Catechol derivatives inhibit the fibril formation of amyloid-β peptides

被引：48
|
作者：
Vu Thi Huong [1 ]
Shimanouchi, Toshinori [1 ]
Shimauchi, Naoya [1 ]
Yagi, Hisashi [2 ]
Umakoshi, Hiroshi [1 ]
Goto, Yuji [2 ]
Kuboi, Ryoichi [1 ]
机构：
[1] Osaka Univ, Grad Sch Engn Sci, Dept Engn Sci, Div Chem Engn, Toyonaka, Osaka 5608531, Japan
[2] Osaka Univ, Inst Prot Res, Suita, Osaka 5650871, Japan
来源：
JOURNAL OF BIOSCIENCE AND BIOENGINEERING | 2010年 / 109卷 / 06期
关键词：
Liposome; Fibril formation; Inhibitor; Catechol derivatives; Amyloid beta; Alzheimer's disease; IN-VITRO; ALZHEIMERS-DISEASE; ALPHA-SYNUCLEIN; VITAMIN-E; PROTEIN; TOXICITY; MODEL; THERAPEUTICS; PREVENTION; MEMBRANES;
D O I：
10.1016/j.jbiosc.2009.11.010
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
The inhibition of fibril formation of amyloid beta proteins (A beta) would be attractive therapeutic targets for the treatment of Alzheimer's disease (AD). Dopamine (DA) and other catechol derivatives were used as inhibitory factors for A beta fibril formation. The fibril formation of A beta was monitored by Thioflavin T fluorescence, a transmission electron microscopy (TEM) and a total internal reflection fluorescence microscopy (TIRFM). Catechol and its derivatives showed the dose-dependent inhibitory effects on the spontaneous A beta fibril formation. The inhibitory activity depended on the chemical structure of catechol derivatives both in the presence and absence of the liposome a model of biomembrane. Formation of catechol quinone-conjugated-A beta adduct by a Schiff-base is a key step for the inhibition effect of A beta fibril formation. (C) 2009, The Society for Biotechnology, japan. All rights reserved.
引用
收藏
页码：629 / 634
页数：6
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