Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • News & Views
  • Published:

Proteomimetics

Mimicking the structure and function of tau folds associated with disease

Tauopathies are neurodegenerative diseases characterized by the pathological aggregation of tau, which forms distinct polymorphic structures in a disease-specific manner. A recent study presents macrocyclic tau-mimicking peptides that structurally and functionally resemble these disease-associated folds, providing new tools for studying tau aggregation and potential therapeutic strategies.

This is a preview of subscription content, access via your institution

Access options

Buy this article

Prices may be subject to local taxes which are calculated during checkout

Fig. 1: A structure-guided approach to tau aggregation.

References

  1. Louros, N., Schymkowitz, J. & Rousseau, F. Nat. Rev. Mol. Cell Biol. 24, 912–933 (2023).

    Article  CAS  PubMed  Google Scholar 

  2. Dobson, C. M., Knowles, T. P. J. & Vendruscolo, M. Cold Spring Harb. Perspect. Biol. https://doi.org/10.1101/cshperspect.a033878 (2019).

    Article  Google Scholar 

  3. Chiti, F. & Dobson, C. M. Annu. Rev. Biochem. 86, 27–68 (2017).

    Article  CAS  PubMed  Google Scholar 

  4. Bulawa, C. E. et al. Proc. Natl Acad. Sci. USA 109, 9629–9634 (2012).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  5. Mullard, A. Nat. Rev. Drug Discov. 24, 6 (2025).

    PubMed  Google Scholar 

  6. Golde, T. E. & Levey, A. I. Science 382, 1242–1244 (2023).

    Article  CAS  PubMed  Google Scholar 

  7. Scheres, S. H. W., Ryskeldi-Falcon, B. & Goedert, M. Nature 621, 701–710 (2023).

    Article  CAS  PubMed  Google Scholar 

  8. Lövestam, S. et al. Nature 625, 119–125 (2024).

    Article  PubMed  Google Scholar 

  9. Yang, Y. et al. Science 375, 167–172 (2022).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  10. Shi, Y. et al. Nature 598, 359–363 (2021).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  11. Chakraborty, P. et al. Proc. Natl Acad. Sci. USA 121, e2414176121 (2024).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  12. Angera, I. J. et al. Nat. Chem. https://doi.org/10.1038/s41557-025-01805-z (2025).

    Article  PubMed  Google Scholar 

  13. Louros, N. et al. Nat. Commun. 15, 1028 (2024).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding authors

Correspondence to Joost Schymkowitz or Frederic Rousseau.

Ethics declarations

Competing interests

The authors declare no competing interests.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Schymkowitz, J., Rousseau, F. Mimicking the structure and function of tau folds associated with disease. Nat. Chem. 17, 793–794 (2025). https://doi.org/10.1038/s41557-025-01841-9

Download citation

  • Published:

  • Issue date:

  • DOI: https://doi.org/10.1038/s41557-025-01841-9

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing