Fullerene inhibits β-amyloid peptide aggregation

被引：194

作者：

Kim, JE ^{[1
]}

Lee, M ^{[1
]}

机构：

[1] Ewha Womans Univ, Div Mol Life Sci, Dept Chem, Fluorescence Nanoscopy Lab, Seoul 120750, South Korea

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2003年 / 303卷 / 02期

关键词：

amyolid; fullerene; aggregation; inhibitor; thioflavin T; Alzheimer; fluorescence; hydrophobicity; oligomer; melatonin;

D O I：

10.1016/S0006-291X(03)00393-0

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：

We report that fullerene inhibits strongly the amyloid peptide aggregation at the early stage. It specifically binds to the central hydrophobic motif, KLVFF, of Abeta peptides. The IC50 value has been measured as 9 muM for both Abeta(11-25) and Abeta(11-40). On the other hand, a control experiment shows melatonin rather specifically binds to the C-terminus region. The IC50 value of fullerene appears to be at least four times larger for Abeta(1-40), compared with melatonin, and 15 times larger for Abeta(11-25). This work shows that fullerene can be a promising candidate in search of AD therapeutics because it has the very high IC50 value for Abeta aggregation. (C) 2003 Elsevier Science (USA). All rights reserved.

引用

页码：576 / 579

页数：4

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