Rapid growth of acetylated Aβ(16-20) into macroscopic crystals

Christian Bortolini, Lasse Hyldgaard Klausen, Søren Vrønning Hoffmann, Nykola C. Jones, Daniela Saadeh, Zegao Wang, Tuomas P.J. Knowles, Mingdong Dong*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)5408-5416
Number of pages9
JournalACS Nano
Issue number6
Early online date17 May 2018
Publication statusPublished - 26 Jun 2018


  • amyloid crystals
  • atomic force microscopy
  • biomaterials
  • circular dichroism
  • protein misfolding
  • self-assembly
  • stopped-flow


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