Specific targeting of acetylcholinesterase and butyrylcholinesterase recognition sites. Rational design of novel, selective, and highly potent cholinesterase inhibitors

被引：151

作者：

Savini, L

Gaeta, A

Fattorusso, C

Catalanotti, B

Campiani, G

Chiasserini, L

Pellerano, C

Novellino, E

McKissic, D

Saxena, A

机构：

[1] Univ Siena, Dipartimento Chim Tecnol, I-53100 Siena, Italy

[2] Univ Naples Federico II, Dipartimento Sostanze Nat, I-80131 Naples, Italy

[3] Univ Naples Federico II, Dipartimento Chim Farmaceut & Tossicol, I-80131 Naples, Italy

[4] Walter Reed Army Inst Res, Div Biochem, Silver Spring, MD 20910 USA

来源：

JOURNAL OF MEDICINAL CHEMISTRY | 2003年 / 46卷 / 01期

关键词：

D O I：

10.1021/jm0255668

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

Tacrine-based AChE and BuChE inhibitors were designed by investigating the topology of the active site gorge of the two enzymes. The homobivalent ligands characterized by a nitrogen-bridged atom at the tether level could be considered among the most potent and selective cholinesterase inhibitors described to date. The nitrogen-containing homobivalent ligands 3e,g and the sulfur-containing 3h validated the hypothesis of extra sites of interaction in the AChE and BuChE active site gorges.

引用

页码：1 / 4

页数：4

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