Amyloid formation in Alzheimer's disease (AD) is driven by hydrophobic interactions and dependent on conformational changes in the amyloid-β (Aβ) molecule. The basic unit for fibrillogenesis appears to be the Aβ conformer adopting an antiparallel β-sheet composed of strands involving the regions 10-24 and 29-40/42 of the peptide. Amyloid formation proceeds by intermolecular interactions between the β-strands of several monomers to form an oligomeric β-sheet structure precursor of the fibrillar β-cross conformation. In this study we designed inhibitors of the fibrillogenesis process based on knowledge of the structural determinants for amyloid formation.
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