Identification of the shortest Aβ-peptide generating highly specific antibodies against the C-terminal end of amyloid-β42.

Alzheimer's disease (AD) is characterized by neurofibrillary tangles, consisting of hyperphosphorylated tau protein and senile plaques, which are consisting mainly of amyloid-β (Aβ). Attempts to generate a safe vaccine against Aβ rely on both B- and T-cell epitopes within the neurotoxic peptide Aβ1-42. This, however, poses a risk for an inflammatory and/or autoimmune response against Aβ-peptides in the brain.

Specific recognition of the C-terminal end of A beta 42 by a high affinity monoclonal antibody.

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.