Inhibitors of fibril formation and cytotoxicity of β-amyloid peptide composed of KLVFF recognition element and flexible hydrophilic disrupting element

被引：62
作者：
Watanabe, K
Nakamura, K
Akikusa, S
Okada, T
Kodaka, M
Konakahara, T
Okuno, H
机构：
[1] Natl Inst Adv Ind Sci & Technol, Tsukuba, Ibaraki 3058566, Japan
[2] Tokyo Univ Sci, Fac Sci & Technol, Noda, Chiba 2788510, Japan
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2002年 / 290卷 / 01期
关键词：
D O I：
10.1006/bbrc.2001.6191
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：
beta-Amyloid peptide (Abeta) is the main protein components of neuritic plaques and its neurotoxicity would be exposed by formation of aggregate. The aggregation inhibitors composed of an Abeta recognition element (KLVFF) and a flexible hydrophilic disrupting element (aminoethoxy ethoxy acetate and aspartate) are designed and chemically synthesized. The inhibitory effects are examined by a pigment binding assay using Congo red or thioflavin T. The present compounds suppress the formation of aggregate, and the compound DDX3 is an especially effective inhibitor. In addition, the synthesized compounds efficiently suppress the cytotoxicity of Abeta against IMR-32 neuroblastoma cells in vitro. (C) 2002 Elsevier Science.
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收藏
页码：121 / 124
页数：4
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