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A small-molecule lead compound for the treatment of Alzheimer’s disease

At autopsy, Alzheimer’s disease is characterised by the presence of amyloid plaques and neurofibrillary tangles, made up of two peptide sequences, amylo-id-β1-40 (Aβ40) and amyloid-β1-42 (Aβ42). In Tyrode’s solution (2 mM Ca2+), 10μM Aβ42 peptide almost immediately aggregates and eventually forms β-sheets. This aggregation can be inhibited with 4,5-dianilinophthalimide (DAPH). Ca2+-permeant AMPA receptors are involved in the neuronal Ca2+ influx (neurotoxicity) induced by the Aβ42 peptide in cultured neuronal cells. The Ca2+ influx observed with pre-incubated Aβ42 peptide was inhibited by DAPH. DAPH also inhibits epidermal growth factor receptor kinase, and this will prevent its development for use in Alzheimer’s disease. The potential of DAPH as a small-molecule lead compound for the treatment of Alzheimer’s disease next requires the separation of the structural requirements that reverse fibril formation and inhibit epidermal growth factor receptor kinase.