title: Structures for amyloid fibrils.
abstract: 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.
authors.affiliation: Department of Biochemistry, John Maynard Smith Building, School of Life Sciences, University of Sussex, Falmer, East Sussex, UK.
authors.forename: O Sumner
authors.initials: OS
authors.lastname: Makin
authors.forename: Louise C
authors.initials: LC
authors.lastname: Serpell
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism; D000682:Amyloid / Q000737:chemistry* / Q000648:ultrastructure*; D000686:Amyloidosis / Q000378:metabolism; D007562:Creutzfeldt-Jakob Syndrome / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D015394:Molecular Structure; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D000682:Amyloid