Send to

Choose Destination
See comment in PubMed Commons below
Proc Natl Acad Sci U S A. 1997 Apr 15;94(8):4109-12.

Disaggregation of Alzheimer beta-amyloid by site-directed mAb.

Author information

  • 1Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Ramat Aviv, Israel.


In Alzheimer disease, beta-amyloid peptide accumulates in the brain as insoluble amyloid plaques. Amyloid filaments, similar to those found in amyloid plaques, can be assembled in vitro from chemically synthesized beta-peptides. In this study, we report that antibodies raised against the N-terminal region (1-28) of the beta-amyloid peptide bind to the in vitro-formed beta-amyloid assemblies, leading to disaggregation of the fibrils and partial restoration of the peptide's solubility. The concomitant addition of fibrillar beta-amyloid with these antibodies to PC 12 cells leads to the inhibition of the neurotoxic effects of beta-amyloid. Some of the mAbs raised against soluble beta-peptide (1-28) have been found to prevent in vitro fibrillar aggregation of beta-amyloid peptide. These experimental data suggest that site-directed mAbs interfere with the aggregation of beta-amyloid and trigger reversal to its nontoxic, normal components. The above findings give hints on how to convert in vivo senile plaques into nontoxic, diffuse components and may have therapeutic interest for those studying Alzheimer disease and other human diseases related to amyloidogenic properties of physiological peptides and proteins.

[PubMed - indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Support Center