51. Identification of amyloid-beta binding sites using an antisense peptide approach.
- Author
-
Milton NG, Mayor NP, and Rawlinson J
- Subjects
- Amino Acid Sequence, Amyloid beta-Peptides genetics, Antisense Elements (Genetics), Binding Sites physiology, Humans, Peptide Fragments genetics, 3-Hydroxyacyl CoA Dehydrogenases, Amyloid beta-Peptides chemistry, Amyloid beta-Peptides metabolism, Carrier Proteins metabolism, Catalase metabolism, Peptide Fragments chemistry, Peptide Fragments metabolism
- Abstract
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.
- Published
- 2001
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