Journal
ACS NANO
Volume 12, Issue 6, Pages 5408-5416Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsnano.8b00448
Keywords
self-assembly; amyloid crystals; biomaterials; protein misfolding; atomic force microscopy; circular dichroism; stopped-flow
Categories
Funding
- 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
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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.
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