title: X-ray crystallographic structures of trimers and higher-order oligomeric assemblies of a peptide derived from Aβ(17-36).
abstract: A peptide derived from Aβ17-36 crystallizes to form trimers that further associate to form higher-order oligomers. The trimers consist of three highly twisted β-hairpins in a triangular arrangement. Two trimers associate face-to-face in the crystal lattice to form a hexamer; four trimers in a tetrahedral arrangement about a central cavity form a dodecamer. These structures provide a working model for the structures of oligomers associated with neurodegeneration in Alzheimer's disease.
authors.affiliation: Department of Chemistry, University of California, Irvine , Irvine, California 92697-2025, United States.
authors.forename: Ryan K
authors.initials: RK
authors.lastname: Spencer
authors.forename: Hao
authors.initials: H
authors.lastname: Li
authors.forename: James S
authors.initials: JS
authors.lastname: Nowick
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry*; D001704:Biopolymers / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D016229:Amyloid beta-Peptides; D001704:Biopolymers; D010455:Peptides