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

doi:10.1016/j.peptides.2003.08.005

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 journal › Article › peer-review

82 Scopus citations

Abstract

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 language	English
Pages (from-to)	1413-1423
Number of pages	11
Journal	Peptides
Volume	24
Issue number	9
DOIs	https://doi.org/10.1016/j.peptides.2003.08.005
State	Published - Sep 2003

Keywords

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

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.peptides.2003.08.005

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title = "The neuroprotective peptide NAP inhibits the aggregation of the beta-amyloid peptide",

abstract = "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.",

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author = "Osnat Ashur-Fabian and Yael Segal-Ruder and Ehud Skutelsky and Brenneman, {Douglas E.} and Steingart, {Ruth A.} and Eliezer Giladi and Illana Gozes",

note = "Funding Information: We thank Drs. Mati Fridkin and Avron D. Spier and Mrs. Sara Rubinraut for their invaluable input. We thank Dr. Malcolm Scott for his kind gift of the Synthaloid plates and Dr. Virginia Smith-Swintosky for the scrambled NAP sequence. Supported in part by the Institute for the Study of Aging (ISOA), Allon Therapeutics, Inc., the US–Israel Binational Science Foundation, the Israel Science Foundation and the Lily and Avraham Gildor Chair for the Investigation of Growth Factors.",

year = "2003",

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AU - Steingart, Ruth A.

AU - Giladi, Eliezer

AU - Gozes, Illana

N1 - Funding Information: We thank Drs. Mati Fridkin and Avron D. Spier and Mrs. Sara Rubinraut for their invaluable input. We thank Dr. Malcolm Scott for his kind gift of the Synthaloid plates and Dr. Virginia Smith-Swintosky for the scrambled NAP sequence. Supported in part by the Institute for the Study of Aging (ISOA), Allon Therapeutics, Inc., the US–Israel Binational Science Foundation, the Israel Science Foundation and the Lily and Avraham Gildor Chair for the Investigation of Growth Factors.

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N2 - 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.

AB - 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.

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

Abstract

Keywords

UN SDGs

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