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

被引：81

作者：

Ashur-Fabian, O

Segal-Ruder, Y

Skutelsky, E

Brenneman, DE

Steingart, RA

Giladi, E

Gozes, I ^{[1
]}

机构：

[1] Tel Aviv Univ, Sackler Fac Med, Dept Clin Biochem, IL-69978 Tel Aviv, Israel

[2] Tel Aviv Univ, Sackler Fac Med, Dept Pathol, IL-69978 Tel Aviv, Israel

[3] NICHD, LDN, SDMP, NIH, Bethesda, MD 20892 USA

来源：

PEPTIDES | 2003年 / 24卷 / 09期

关键词：

A beta aggregation; activity-dependent neuroprotective protein; Alzheimer's disease; brain-cortical cultures; vasoactive intestinal peptide; NAP;

D O I：

10.1016/j.peptides.2003.08.005

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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-dependant 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. (C) 2003 Elsevier Inc. All rights reserved.

引用

页码：1413 / 1423

页数：11

共 59 条

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