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Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide

Nature Structural Biology volume 2, pages 990–998 (1995)Cite this article

Abstract

Amyloids are a class of noncrystalline, yet ordered, protein aggregates. A new approach was used to provide the initial structural data on an amyloid fibril—comprising a peptide (β34–42) from the C-terminus of the β-amyloid protein—based on measurement of intramolecular 13C–13C distances and 13C chemical shifts by solid-state 13C NMR and individual amide absorption frequencies by isotope-edited infrared spectroscopy. Intermolecular orientation and alignment within the amyloid sheet was determined by fitting models to observed intermolecular 13C–13C couplings. Although the structural model we present is defined to relatively low resolution, it nevertheless shows a pleated antiparallel β-sheet characterized by a specific intermolecular alignment.

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Author information

Author notes

  1. Janet M. Griffiths

    Present address: Department of Chemical Engineering, Massachusetts Institute of Technology, Harvard University, Cambridge, Massachusetts, USA

  2. Eric J. Simon

    Present address: Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts, USA

  3. Michèle Auger

    Present address: Laval University, Quebec City, Quebec, Canada

  4. Kurt J. Halverson

    Present address: 3M Corp., St. Paul, Minnesota, USA

  5. Richard G.S. Spencer

    Present address: National Institute on Aging, Baltimore, Maryland, USA

Authors and Affiliations

  1. Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, USA

    Peter T. Lansbury Jr., Philip R. Costa, Janet M. Griffiths, Michèle Auger, Kurt J. Halverson, David A. Kocisko, Zachary S. Hendsch, Ted T. Ashburn, Richard G.S. Spencer, Bruce Tidor & Robert G. Griffin

  2. Francis Bitter National Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, USA

    Philip R. Costa, Janet M. Griffiths, Michèle Auger, Richard G.S. Spencer & Robert G. Griffin

  3. Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, USA

    Eric J. Simon, Zachary S. Hendsch & Bruce Tidor

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Lansbury, P., Costa, P., Griffiths, J. et al. Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide. Nat Struct Mol Biol 2, 990–998 (1995). https://doi.org/10.1038/nsb1195-990

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