An Additive-Free Model for Tau Self-Assembly

Youssra K. Al-Hilaly, Karen E. Marshall, Liisa Lutter, Luca Biasetti, Kurtis Mengham, Charles R. Harrington, Wei Feng Xue, Claude M. Wischik, Louise C. Serpell

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)


Tau is a natively unfolded protein that contributes to the stability of microtubules. Under pathological conditions such as Alzheimer's disease (AD), tau protein misfolds and self-assembles to form paired helical filaments (PHFs) and straight filaments (SFs). Full-length tau protein assembles poorly and its self-assembly is enhanced with polyanions such as heparin and RNA in vitro, but a role for heparin or other polyanions in vivo remains unclear. Recently, a truncated form of tau (297-391) has been shown to self-assemble in the absence of additives which provides an alternative in vitro PHF model system. Here we describe methods to prepare in vitro PHFs and SFs from tau (297-391) named dGAE. We also discuss the range of biophysical/biochemical techniques used to monitor tau filament assembly and structure.

Original languageEnglish
Pages (from-to)163-188
Number of pages26
JournalMethods in molecular biology (Clifton, N.J.)
Early online date31 Oct 2022
Publication statusPublished - 2023

Bibliographical note

Publisher Copyright:
© 2023. Springer Science+Business Media, LLC, part of Springer Nature.


  • Atomic force microscopy
  • Circular dichroism
  • Cross-beta
  • Electron microscopy
  • Paired helical filament
  • Self-assembly
  • Tau
  • Thioflavin S fluorescence
  • Tyrosine fluorescence
  • X-ray fibre diffraction


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