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Published on: September 17, 2017

Structures and Dynamics of Tau Assemblies from Solid-State NMR.

Nadia El Mammeri1, Mei Hong1

  • 1Department of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, Massachusetts 02139, United States.

Accounts of Chemical Research
|June 12, 2026
PubMed
Summary
This summary is machine-generated.

Microtubule-associated protein tau aggregation into fibrils is key in neurodegenerative diseases. Solid-state NMR reveals tau structures and dynamics, aiding the development of diagnostics and therapeutics for Alzheimer's disease and related tauopathies.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Structural Biology

Background:

  • Aggregation of microtubule-associated protein tau into β-sheet fibrils is a hallmark of neurodegenerative diseases like Alzheimer's disease (AD).
  • Understanding tau's structure and dynamics in various states (fibrillar, membrane-bound, microtubule-bound) is crucial for elucidating disease mechanisms.

Purpose of the Study:

  • To elucidate the structure and dynamics of different tau assemblies using solid-state NMR spectroscopy.
  • To investigate the role of post-translational modifications (PTMs) and environmental conditions on tau fibril formation and structure.
  • To explore the potential for in vitro reconstruction of AD-tau for therapeutic and diagnostic development.

Main Methods:

  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy was employed to analyze various tau assemblies.
  • In vitro fibrillization experiments were conducted using full-length tau and truncated constructs, with and without heparin.
  • Phospho-mimetic mutations and varying environmental conditions (pH, temperature, ionic strength) were used to study tau structure.

Main Results:

  • Heparin-induced tau fibrils exhibit homogeneous structures dependent on microtubule-binding repeats, differing from ex vivo structures.
  • Phospho-mimetic mutations, particularly at the PHF1 epitope, induce a three-layered rigid core mimicking 4R tau in tauopathies, indicating PTM redundancy.
  • Reproducible in vitro reconstruction of AD-tau fold was achieved, but full-length AD tau lacked seeding potency, suggesting fuzzy coat dynamics are essential for propagation.
  • Cholesterol-rich membranes induce tau fibrils and membrane insertion, supporting a role in nucleation and transmission.
  • The R' segment N-terminal to the PHF1 epitope is the highest-affinity microtubule-binding domain.

Conclusions:

  • Solid-state NMR provides detailed insights into tau structures and dynamics across different assemblies, advancing understanding of tau aggregation mechanisms.
  • The in vitro reconstruction of AD-tau fold offers a platform for developing diagnostics and therapeutics.
  • Fuzzy coat dynamics, not just the rigid core, appear critical for prion-like propagation of tau aggregates.
  • Lipid membranes play a role in tau nucleation and transmission.
  • Targeting the R' segment may offer a strategy to inhibit tau aggregation.