| abstract |
Anti-AβP scFvs and single domain antibodies were generated, and when these antibodies were displayed on filamentous phage or as soluble protein molecules, stabilized by the maltose binding protein, they could prevent the fibrilization of Abp 1-40 and disaggregate Abp 1-40 fibrils generated in vitro. The anti-Aβp scFv antibodies also stained amyloid neuritic plaques on slices from transgenic mice. The anti-ABP scFv and single domain antibodies can be used for inhibiting or treating Alzheimer's disease. |