ethyl 2-<4-<(cyclopentyl)oxy>phenyl>-2-oxoacetate | 166319-62-6

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚醚
• 英文名称: ethyl 2-<4-<(cyclopentyl)oxy>phenyl>-2-oxoacetate
• 英文别名: Ethyl 2-(4-cyclopentyloxyphenyl)-2-oxoacetate
• CAS: 166319-62-6
• 化学式: C₁₅H₁₈O₄
• 分子量: 262.306
• InChiKey: MBIVBLFBRQKZFQ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.3
• 重原子数：
  19
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  52.6
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  ethyl 2-<4-<(cyclopentyl)oxy>phenyl>-2-oxoacetate 在 palladium on activated charcoal 盐酸 、 氨 、 氢气 、 1,8-二氮杂双环[5.4.0]十一碳-7-烯 、 三乙胺 作用下， 以 四氢呋喃 、 乙醇 为溶剂， 25.0 ℃ 、101.33 kPa 条件下， 反应 23.0h， 生成 ethyl 3-<7-(N-tert-butoxycarbonylamidino)-2-naphthyl>-2-<4-<(cyclopentyl)oxy>phenyl>propanoate
  参考文献：
  名称：

  Molecular model of an interaction between factor Xa and DX-9065a, a novel factor Xa inhibitor: Contribution of the acetimidoylpyrrolidine moiety of the inhibitor to potency and selectivity for serine proteases

  摘要：

  Molecular modeling of a complex between factor Xa (FXa) and DX-9065a, a novel FXa inhibitor, has demonstrated a salt-bridge interaction of the amidinonaphthalene moiety of the inhibitor to the S1 site pocket of the enzyme and a crucial carboxyl group of the inhibitor for the FXa/thrombin selectivity. In the present study, we synthesized some DX-9065a derivatives and studied their interaction modes with FXa, trypsin and thrombin to evaluate the role of the acetimidoylpyrrolidine moiety. The docking study of the inhibitor in the FXa model provided a molecular model of the inhibitor-FXa complex showing a hydrophobic interaction of the pyrrolidine ring with an aryl binding site of FXa, and a hydrogen bond between the acetimidoyl group and the backbone carbonyl oxygen of Glu97. Comparison between the interaction mode of DX-9065a with FXa and those with trypsin and thrombin explained the inhibitory potencies of the enzymes.

  DOI：

  10.1016/0223-5234(96)88248-1
• 作为产物：
  描述：

  2-(4-羟苯基)-2-氧代乙酸乙酯 、 环戊醇 在 三苯基膦 、 偶氮二甲酸二乙酯 作用下， 以 四氢呋喃 为溶剂， 反应 18.0h， 以85.8%的产率得到ethyl 2-<4-<(cyclopentyl)oxy>phenyl>-2-oxoacetate
  参考文献：
  名称：

  Molecular model of an interaction between factor Xa and DX-9065a, a novel factor Xa inhibitor: Contribution of the acetimidoylpyrrolidine moiety of the inhibitor to potency and selectivity for serine proteases

  摘要：

  Molecular modeling of a complex between factor Xa (FXa) and DX-9065a, a novel FXa inhibitor, has demonstrated a salt-bridge interaction of the amidinonaphthalene moiety of the inhibitor to the S1 site pocket of the enzyme and a crucial carboxyl group of the inhibitor for the FXa/thrombin selectivity. In the present study, we synthesized some DX-9065a derivatives and studied their interaction modes with FXa, trypsin and thrombin to evaluate the role of the acetimidoylpyrrolidine moiety. The docking study of the inhibitor in the FXa model provided a molecular model of the inhibitor-FXa complex showing a hydrophobic interaction of the pyrrolidine ring with an aryl binding site of FXa, and a hydrogen bond between the acetimidoyl group and the backbone carbonyl oxygen of Glu97. Comparison between the interaction mode of DX-9065a with FXa and those with trypsin and thrombin explained the inhibitory potencies of the enzymes.

  DOI：

  10.1016/0223-5234(96)88248-1

文献信息

• Molecular model of an interaction between factor Xa and DX-9065a, a novel factor Xa inhibitor: Contribution of the acetimidoylpyrrolidine moiety of the inhibitor to potency and selectivity for serine proteases
  作者：S Katakura、T Nagahara、T Hara、S Kunitada、M Iwamoto

  DOI：10.1016/0223-5234(96)88248-1

  日期：1995.1

  Molecular modeling of a complex between factor Xa (FXa) and DX-9065a, a novel FXa inhibitor, has demonstrated a salt-bridge interaction of the amidinonaphthalene moiety of the inhibitor to the S1 site pocket of the enzyme and a crucial carboxyl group of the inhibitor for the FXa/thrombin selectivity. In the present study, we synthesized some DX-9065a derivatives and studied their interaction modes with FXa, trypsin and thrombin to evaluate the role of the acetimidoylpyrrolidine moiety. The docking study of the inhibitor in the FXa model provided a molecular model of the inhibitor-FXa complex showing a hydrophobic interaction of the pyrrolidine ring with an aryl binding site of FXa, and a hydrogen bond between the acetimidoyl group and the backbone carbonyl oxygen of Glu97. Comparison between the interaction mode of DX-9065a with FXa and those with trypsin and thrombin explained the inhibitory potencies of the enzymes.