Review Article | Published:

The activities of amyloids from a structural perspective

Nature volume 539, pages 227235 (10 November 2016) | Download Citation

Abstract

The aggregation of proteins into structures known as amyloids is observed in many neurodegenerative diseases, including Alzheimer's disease. Amyloids are composed of pairs of tightly interacting, many stranded and repetitive intermolecular β-sheets, which form the cross-β-sheet structure. This structure enables amyloids to grow by recruitment of the same protein and its repetition can transform a weak biological activity into a potent one through cooperativity and avidity. Amyloids therefore have the potential to self-replicate and can adapt to the environment, yielding cell-to-cell transmissibility, prion infectivity and toxicity.

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Acknowledgements

We thank K. Comiotto and M. Sawaya for making figures and the Swiss National Science Foundation (SNSF), the US National Institutes of Health and the Howard Hughes Medical Institute for continuing support of our research, including an SNSF Sinergia grant to R.R.

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Affiliations

  1. Laboratory of Physical Chemistry, Department of Chemistry and Applied Biosciences, ETH Zurich, 8093 Zürich, Switzerland.

    • Roland Riek
  2. UCLA-DOE Institute, Los Angeles, California 90095-1570, USA.

    • David S. Eisenberg
  3. Howard Hughes Medical Institute, Los Angeles, California 90095-1570, USA.

    • David S. Eisenberg

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Correspondence to Roland Riek or David S. Eisenberg.

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