Aminostyrylbenzofuran derivatives as potent inhibitors for Aβ fibril formation

被引：61

作者：

Byun, Ji Hun ^{[1
,2
,3
]}

Kim, HyeYun ^{[3
]}

Kim, YoungSoo ^{[3
]}

Mook-Jung, Inhee ^{[4
,5
]}

Kim, Dong Jin ^{[3
]}

Lee, Won Koo ^{[1
,2
]}

Yoo, Kyung Ho ^{[3
]}

机构：

[1] Sogang Univ, Dept Chem, Seoul 121742, South Korea

[2] Sogang Univ, Interdisciplinary Program Integrated Biotechnol, Seoul 121742, South Korea

[3] Korea Inst Sci & Technol, Life Sci Res Div, Seoul 130650, South Korea

[4] Seoul Natl Univ, Coll Med, Dept Biochem, Seoul 110799, South Korea

[5] Seoul Natl Univ, Coll Med, Canc Res Inst, Seoul 110799, South Korea

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2008年 / 18卷 / 20期

关键词：

Alzheimer's disease; A beta 42 fibrils; aminostyrylbenzofurans; inhibitory activity;

D O I：

10.1016/j.bmcl.2008.08.111

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

The synthesis of a novel series of aminostyrylbenzofuran derivatives 1a-w and their inhibitory activities for A beta fibril formation were described. All the synthesized compounds were evaluated by thioflavin T (ThT) assay and displayed potent inhibitory activities for A beta fibril formation. Among them, compounds 1i and 1q exhibited excellent inhibitory activities (IC(50) = 0.07 and 0.08 mu M, respectively) than those of Curcumin (IC(50) = 0.80 mu M) and IMSB (IC(50) = 8.00 mu M) as reference compounds. Both compounds were selected as promising candidates for further biological evaluation. (C) 2008 Elsevier Ltd. All rights reserved.

引用

页码：5591 / 5593

页数：3

共 27 条

[1] Synthesis of calix[4] crowns containing soft donor atoms and a study of their metal-cation binding properties:: highly selective receptors for Cu2+ [J].

Ashram, M .

JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS 2, 2002, (10) :1662-1668

[2] THE MICHAELIS-ARBUZOV REARRANGEMENT [J].

BHATTACHARYA, AK ;

THYAGARAJAN, G .

CHEMICAL REVIEWS, 1981, 81 (04) :415-430

[3] RELEASE OF EXCESS AMYLOID BETA-PROTEIN FROM A MUTANT AMYLOID BETA-PROTEIN PRECURSOR [J].

CAI, XD ;

GOLDE, TE ;

YOUNKIN, SG .

SCIENCE, 1993, 259 (5094) :514-516

[4] Clinical features of Alzheimer's disease [J].

Förstl, H ;

Kurz, A .

EUROPEAN ARCHIVES OF PSYCHIATRY AND CLINICAL NEUROSCIENCE, 1999, 249 (06) :288-290

[5] The role of cerebral amyloid β accumulation in common forms of Alzheimer disease [J].

Gandy, S .

JOURNAL OF CLINICAL INVESTIGATION, 2005, 115 (05) :1121-1129

[6] ALZHEIMERS-DISEASE - INITIAL REPORT OF THE PURIFICATION AND CHARACTERIZATION OF A NOVEL CEREBROVASCULAR AMYLOID PROTEIN [J].

GLENNER, GG ;

WONG, CW .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1984, 120 (03) :885-890

[7] Prevention of transthyretin amyloid disease by changing protein misfolding energetics [J].

Hammarström, P ;

Wiseman, RL ;

Powers, ET ;

Kelly, JW .

SCIENCE, 2003, 299 (5607) :713-716

[8] Medicine - The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics [J].

Hardy, J ;

Selkoe, DJ .

SCIENCE, 2002, 297 (5580) :353-356

[9] Total syntheses of three natural products, vignafuran, 2-(4-hydroxy-2-methoxyphenyl)-6-methoxybenzofuran-3-carboxylic acid methyl ester, and coumestrol from a common starting material [J].

Hiroya, K ;

Suzuki, N ;

Yasuhara, A ;

Egawa, Y ;

Kasano, A ;

Sakamoto, T .

JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS 1, 2000, (24) :4339-4346

[10] Convenient method for the ortho-formylation of phenols [J].

Hofslokken, NU ;

Skattebol, L .

ACTA CHEMICA SCANDINAVICA, 1999, 53 (04) :258-262

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