Methyl 2-[4-(cyanomethyl)phenoxy]acetate | 1016782-84-5

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: Methyl 2-[4-(cyanomethyl)phenoxy]acetate
• CAS: 1016782-84-5
• 化学式: C₁₁H₁₁NO₃
• mdl: MFCD09934187
• 分子量: 205.213
• InChiKey: FOKHTQPSQAUWMB-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.1
• 重原子数：
  15
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.272
• 拓扑面积：
  59.3
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  Methyl 2-[4-(cyanomethyl)phenoxy]acetate 在 sodium tetrahydroborate 作用下， 以 四氢呋喃 、 甲醇 为溶剂， 生成 2-(4-carbomethoxymethoxyphenyl)ethanamine
  参考文献：
  名称：

  Structure–activity relationship studies of a bisbenzimidazole-based, Zn2+-dependent inhibitor of HCV NS3 serine protease

  摘要：

  A survey of isosteric replacements of the phosphonoalanine side chain coupled with a process of conformational constraint of a bisbenzimidazole-based, Zn2+-dependent inhibitor of hepatitis C virus (HCV) NS3 serine protease resulted in the identification of novel series of active compounds with extended side chains. However, Zn2+-dependent HCV NS3 inhibition was relatively insensitive to the structural variations examined but dependent on the presence of negatively charged functionality. This result was interpreted in the context of an initial electrostatic interaction between protease and inhibitor that is subsequently consolidated by Zn2+, with binding facilitated by the featureless active site and proximal regions of the HCV NS3 protein. (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(01)00457-7
• 作为产物：
  描述：

  对羟基苯乙腈 、 溴乙酸甲酯 在 potassium carbonate 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 Methyl 2-[4-(cyanomethyl)phenoxy]acetate
  参考文献：
  名称：

  Structure–activity relationship studies of a bisbenzimidazole-based, Zn2+-dependent inhibitor of HCV NS3 serine protease

  摘要：

  A survey of isosteric replacements of the phosphonoalanine side chain coupled with a process of conformational constraint of a bisbenzimidazole-based, Zn2+-dependent inhibitor of hepatitis C virus (HCV) NS3 serine protease resulted in the identification of novel series of active compounds with extended side chains. However, Zn2+-dependent HCV NS3 inhibition was relatively insensitive to the structural variations examined but dependent on the presence of negatively charged functionality. This result was interpreted in the context of an initial electrostatic interaction between protease and inhibitor that is subsequently consolidated by Zn2+, with binding facilitated by the featureless active site and proximal regions of the HCV NS3 protein. (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(01)00457-7

文献信息

• Structure–activity relationship studies of a bisbenzimidazole-based, Zn2+-dependent inhibitor of HCV NS3 serine protease
  作者：Kap-Sun Yeung、Nicholas A. Meanwell、Zhilei Qiu、Dennis Hernandez、Sharon Zhang、Fiona McPhee、Steve Weinheimer、James M. Clark、James W. Janc

  DOI：10.1016/s0960-894x(01)00457-7

  日期：2001.9

  A survey of isosteric replacements of the phosphonoalanine side chain coupled with a process of conformational constraint of a bisbenzimidazole-based, Zn2+-dependent inhibitor of hepatitis C virus (HCV) NS3 serine protease resulted in the identification of novel series of active compounds with extended side chains. However, Zn2+-dependent HCV NS3 inhibition was relatively insensitive to the structural variations examined but dependent on the presence of negatively charged functionality. This result was interpreted in the context of an initial electrostatic interaction between protease and inhibitor that is subsequently consolidated by Zn2+, with binding facilitated by the featureless active site and proximal regions of the HCV NS3 protein. (C) 2001 Elsevier Science Ltd. All rights reserved.