Abstract
The neurotoxic peptide A beta(42) is derived from the amyloid precursor protein by proteolytic cleavage and is deposited in the brain of patients suffering from Alzheimer's disease (AD). In this study we generate a high affinity monoclonal antibody that targets the C-terminal end of A beta(42) with high specificity. By this is meant that the paratope of the antibody must enclose the C-terminal end of A beta(42) including the carboxy-group of amino acid 42, and not just recognize a linear epitope in the C-terminal part of A beta. This has been accomplished by using a unique antigen construct made by the Ligand Presenting Assembly technology (LPA technology). This strategy results in dimeric presentation of the free C-terminal end of A beta(42). The generated Mab A beta1.1 is indeed specific for the C-terminal end of A beta(42) to which it binds with high affinity. Mab A beta1.1 recognizes the epitope in human AD tissue and stains plaques with high specificity. Therefore the monoclonal antibody can thus be useful in the histological investigations of the AD pathology.
| Original language | English |
|---|---|
| Journal | Molecular Immunology |
| Volume | 46 |
| Issue number | 11-12 |
| Pages (from-to) | 2267-73 |
| Number of pages | 7 |
| DOIs | |
| Publication status | Published - Jul 2009 |
Keywords
- Alzheimer Disease
- Amyloid beta-Peptides
- Antibodies, Monoclonal
- Antibody Affinity
- Brain
- Humans
- Immunohistochemistry
- Peptide Fragments
- Protein Multimerization
- Journal Article
