Synthesis and activity of fibrillogenesis peptide inhibitors related to the 17-21 beta-amyloid sequence

Eur J Med Chem. 2009 Jan;44(1):179-89. doi: 10.1016/j.ejmech.2008.03.036. Epub 2008 Apr 8.

Abstract

Peptide derivatives 1-5, incorporating synthetic non-proteinogenic amino acids, related to the beta-amyloid 17-21 fragment of the amyloidogenic Abeta(1-40), and the N-protected decapeptide 6, corresponding to a dimeric sequence of the same fragment, have been synthesized. These compounds were designed by using Soto's pentapeptide Ac-LPFFD-NH(2) (iAbeta5p) as lead compound. Their activity as inhibitors of fibrillogenesis and stability against enzymatic degradation have been determined. Compounds 1, 5 and 6 are potent inhibitors in comparison to the lead compound. Exposure to chymotrypsin of peptide derivatives 1-5, all containing unnatural amino acids, shows increased stability as compared with iAbeta5p and 6. Conformational properties of the new compounds have been determined by CD and FT-IR spectroscopies.

MeSH terms

  • Amino Acid Sequence
  • Amyloid / antagonists & inhibitors*
  • Amyloid beta-Peptides / antagonists & inhibitors*
  • Drug Design*
  • Drug Stability
  • Humans
  • Molecular Conformation
  • Peptide Fragments / antagonists & inhibitors*
  • Peptide Fragments / chemical synthesis
  • Structure-Activity Relationship

Substances

  • Amyloid
  • Amyloid beta-Peptides
  • Peptide Fragments