[Difluoro-[4-[(2-pyridin-2-ylbenzimidazol-1-yl)methyl]phenyl]methyl]phosphonic acid | 1408232-38-1

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并咪唑类
• 英文名称: [Difluoro-[4-[(2-pyridin-2-ylbenzimidazol-1-yl)methyl]phenyl]methyl]phosphonic acid
• 英文别名: [difluoro-[4-[(2-pyridin-2-ylbenzimidazol-1-yl)methyl]phenyl]methyl]phosphonic acid
• CAS: 1408232-38-1
• 化学式: C₂₀H₁₆F₂N₃O₃P
• 分子量: 415.336
• InChiKey: YANRDVUWSCOVLC-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.4
• 重原子数：
  29
• 可旋转键数：
  5
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.1
• 拓扑面积：
  88.2
• 氢给体数：
  2
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  [(η⁶-1,3,5-ⁱPr₃C₆H₃)RuCl(μ-Cl)]₂ 、 [Difluoro-[4-[(2-pyridin-2-ylbenzimidazol-1-yl)methyl]phenyl]methyl]phosphonic acid 以 甲醇 、 水 为溶剂， 以90%的产率得到[(η⁶-TIPB)Ru(NC₇H₄C₃H₂N₂CH₂C₆H₄CF₂P(O)(OH)₂)Cl]PF₆
  参考文献：
  名称：

  Rational Design of Selective Organoruthenium Inhibitors of Protein Tyrosine Phosphatase 1B

  摘要：

  Protein tyrosine phosphatases (PTPs) belong to a large family of important regulatory enzymes involved in vital mammalian signaling pathways. Selective inhibitors of PTPs are highly valuable from a therapeutic standpoint given their association with various pathological conditions. One such target is PTP-1B which has previously been linked to diabetes and cancer. However, developing a selective inhibitor against PTP-1B has proven to be daunting because the enzyme shares a high degree of structural homology with TC-PTP, an essential PTP involved in modulating immune functions. To address this challenge, a series of organoruthenium complexes was developed to bind at the PTP substrate-binding site while simultaneously target the peripheral structural space. By capitalizing on the potential difference in the structural environment proximal to the active site between different PTPs, selectivity toward PTP-1B over TC-PTP was improved, paving the way for organoruthenium complexes as selective PTP-1B metalloinhibitors.

  DOI：

  10.1021/ic301884j
• 作为产物：
  描述：

  diethyl (4-methylbenzoyl)phosphonate 在 甲醇 、 偶氮二异丁腈 、 碘代三甲硅烷 、 potassium tert-butylate 、 N,O-双(三甲基硅烷基)三氟乙酰胺 作用下， 以 四氯化碳 、 二氯甲烷 、 N,N-二甲基甲酰胺 、 正丁醇 为溶剂， 反应 27.0h， 生成 [Difluoro-[4-[(2-pyridin-2-ylbenzimidazol-1-yl)methyl]phenyl]methyl]phosphonic acid
  参考文献：
  名称：

  Rational Design of Selective Organoruthenium Inhibitors of Protein Tyrosine Phosphatase 1B

  摘要：

  Protein tyrosine phosphatases (PTPs) belong to a large family of important regulatory enzymes involved in vital mammalian signaling pathways. Selective inhibitors of PTPs are highly valuable from a therapeutic standpoint given their association with various pathological conditions. One such target is PTP-1B which has previously been linked to diabetes and cancer. However, developing a selective inhibitor against PTP-1B has proven to be daunting because the enzyme shares a high degree of structural homology with TC-PTP, an essential PTP involved in modulating immune functions. To address this challenge, a series of organoruthenium complexes was developed to bind at the PTP substrate-binding site while simultaneously target the peripheral structural space. By capitalizing on the potential difference in the structural environment proximal to the active site between different PTPs, selectivity toward PTP-1B over TC-PTP was improved, paving the way for organoruthenium complexes as selective PTP-1B metalloinhibitors.

  DOI：

  10.1021/ic301884j

文献信息

• Rational Design of Selective Organoruthenium Inhibitors of Protein Tyrosine Phosphatase 1B
  作者：Jun Xiang Ong、Chun Wei Yap、Wee Han Ang

  DOI：10.1021/ic301884j

  日期：2012.11.19

  Protein tyrosine phosphatases (PTPs) belong to a large family of important regulatory enzymes involved in vital mammalian signaling pathways. Selective inhibitors of PTPs are highly valuable from a therapeutic standpoint given their association with various pathological conditions. One such target is PTP-1B which has previously been linked to diabetes and cancer. However, developing a selective inhibitor against PTP-1B has proven to be daunting because the enzyme shares a high degree of structural homology with TC-PTP, an essential PTP involved in modulating immune functions. To address this challenge, a series of organoruthenium complexes was developed to bind at the PTP substrate-binding site while simultaneously target the peripheral structural space. By capitalizing on the potential difference in the structural environment proximal to the active site between different PTPs, selectivity toward PTP-1B over TC-PTP was improved, paving the way for organoruthenium complexes as selective PTP-1B metalloinhibitors.