The inhibitory effect of laminin 1 and synthetic peptides deduced from the sequence in the laminin α1 chain on Aβ40 fibril formation in vitro

被引:12
作者
Monji, A [1 ]
Tashiro, K
Hayashi, Y
Yoshida, I
Tashiro, N
机构
[1] Kyushu Univ, Fac Med, Dept Neuropsychiat, Fukuoka 8128582, Japan
[2] Miyazaki Med Coll, Dept Psychiat, Miyazaki 8891601, Japan
关键词
laminin; Alzheimer's disease; amyloid-beta-protein; synthetic peptides; thioflavine-T fluorescence; electron microscopy;
D O I
10.1016/S0304-3940(98)00499-6
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
We investigated whether or not laminin 1 and the two different synthetic peptides deduced from the sequence in the laminin arl chain, both of which mediate cell attachment and neurite outgrowth in PC12 cells, have an effect on A beta 40 fibril formation in vitro. A thioflavine-T fluorometric assay showed a synthetic peptide containing the YFQRYLI sequence from the laminin alpha 1 chain to inhibit A beta 40 fibril formation while the inhibitory effect of this peptide was found to be somewhat less than that of intact laminin 1. These results were confirmed by electron microscopic observations using negative staining. The findings of the present study suggested that the synthetic peptide derived from the laminin alpha 1 chain may thus be an effective therapeutic agent for either preventing or slowing down the progression of amyloidogenesis in Alzheimer's disease. (C) 1998 Elsevier Science Ireland Ltd. All rights reserved.
引用
收藏
页码:65 / 68
页数:4
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