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• W321130179 endingPage "215" @default.
• W321130179 startingPage "197" @default.
• W321130179 abstract "Alzheimer's disease (AD) is a devastating neurodegenerative disease with pathological misfolding of amyloid-β protein (Aβ). The recent interest in Aβ misfolding intermediates necessitates development of novel detection methods and ability to trap these intermediates. We speculated that two regions of Aβ may allow for detection of specific Aβ species: the N-terminal and 22-35, both likely important in oligomer interaction and formation. We determined via epitomics, proteomic assays, and electron microscopy that the Aβ(42) species (wild type, ΔE22, and MetOx) predominantly formed fibrils, oligomers, or dimers, respectively. The 2H4 antibody to the N-terminal of Aβ, in the presence of 2% SDS, primarily detected fibrils, and an antibody to the 22-35 region detected low molecular weight Aβ species. Simulated molecular modeling provided insight into these SDS-induced structural changes. We next determined if these methods could be used to screen anti-Aβ drugs as well as identify compounds that trap Aβ in various conformations. Immunoblot assays determined that taurine, homotaurine (Tramiprosate), myoinositol, methylene blue, and curcumin did not prevent Aβ aggregation. However, calmidazolium chloride trapped Aβ at oligomers, and berberine reduced oligomer formation. Finally, pretreatment of AD brain tissues with SDS enhanced 2H4 antibody immunostaining of fibrillar Aβ. Thus we identified and characterized Aβs that adopt specific predominant conformations (modified Aβ or via interactions with compounds), developed a novel assay for aggregated Aβ, and applied it to drug screening and immunohistochemistry. In summary, our novel approach facilitates drug screening, increases the probability of success of antibody therapeutics, and improves antibody-based detection and identification of different conformations of Aβ." @default.
• W321130179 created "2016-06-24" @default.
• W321130179 creator A5002533845 @default.
• W321130179 creator A5006193152 @default.
• W321130179 creator A5027818184 @default.
• W321130179 creator A5038472272 @default.
• W321130179 creator A5039438549 @default.
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• W321130179 creator A5058843845 @default.
• W321130179 creator A5065800928 @default.
• W321130179 creator A5071772212 @default.
• W321130179 date "2012-09-25" @default.
• W321130179 modified "2023-10-10" @default.
• W321130179 title "Probing and Trapping a Sensitive Conformation: Amyloid-β Fibrils, Oligomers, and Dimers" @default.
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