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An Additive-Free Model for Tau Self-Assembly.

Methods in molecular biology (Clifton, N.J.) (2022-11-01)
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
ABSTRACT

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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-TAU antibody produced in rabbit, affinity isolated antibody
Sigma-Aldrich
Anti-Tau (T22), oligomeric Antibody, serum, from rabbit