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

Stuart A. Sievers, John Karanicolas, Howard W. Chang, Anni Zhao, Lin Jiang, Onofrio Zirafi, Jason T. Stevens, Jan Münch, David Baker and David Eisenberg ()
Additional contact information
Stuart A. Sievers: Howard Hughes Medical Institute, UCLA, Box 951970
John Karanicolas: University of Washington
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

Nature, 2011, vol. 475, issue 7354, 96-100

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.

Date: 2011
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DOI: 10.1038/nature10154

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