2-Hydroxy-1,4-dihydroisoquinolin-3-one

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 异喹啉及其衍生物
• 英文名称: 2-Hydroxy-1,4-dihydroisoquinolin-3-one
• 化学式: C₉H₉NO₂
• 分子量: 163.176
• InChiKey: YOZVVRFEIGPQPK-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.4
• 重原子数：
  12
• 可旋转键数：
  0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.22
• 拓扑面积：
  40.5
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  甜菜安 在 盐酸 、 盐酸羟胺 、 sodium carbonate 作用下， 以 甲醇 、 乙醚 为溶剂， 反应 22.0h， 生成 2-Hydroxy-1,4-dihydroisoquinolin-3-one
  参考文献：
  名称：

  Synthesis and structure activity relationships of novel non-peptidic metallo-aminopeptidase inhibitors

  摘要：

  Racemic derivatives of 3-amino-2-tetralone were synthesised and evaluated for their ability to inhibit metallo-aminopeptidase activities. New compounds substituted in position 2 by methyl ketone, substituted oximes or hydroxamic acids as well as heterocyclic derivatives were evaluated against representative members of zinc-dependent aminopeptidases: leucine aminopeptidase (E.C. 3.4.11.1), aminopeptidase-N(E.C. 3.4.11.2), Aeronumas proteolytica aminopeptidase (E.C. 3.4.11.10), and the aminopeptidase activity of leukotriene A(4) hydrolase (E.C. 3.3.2.6). Several compounds showed K-i values in the low micromolar range against the 'one-zinc' aminopeptidases, while most of them were rather poor inhibitors of the 'two-zinc' enzymes. This interesting selectivity profile may guide the design of new, specific inhibitors of target mammalian aminopeptidases with one active site zinc. (c) 2006 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2006.06.050

文献信息

• US6183934B1
  申请人：——

  公开号：US6183934B1

  公开（公告）日：2001-02-06
• Synthesis and structure activity relationships of novel non-peptidic metallo-aminopeptidase inhibitors
  作者：Sébastien Albrecht、Albert Defoin、Emmanuel Salomon、Céline Tarnus、Anders Wetterholm、Jasper Z. Haeggström

  DOI：10.1016/j.bmc.2006.06.050

  日期：2006.11

  Racemic derivatives of 3-amino-2-tetralone were synthesised and evaluated for their ability to inhibit metallo-aminopeptidase activities. New compounds substituted in position 2 by methyl ketone, substituted oximes or hydroxamic acids as well as heterocyclic derivatives were evaluated against representative members of zinc-dependent aminopeptidases: leucine aminopeptidase (E.C. 3.4.11.1), aminopeptidase-N(E.C. 3.4.11.2), Aeronumas proteolytica aminopeptidase (E.C. 3.4.11.10), and the aminopeptidase activity of leukotriene A(4) hydrolase (E.C. 3.3.2.6). Several compounds showed K-i values in the low micromolar range against the 'one-zinc' aminopeptidases, while most of them were rather poor inhibitors of the 'two-zinc' enzymes. This interesting selectivity profile may guide the design of new, specific inhibitors of target mammalian aminopeptidases with one active site zinc. (c) 2006 Elsevier Ltd. All rights reserved.