期刊
ACS NANO
卷 12, 期 6, 页码 5408-5416出版社
AMER CHEMICAL SOC
DOI: 10.1021/acsnano.8b00448
关键词
self-assembly; amyloid crystals; biomaterials; protein misfolding; atomic force microscopy; circular dichroism; stopped-flow
类别
资金
- Leverhulme Trust Research Leadership Award
- European Research Council under the European Union's Seventh Framework Programme (FP7/2007-2013) through the ERC grant PhysProt [337969]
- EU [MNR4SCell 734174]
- Biotechnology and Biological Sciences Research Council [BB/J002119/1] Funding Source: researchfish
- Lundbeck Foundation [R192-2015-1128] Funding Source: researchfish
- BBSRC [BB/J002119/1] Funding Source: UKRI
Aberrant assembly of the amyloid-beta (A beta) is responsible for the development of Alzheimer's disease, but can also be exploited to obtain highly functional biomaterials. The short A beta fragment, KLVFF (A beta(16-20)), is crucial for A beta assembly and considered to be an A beta aggregation inhibitor. Here, we show that acetylation of KLVFF turns it into an extremely fast self assembling molecule, reaching macroscopic (i.e., mm) size in seconds. We show that KLVFF is metastable and that the self-assembly can be directed toward a crystalline or fibrillar phase simply through chemical modification, via acetylation or amidation of the peptide. Amidated KLVFF can form amyloid fibrils; we observed folding events of such fibrils occurring in as little as 60 ms. The ability of single KLVFF molecules to rapidly assemble as highly ordered macroscopic structures makes it a promising candidate for applications as a rapid-forming templating material.
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