title: Structural differences between amyloid beta oligomers.
abstract: In Alzheimer's disease, soluble Aβ oligomers are believed to play important roles in the disease pathogenesis, and their levels correlate with cognitive impairment. We have previously shown that Aβ oligomers can be categorized into multiple structural classes based on their reactivity with conformation-dependent antibodies. In this study, we analyzed the structures of Aβ40 oligomers belonging to two of these classes: fibrillar and prefibrillar oligomers. We found that fibrillar oligomers were similar in structure to fibrils but were less stable towards denaturation while prefibrillar oligomers were found to be partially disordered. These results are consistent with previously proposed structures for both oligomer classes while providing additional structural information.
authors.affiliation: Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, United States; Department of Molecular Medicine and Byrd Alzheimer's Institute, University of South Florida, Tampa, FL 33612, United States. Electronic address: lbreydo@health.usf.edu.
authors.forename: Leonid
authors.initials: L
authors.lastname: Breydo
authors.affiliation: Department of Chemistry, University at Albany, SUNY, 1400 Washington Avenue, Albany, NY 12222, United States.
authors.forename: Dmitry
authors.initials: D
authors.lastname: Kurouski
authors.affiliation: Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, United States.
authors.forename: Suhail
authors.initials: S
authors.lastname: Rasool
authors.affiliation: Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, United States.
authors.forename: Saskia
authors.initials: S
authors.lastname: Milton
authors.affiliation: Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, United States.
authors.forename: Jessica W
authors.initials: JW
authors.lastname: Wu
authors.affiliation: Department of Molecular Medicine and Byrd Alzheimer's Institute, University of South Florida, Tampa, FL 33612, United States; Department of Biological Sciences, Faculty of Sciences, King Abdulaziz University, Jeddah, Saudi Arabia.
authors.forename: Vladimir N
authors.initials: VN
authors.lastname: Uversky
authors.affiliation: Department of Chemistry, University at Albany, SUNY, 1400 Washington Avenue, Albany, NY 12222, United States.
authors.forename: Igor K
authors.initials: IK
authors.lastname: Lednev
authors.affiliation: Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, United States; Biochemistry Department, Faculty of Science and Experimental Biochemistry Unit, King Fahd Medical Research Center, King Abdulaziz University, Jeddah, Saudi Arabia.
authors.forename: Charles G
authors.initials: CG
authors.lastname: Glabe
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000648:ultrastructure*; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000648:ultrastructure*; D019281:Dimerization; D010446:Peptide Fragments / Q000737:chemistry* / Q000648:ultrastructure*; D011487:Protein Conformation
chemical_list: D000682:Amyloid; D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40)
keywords: Alzheimer’s disease; Amyloid beta; Oligomers; Protein aggregation