Inhibition of Alzheimer's amyloid-β peptide aggregation and its disruption by a conformationally restricted α/β hybrid peptide

Chem Commun (Camb). 2015 Feb 11;51(12):2245-8. doi: 10.1039/c4cc09063b.

Abstract

Insertion of an anthranilic acid in an amyloidogenic peptide sequence generates a novel conformationally restricted α/β-hybrid peptide that inhibits amyloid formation of Aβ(1-40) and disrupts preformed fibrillar aggregates in vitro. Such β-sheet breaker hybrid peptides (BSBHps) may be useful for designing novel physiologically important compounds relevant to diverse amyloidoses and for studying the process of aggregation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alzheimer Disease / metabolism
  • Alzheimer Disease / pathology
  • Amyloid beta-Peptides / chemical synthesis
  • Amyloid beta-Peptides / chemistry
  • Amyloid beta-Peptides / metabolism*
  • Circular Dichroism
  • Humans
  • Microscopy, Electron, Transmission
  • Peptide Fragments / chemical synthesis
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism*
  • Protein Binding
  • Protein Structure, Secondary
  • ortho-Aminobenzoates / chemistry
  • ortho-Aminobenzoates / metabolism

Substances

  • Amyloid beta-Peptides
  • Peptide Fragments
  • amyloid beta-protein (1-40)
  • ortho-Aminobenzoates
  • anthranilic acid