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Accumulation of cytotoxic oligomers of amyloid ß (Aß) is one of the major pathological hallmarks of Alzheimer's disease (AD). Several immunological approaches that prevent the conversion of Aß into its toxic form or that accelerate its clearance are being actively pursued worldwide. As part of these attempts, we have carried out sequential epitope analysis of Aß where antibodies raised against native Aß and its homologue Aß-KEK were screened for binding to five overlapping hexadecapeptides encompassing the full length of Aß sequence with 10 amino acid overlap. By this approach, we could identify a neutralizing epitope spanning the region 13-28 in Aß. These results demonstrate the presence of an additional stretch of Aß that can serve as mini-vaccine for AD.

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