Alzheimer's amyloid fibrils: structure and assembly.
By Louise C. Serpell. Biochimica et Biophysica Acta, 2000
912 citations recorded by the source corpus.
Structural studies of Alzheimer's amyloid fibrils have revealed information about the structure at different levels. The amyloid-beta peptide has been examined in various solvents and conditions and this has led to a model by which a conformational switching occurs from alpha-helix or random coil, to a beta-sheet structure. Amyloid fibril assembly proceeds by a nucleation dependent pathway leading to elongation of the fibrils. Along this pathway small oligomeric intermediates and short fibrillar structures (protofibrils) have been observed. In cross-section the fibril appears to be composed of several subfibrils or protofilaments. Each of these protofilaments is composed of beta-sheet structure in which hydrogen bonding occurs along the length of the fibre and the beta-strands run perpendicular to the fibre axis. This hierarchy of structure is discussed in this review.
Subfields: Biomaterials, Molecular Biology, Physiology
View Paper: https://www.semanticscholar.org/paper/eac270cfbf210b30afa881b5520e7da37a694ce2
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Citations in the corpus
- Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies (2002, neutral): “…confirmed many times (Kuroda and Kawahara, 1994; Howlett et al., 1995; Forloni et al., 1996; Weldon et al., 1998), a fact lending considerable importance to efforts to elucidate the structural and thermodynamic features of the fibril assembly process (for reviews, see Teplow, 1998; Serpell, 2000).”
- Molecular dynamics simulations and novel drug discovery (2018, background): “display similar properties to the full-length protein, such as similar aggregation propensity and neurotoxicity [78].”