Interactions among amyloidogenic peptides and proteins are central to the pathology of Alzheimer's and other amyloid diseases. Aggregation of the �-amyloid peptide (A�) in Alzheimer's disease to form fibrils occurs through interactions between different regions of A�. Molecular recognition between these regions of A� may also be involved in the formation of toxic oligomers that damage or kill neurons. This presentation describes the use of chemical model systems to study molecular recognition through hydrogen bonding and hydrophobic interactions between two regions of A�. The model systems are macrocyclic �-sheets containing the tripeptide �-strand mimic Hao, the �-turn mimic d-linked ornithine (dOrn), and heptapeptides from A�. Nuclear magnetic resonance studies show systems containing the �-amyloid peptides A�17-23 and A�30-36 preferentially form mixed oligomers in aqueous solution. 

Molecular recognition between chemical models of �-amyloid peptides

246th National Meeting (2013)

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