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A peptide hairpin inhibitor of amyloid beta-protein oligomerization and fibrillogenesis.

  • Author(s): Yamin, Ghiam
  • Ruchala, Piotr
  • Teplow, David B
  • et al.

Published Web Location

https://doi.org/10.1021/bi901325g
Abstract

Amyloid beta-protein (Abeta) self-assembly is linked strongly to Alzheimer's disease. We found that PP-Leu, a tridecapeptide analogue of broad-spectrum antiviral peptides termed theta-defensins, potently inhibits Abeta oligomer and fibril formation. This effect appeared to be mediated through sequestration of the amyloidogenic Abeta peptide in colloid-like assemblies. PP-Leu comprises a turn formed by a d-Pro-l-Pro amino acid dyad and stabilized by a disulfide bond, a motif that was exceptionally resistant to endoproteinase K digestion. This combination of assembly inhibitory activity and protease resistance suggests that PP-Leu may have potential therapeutic value.

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