title: Context dependence of protein misfolding and structural strains in neurodegenerative diseases.
abstract: Vast arrays of structural forms are accessible to simple amyloid peptides and environmental conditions can direct assembly into single phases. These insights are now being applied to the aggregation of the Aβ peptide of Alzheimer's disease and the identification of causative phases. We extend use of the imaging agent Pittsburgh compound B to discriminate among Aβ phases and begin to define conditions of relevance to the disease state. Also, we specifically highlight the development of methods for defining the structures of these more complex phases.
authors.affiliation: Department of Chemistry, Alzheimer's Disease Research Center, Emory University, Atlanta, GA, 30322; Department of Biology, Alzheimer's Disease Research Center, Emory University, Atlanta, GA, 30322.
authors.forename: Anil K
authors.initials: AK
authors.lastname: Mehta
authors.forename: Rebecca F
authors.initials: RF
authors.lastname: Rosen
authors.forename: W Seth
authors.initials: WS
authors.lastname: Childers
authors.forename: John D
authors.initials: JD
authors.lastname: Gehman
authors.forename: Lary C
authors.initials: LC
authors.lastname: Walker
authors.forename: David G
authors.initials: DG
authors.lastname: Lynn
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism; D000682:Amyloid; D016229:Amyloid beta-Peptides / Q000378:metabolism; D006801:Humans; D019636:Neurodegenerative Diseases; D010446:Peptide Fragments / Q000378:metabolism
chemical_list: D000682:Amyloid; D016229:Amyloid beta-Peptides; D010446:Peptide Fragments
keywords: NMR spectrsocopy; PIB; amyloid; amyloid strains; nanotubes
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