The amyloids from A�, islet amyloid polypeptide, and the human prion protein contain long �-strands, comprising nine or more amino acids, that self-assemble through intermolecular hydrogen bonding to form extended networks of �-sheets. Here, we describe a new class of �-sheet macrocycles that present a nonapeptide �-strand and self-assemble to form stable, well-defined water-soluble oligomers. These macrocycles hold the promise of inhibiting amyloid aggregation and providing insight into amyloid structure and formation.

β-Sheet macrocycles containing a nonapeptide β-strand

243rd National Meeting (2012)

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