[(η⁶-cymene)Ru(NC₅H₄C₃H₂N₂CH₂C₆H₄CF₂P(O)(OEt)₂)Cl]PF₆ | 1408238-96-9

• 英文名称: [(η⁶-cymene)Ru(NC₅H₄C₃H₂N₂CH₂C₆H₄CF₂P(O)(OEt)₂)Cl]PF₆
• CAS: 1408238-96-9
• 化学式: C₃₀H₃₆ClF₂N₃O₃PRu*F₆P
• 分子量: 837.092
• InChiKey: YRGYGWZACGIHIE-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  None
• 重原子数：
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• 可旋转键数：
  None
• 环数：
  None
• sp3杂化的碳原子比例：
  None
• 拓扑面积：
  None
• 氢给体数：
  None
• 氢受体数：
  None

反应信息

• 作为反应物：
  描述：

  甲醇 、 碘代三甲硅烷 、 [(η⁶-cymene)Ru(NC₅H₄C₃H₂N₂CH₂C₆H₄CF₂P(O)(OEt)₂)Cl]PF₆ 以 二氯甲烷 为溶剂， 反应 24.0h， 以81%的产率得到[(η⁶-cymene)Ru(NC₅H₄C₃H₂N₂CH₂C₆H₄CF₂P(O)(OH)₂)I]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：

  ammonium hexafluorophosphate 、 [ruthenium(II)(η⁶-1-methyl-4-isopropyl-benzene)(chloride)(μ-chloride)]₂ 、 2-[1-[[4-[Diethoxyphosphoryl(difluoro)methyl]phenyl]methyl]imidazol-2-yl]pyridine 以 甲醇 为溶剂， 反应 4.5h， 以95%的产率得到[(η⁶-cymene)Ru(NC₅H₄C₃H₂N₂CH₂C₆H₄CF₂P(O)(OEt)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