Rapid Growth of Acetylated Aβ(16-20) into Macroscopic Crystals

ACS Nano
Christian BortoliniMingdong Dong

Abstract

Aberrant assembly of the amyloid-β (Aβ) is responsible for the development of Alzheimer's disease, but can also be exploited to obtain highly functional biomaterials. The short Aβ fragment, KLVFF (Aβ16-20), is crucial for Aβ assembly and considered to be an Aβ 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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Citations

Mar 17, 2020·Journal of Alzheimer's Disease : JAD·Ariel J Kuhn, Jevgenij Raskatov
Dec 12, 2018·ACS Applied Materials & Interfaces·Jie WangMingdong Dong

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