Identification of amyloid-beta binding sites using an antisense peptide approach

Neuroreport. 2001 Aug 8;12(11):2561-6. doi: 10.1097/00001756-200108080-00054.


The amyloid-beta (A beta) peptide is a cytotoxic peptide implicated in the pathology of Alzheimer's disease (AD). Catalase and the endoplasmic reticulum A beta binding dehydrogenase (ERAB) are both inhibited by characterized fragments of the A beta peptide. In order to target such proteins it is essential to determine which components of these enzymes interact with A beta. This study reports the use of antisense peptide methodology to identify specific A beta-binding domains. Synthetic peptides corresponding to the regions of catalase and ERAB identified showed specific binding to A beta and also prevented A beta cytotoxicity. Antisense peptide methodology has identified A beta recognition sequences and may also be applied to the identification of novel A beta protein interactions to identify targets for use in the treatment of AD.

MeSH terms

  • 3-Hydroxyacyl CoA Dehydrogenases*
  • Amino Acid Sequence
  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / genetics
  • Amyloid beta-Peptides / metabolism*
  • Antisense Elements (Genetics)
  • Binding Sites / physiology
  • Carrier Proteins / metabolism*
  • Catalase / metabolism*
  • Humans
  • Peptide Fragments / chemistry*
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism*


  • Amyloid beta-Peptides
  • Antisense Elements (Genetics)
  • Carrier Proteins
  • Peptide Fragments
  • amyloid beta-protein (1-43)
  • 3-Hydroxyacyl CoA Dehydrogenases
  • HSD17B10 protein, human
  • Hsd17b10 protein, mouse
  • Catalase