N-[bis(diethoxyphosphoryl)methyl]-2,5-dichloroaniline | 666839-69-6

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机膦酸及其衍生物
• 英文名称: N-[bis(diethoxyphosphoryl)methyl]-2,5-dichloroaniline
• CAS: 666839-69-6
• 化学式: C₁₅H₂₅Cl₂NO₆P₂
• 分子量: 448.22
• InChiKey: FQMBDZUPPWIOBP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.4
• 重原子数：
  26
• 可旋转键数：
  12
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.6
• 拓扑面积：
  83.1
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  N-[bis(diethoxyphosphoryl)methyl]-2,5-dichloroaniline 在 盐酸 作用下， 反应 6.0h， 生成 N-(2,5-dichlorophenyl)aminomethylenebisphosphonic acid
  参考文献：
  名称：

  Tailoring the Structure of Aminobisphosphonates To Target Plant P5C Reductase

  摘要：

  Using the structure of (3,5-dichlorophenyl)aminomethylenebisphosphonic acid as a lead compound, 25 new phosphonates were synthesized and evaluated as possible inhibitors of Arabidopsis thaliana delta(1)-pyrroline-5-carboxylate (P5C) reductase. Derivatives substituted in the phenyl ring retained the inhibitory potential, though to a different extent. On the contrary any variation in the scaffold, i.e., the replacement of the second phosphonate moiety with a hydroxyl or an amino residue, resulted in a significant loss of biological activity. The availability of several structures capable of interfering with the catalytic mechanism in the micromolar to millimolar range allowed a proper structure-activity relationship analysis, leading us to hypothesize about the steric and electronic requirements for maintenance or enhancement of the inhibitory properties. Reversal experiments with suspension cultured cells provided evidence for the occurrence of enzyme inhibition in vivo. Because in higher plants the step catalyzed by P5C reductase is shared by all pathways leading to proline synthesis, these compounds may be exploited for the design of new substances endowed with herbicidal activity.

  DOI：

  10.1021/jf800029t
• 作为产物：
  描述：

  2,5-二氯苯胺 、 原甲酸三乙酯 、 亚磷酸二乙酯 生成 N-[bis(diethoxyphosphoryl)methyl]-2,5-dichloroaniline
  参考文献：
  名称：

  Tailoring the Structure of Aminobisphosphonates To Target Plant P5C Reductase

  摘要：

  Using the structure of (3,5-dichlorophenyl)aminomethylenebisphosphonic acid as a lead compound, 25 new phosphonates were synthesized and evaluated as possible inhibitors of Arabidopsis thaliana delta(1)-pyrroline-5-carboxylate (P5C) reductase. Derivatives substituted in the phenyl ring retained the inhibitory potential, though to a different extent. On the contrary any variation in the scaffold, i.e., the replacement of the second phosphonate moiety with a hydroxyl or an amino residue, resulted in a significant loss of biological activity. The availability of several structures capable of interfering with the catalytic mechanism in the micromolar to millimolar range allowed a proper structure-activity relationship analysis, leading us to hypothesize about the steric and electronic requirements for maintenance or enhancement of the inhibitory properties. Reversal experiments with suspension cultured cells provided evidence for the occurrence of enzyme inhibition in vivo. Because in higher plants the step catalyzed by P5C reductase is shared by all pathways leading to proline synthesis, these compounds may be exploited for the design of new substances endowed with herbicidal activity.

  DOI：

  10.1021/jf800029t

文献信息

• Tailoring the Structure of Aminobisphosphonates To Target Plant P5C Reductase
  作者：Giuseppe Forlani、Andrea Occhipinti、Łukasz Berlicki、Gabriela Dziedzioła、Anna Wieczorek、Paweł Kafarski

  DOI：10.1021/jf800029t

  日期：2008.5.1

  Using the structure of (3,5-dichlorophenyl)aminomethylenebisphosphonic acid as a lead compound, 25 new phosphonates were synthesized and evaluated as possible inhibitors of Arabidopsis thaliana delta(1)-pyrroline-5-carboxylate (P5C) reductase. Derivatives substituted in the phenyl ring retained the inhibitory potential, though to a different extent. On the contrary any variation in the scaffold, i.e., the replacement of the second phosphonate moiety with a hydroxyl or an amino residue, resulted in a significant loss of biological activity. The availability of several structures capable of interfering with the catalytic mechanism in the micromolar to millimolar range allowed a proper structure-activity relationship analysis, leading us to hypothesize about the steric and electronic requirements for maintenance or enhancement of the inhibitory properties. Reversal experiments with suspension cultured cells provided evidence for the occurrence of enzyme inhibition in vivo. Because in higher plants the step catalyzed by P5C reductase is shared by all pathways leading to proline synthesis, these compounds may be exploited for the design of new substances endowed with herbicidal activity.