Alzheimer's disease (AD) is a neurological disease that is slated to cost well over one trillion dollars in the next decade. Many strategies have been investigated to prevent AD, however; there is currently no cure for the disease. Of these strategies, amyloid beta (A�) inhibitors have been well studied, including the peptide KLVFF. Peptide KLVFF is the key essential binding region that can be used to allow inhibitors to bind to the residues 16-20 of A�. In this study, we have designed a series of peptoids that mimic the peptide KLVFF that are capable of binding to A�1-40. Our peptoid inhibitor JPT1 has shown to prevent A� aggregation up to ~84% in a 5:1 molar excess ratio (Peptoid Inhibitor to A�1-40), while rapidly accelerating through the toxic oligomeric stages. Furthermore, we believe we can modify our peptoid inhibitors to completely inhibit A� aggregation which in turn will lead to a peptoid sequence that holds promise as a therapeutic agent.

Peptoids that mimic the peptide KLVFF prevent aggregation of A�<sub>1-40</sub>

247th National Meeting (2014)

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Peptoids that mimic the peptide KLVFF prevent aggregation of A�1-40

Peptoids that mimic the peptide KLVFF prevent aggregation of A�_1-40