Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy

Angew Chem Int Ed Engl. 2009;48(12):2118-21. doi: 10.1002/anie.200804198.


The fibril structure formed by the amyloidogenic fragment SNNFGAILSS of the human islet amyloid polypeptide (hIAPP) is determined with 0.52 A resolution. Symmetry information contained in the easily obtainable resonance assignments from solid-state NMR spectra (see picture), along with long-range constraints, can be applied to uniquely identify the supramolecular organization of fibrils.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid / chemistry
  • Amyloid / ultrastructure*
  • Humans
  • Islet Amyloid Polypeptide
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Protein Structure, Tertiary


  • Amyloid
  • Islet Amyloid Polypeptide