Structures for amyloid fibrils

FEBS J. 2005 Dec;272(23):5950-61. doi: 10.1111/j.1742-4658.2005.05025.x.


Alzheimer's disease and Creutzfeldt-Jakob disease are the best-known examples of a group of diseases known as the amyloidoses. They are characterized by the extracellular deposition of toxic, insoluble amyloid fibrils. Knowledge of the structure of these fibrils is essential for understanding the process of pathology of the amyloidoses and for the rational design of drugs to inhibit or reverse amyloid formation. Structural models have been built using information from a wide variety of techniques, including X-ray diffraction, electron microscopy, solid state NMR and EPR. Recent advances have been made in understanding the architecture of the amyloid fibril. Here, we describe and compare postulated structural models for the mature amyloid fibril and discuss how the ordered structure of amyloid contributes to its stability.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Alzheimer Disease / metabolism
  • Amyloid / chemistry*
  • Amyloid / ultrastructure*
  • Amyloidosis / metabolism
  • Creutzfeldt-Jakob Syndrome / metabolism
  • Humans
  • Models, Molecular
  • Molecular Structure
  • Protein Conformation*
  • X-Ray Diffraction


  • Amyloid