(2Z)-2-benzylidene-N-(4-phenylbutyl)-N'-trityloxypropanediamide | 934619-04-2

• 分子结构分类: 有机化合物 - 苯类化合物 - 三苯基化合物
• 英文名称: (2Z)-2-benzylidene-N-(4-phenylbutyl)-N'-trityloxypropanediamide
• CAS: 934619-04-2
• 化学式: C₃₉H₃₆N₂O₃
• 分子量: 580.726
• InChiKey: XYACRSXZDVYZBI-BBTNWVSFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  9.6
• 重原子数：
  44
• 可旋转键数：
  13
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.13
• 拓扑面积：
  67.4
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  (2Z)-2-benzylidene-N-(4-phenylbutyl)-N'-trityloxypropanediamide 在 三异丙基硅烷 、 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 0.08h， 以89%的产率得到N-hydroxy-N''-(4-phenyl-butyl)-2-[1-phenyl-meth-(Z)-ylidene]-malonamide
  参考文献：
  名称：

  Novel Selective Inhibitors of the Zinc Plasmodial Aminopeptidase PfA-M1 as Potential Antimalarial Agents

  摘要：

  Proteases that are expressed during the erythocytic stage of Plasmodium falciparum are newly explored drug targets for the treatment of malaria. We report here the discovery of potent inhibitors of PfA-M1, a metallo-aminopeptidase of the parasite. These compounds are based on a malonic hydroxamic template and present a very good selectivity toward neutral aminopeptidase (APN-CD13), a related protease in mammals. Structure-activity relationships in these series are described. Further optimization of the best inhibitor yielded a nanomolar, selective inhibitor of PfA-M1. This inhibitor displays good physicochemical and pharmacokinetic properties and a promising antimalarial activity.

  DOI：

  10.1021/jm061169b
• 作为产物：
  描述：

  (Z)-2-(ethoxycarbonyl)-3-phenylacrylic acid 在 N,N-二甲基甲酰胺 lithium hydroxide 、 草酰氯 、 氯甲酸乙酯 、 三乙胺 、 N,N-二异丙基乙胺 作用下， 以 四氢呋喃 、 二氯甲烷 、 水 为溶剂， 反应 5.25h， 生成 (2Z)-2-benzylidene-N-(4-phenylbutyl)-N'-trityloxypropanediamide
  参考文献：
  名称：

  Novel Selective Inhibitors of the Zinc Plasmodial Aminopeptidase PfA-M1 as Potential Antimalarial Agents

  摘要：

  Proteases that are expressed during the erythocytic stage of Plasmodium falciparum are newly explored drug targets for the treatment of malaria. We report here the discovery of potent inhibitors of PfA-M1, a metallo-aminopeptidase of the parasite. These compounds are based on a malonic hydroxamic template and present a very good selectivity toward neutral aminopeptidase (APN-CD13), a related protease in mammals. Structure-activity relationships in these series are described. Further optimization of the best inhibitor yielded a nanomolar, selective inhibitor of PfA-M1. This inhibitor displays good physicochemical and pharmacokinetic properties and a promising antimalarial activity.

  DOI：

  10.1021/jm061169b

文献信息

• Novel Selective Inhibitors of the Zinc Plasmodial Aminopeptidase PfA-M1 as Potential Antimalarial Agents
  作者：Marion Flipo、Terence Beghyn、Virginie Leroux、Isabelle Florent、Benoit P. Deprez、Rebecca F. Deprez-Poulain

  DOI：10.1021/jm061169b

  日期：2007.3.1

  Proteases that are expressed during the erythocytic stage of Plasmodium falciparum are newly explored drug targets for the treatment of malaria. We report here the discovery of potent inhibitors of PfA-M1, a metallo-aminopeptidase of the parasite. These compounds are based on a malonic hydroxamic template and present a very good selectivity toward neutral aminopeptidase (APN-CD13), a related protease in mammals. Structure-activity relationships in these series are described. Further optimization of the best inhibitor yielded a nanomolar, selective inhibitor of PfA-M1. This inhibitor displays good physicochemical and pharmacokinetic properties and a promising antimalarial activity.