The neuroprotective peptide NAP inhibits the aggregation of the beta-amyloid peptide

  • Peptides. 2003 Sep;24(9):1413-23. doi: 10.1016/j.peptides.2003.08.005.
Osnat Ashur-Fabian  1 ,  Yael Segal-Ruder ,  Ehud Skutelsky ,  Douglas E Brenneman ,  Ruth A Steingart ,  Eliezer Giladi ,  Illana Gozes
Affiliations
  • 1. Department of Clinical Biochemistry, Sackler Faculty of Medicine, Tel-Aviv University, Tel-Aviv 69978, Israel.
PMID: 14706557 DOI: 10.1016/j.peptides.2003.08.005
Abstract

Alzheimer's disease (AD) is characterized by brain plaques containing the beta-amyloid peptide (Abeta). One approach for treating AD is by blocking Abeta aggregation. Activity-dependent neuroprotective protein contains a peptide, NAP that protects neurons in culture against Abeta toxicity. Here, NAP was shown to inhibit Abeta aggregation using: (1) fluorimetry; (2) electron microscopy; (3) high-throughput screening of Abeta deposition onto a synthetic template (synthaloid); and (4) Congo Red staining of neurons. Further assays showed biotin-NAP binding to Abeta. These results suggest that part of the neuroprotective mechanism exerted by NAP is through modulation of toxic protein folding in the extracellular milieu.