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

Osnat Ashur-Fabian, Yael Segal-Ruder, Ehud Skutelsky, Douglas E. Brenneman, Ruth A. Steingart, Eliezer Giladi, Illana Gozes*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

82 Scopus citations


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

Original languageEnglish
Pages (from-to)1413-1423
Number of pages11
Issue number9
StatePublished - Sep 2003


FundersFunder number
Allon Therapeutics, Inc.
Institute for the Study of Aging
US–Israel Binational Science Foundation
Israel Science Foundation


    • Activity-dependent neuroprotective protein
    • Alzheimer's disease
    • Aβ aggregation
    • Brain-cortical cultures
    • NAP
    • Vasoactive intestinal peptide


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