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

• Published in: Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2003-09, Vol.24 (9), p.1413-1423
• Main Authors: Ashur-Fabian, Osnat, Segal-Ruder, Yael, Skutelsky, Ehud, Brenneman, Douglas E., Steingart, Ruth A., Giladi, Eliezer, Gozes, Illana
• Format: Article
• Language: English
• Subjects: Activity-dependent neuroprotective protein; Alzheimer Disease; Alzheimer’s disease; Amyloid beta-Peptides - antagonists & inhibitors; Amyloid beta-Peptides - chemistry; Amyloid beta-Peptides - metabolism; Amyloid beta-Peptides - ultrastructure; Animals; Animals, Newborn; Aβ aggregation; Biological and medical sciences; Brain-cortical cultures; Cell Aggregation; Cells, Cultured; Congo Red - analysis; Copper - metabolism; Fundamental and applied biological sciences. Psychology; Microscopy, Electron; NAP; Neurons - cytology; Neurons - metabolism; Oligopeptides - metabolism; Oligopeptides - pharmacology; Peptide Fragments - antagonists & inhibitors; Peptide Fragments - chemistry; Peptide Fragments - metabolism; Peptide Fragments - ultrastructure; Protein Binding - drug effects; Protein Structure, Quaternary - drug effects; Rats; Vasoactive intestinal peptide; Vertebrates: endocrinology
• ISSN: 0196-9781; 1873-5169
• DOI: 10.1016/j.peptides.2003.08.005

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.