期刊
PEERJ
卷 3, 期 -, 页码 -出版社
PEERJ INC
DOI: 10.7717/peerj.1207
关键词
Amyloid; Prion; Protein misfolding; Protein aggregation; Amyloid-like fibrils; Prion strain; Polymorphism; Elongation; Nucleation
资金
- Research Council of Lithuania [MIP-030/2012]
- Marie Curie Career Integration Grant [293476]
Prions are infectious proteins where the same protein may express distinct strains. The strains are enciphered by different misfolded conformations. Strain-like phenomena have also been reported in a number of other amyloid-forming proteins. One of the features of amyloid strains is the ability to self-propagate, maintaining a constant set of physical properties despite being propagated under conditions different from those that allowed initial formation of the strain. Here we report a cross-seeding experiment using strains formed under different conditions. Using high concentrations of seeds results in rapid elongation and new fibrils preserve the properties of the seeding fibrils. At low seed concentrations, secondary nucleation plays the major role and new fibrils gain properties predicted by the environment rather than the structure of the seeds. Our findings could explain conformational switching between amyloid strains observed in a wide variety of in vivo and in vitro experiments.
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