Practical assay and molecular mechanism of aggregation inhibitors of β-amyloid

被引：16

作者：

Akikusa, S

Nakamura, K

Watanabe, KI

Horikawa, E

Konakahara, T

Kodaka, M

Okuno, H

机构：

[1] AIST, Natl Inst Adv Ind Sci & Technol, Tsukuba, Ibaraki 3058566, Japan

[2] Tokyo Univ Sci, Fac Sci & Technol, Chiba, Japan

来源：

JOURNAL OF PEPTIDE RESEARCH | 2003年 / 61卷 / 01期

关键词：

aggregation inhibitor; Alzheimer's disease; beta-amyloid; fluorescence assay; molecular interaction; Multipin (TM);

D O I：

10.1034/j.1399-3011.2003.21028.x

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

beta-Amyloid peptide (Abeta) is the main protein component of neuritic plaques in the brain of patients of Alzheimer's disease (AD), and its neurotoxicity would be exposed by the formation of aggregates. The aggregation inhibitors composed of an Abeta recognition element (KLVFF) and a hydrophilic moiety are evaluated by a novel fluorescence assay. These compounds inhibit growth of the model aggregates on the KLVFF immobilized surface. In addition, some compounds also possess disrupting activities of preformed aggregates. These compounds could be a key candidate for therapeutic drugs for AD by their novel molecular mechanisms.

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页码：1 / 6

页数：6

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