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Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

Author

Listed:
  • Stuart A. Sievers

    (Howard Hughes Medical Institute, UCLA, Box 951970)

  • John Karanicolas

    (University of Washington
    University of Kansas)

  • Howard W. Chang

    (Howard Hughes Medical Institute, UCLA, Box 951970)

  • Anni Zhao

    (Howard Hughes Medical Institute, UCLA, Box 951970)

  • Lin Jiang

    (Howard Hughes Medical Institute, UCLA, Box 951970)

  • Onofrio Zirafi

    (Institute of Molecular Virology, University Hospital Ulm, Meyerhofstrasse 1)

  • Jason T. Stevens

    (University of Kansas)

  • Jan Münch

    (Institute of Molecular Virology, University Hospital Ulm, Meyerhofstrasse 1)

  • David Baker

    (University of Washington)

  • David Eisenberg

    (Howard Hughes Medical Institute, UCLA, Box 951970)

Abstract

Anti-amyloid drug design Amyloid diseases such as Alzheimer's are associated with the transformation of normally soluble proteins into amyloid fibrils — elongated, unbranched protein aggregates. Inhibitors of pathological amyloid fibril formation may be useful as therapeutics if they are sufficiently specific. Sievers et al. use computer-aided, structure-based design, with known atomic structures of segments of amyloid fibres as templates, to evolve a D-amino-acid peptide that delays amyloid fibril formation.

Suggested Citation

  • Stuart A. Sievers & John Karanicolas & Howard W. Chang & Anni Zhao & Lin Jiang & Onofrio Zirafi & Jason T. Stevens & Jan Münch & David Baker & David Eisenberg, 2011. "Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation," Nature, Nature, vol. 475(7354), pages 96-100, July.
    • Handle: RePEc:nat:nature:v:475:y:2011:i:7354:d:10.1038_nature10154
    DOI: 10.1038/nature10154
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    Cited by:

    1. Guizhao Liang & Yonglan Liu & Bozhi Shi & Jun Zhao & Jie Zheng, 2013. "An Index for Characterization of Natural and Non-Natural Amino Acids for Peptidomimetics," PLOS ONE, Public Library of Science, vol. 8(7), pages 1-16, July.
    2. Marc Oeller & Ryan J. D. Kang & Hannah L. Bolt & Ana L. Gomes dos Santos & Annika Langborg Weinmann & Antonios Nikitidis & Pavol Zlatoidsky & Wu Su & Werngard Czechtizky & Leonardo De Maria & Pietro S, 2023. "Sequence-based prediction of the intrinsic solubility of peptides containing non-natural amino acids," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    3. Einav Tayeb-Fligelman & Jeannette T. Bowler & Christen E. Tai & Michael R. Sawaya & Yi Xiao Jiang & Gustavo Garcia & Sarah L. Griner & Xinyi Cheng & Lukasz Salwinski & Liisa Lutter & Paul M. Seidler &, 2023. "Low complexity domains of the nucleocapsid protein of SARS-CoV-2 form amyloid fibrils," Nature Communications, Nature, vol. 14(1), pages 1-18, December.

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