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The two major forms of the amyloid-beta (Aβ) peptide found in plaques in patients suffering from Alzheimer's disease, Aβ40 and Aβ42, only differ by two amino acids in the C-terminal region, yet they display markedly different aggregation behavior. The origins of these differences have remained challenging to connect to specific molecular-level processes(More)
Alzheimer's disease is an increasingly prevalent neurodegenerative disorder whose pathogenesis has been associated with aggregation of the amyloid-β peptide (Aβ42). Recent studies have revealed that once Aβ42 fibrils are generated, their surfaces effectively catalyze the formation of neurotoxic oligomers. Here we show that a molecular chaperone, a human(More)
Disease related mutations and environmental factors are key determinants of the aggregation mechanism of the amyloid-β peptide implicated in Alzheimer's disease. Here we present an approach to investigate these factors through acquisition of highly reproducible data and global kinetic analysis to determine the mechanistic influence of intrinsic and(More)
Ziziphus is an important genus within the family Rhamnaceae. This genus includes several important fruit tree species that are widely planted in China and India, such as the Chinese jujube (Ziziphus jujuba Mill.), the wild jujube (Z. acidojujuba), and the Indian jujube (Z. mauritiana). However, information about their domestication based on the chlorotype(More)
Kinetic rate laws Following our previous analysis 19,26 , the generation of fibril mass, M, when both primary and secondary nucleation events occur is described by the integrated rate law: í µí±€(í µí±¡) í µí±€(∞) = 1 − � í µí°µ + + í µí° ¶ + í µí°µ + + í µí° ¶ + í µí±’ í µí¼…í µí¼… í µí°µ − + í µí° ¶ + í µí±’ í µí¼…í µí¼… í µí°µ − + í µí° ¶ + � í µí±˜ ∞ 2(More)
The amyloid β peptide (Aβ42), whose aggregation is associated with Alzheimer's disease, is an amphiphatic peptide with a high propensity to self-assemble. Aβ42 has a net negative charge at physiological pH and modulations of intermolecular electrostatic interactions can significantly alter its aggregation behaviour. Variations in sequence and solution(More)
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