be significantly reduced, and even, in the specific case of phosphonate dendrimers, the fibrillation can be totally inhibited at low concentrations. The presented results indicate that viologen-phosphorus dendrimers are able to inhibit ASN fibril formation and may be used as fibrillar regulating agents in neurodegenerative disorders.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据