PTP抑制剂IV | 329317-98-8

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 中文名称: PTP抑制剂IV
• 英文名称: C,C,C-Trifluoro-N-[4-(1-methyl-1-{4-[1-methyl-1-(4-trifluoromethanesulfonylamino-phenyl)-ethyl]-phenyl}-ethyl)-phenyl]-methanesulfonamide
• 英文别名: PTP Inhibitor IV；1,1,1-trifluoro-N-[4-[2-[4-[2-[4-(trifluoromethylsulfonylamino)phenyl]propan-2-yl]phenyl]propan-2-yl]phenyl]methanesulfonamide
• CAS: 329317-98-8
• 化学式: C₂₆H₂₆F₆N₂O₄S₂
• 分子量: 608.626
• InChiKey: JWNAVYMNAQDLHX-UHFFFAOYSA-N

物化性质

• 沸点：
  578.0±60.0 °C(Predicted)
• 密度：
  1.416±0.06 g/cm3(Predicted)
• 溶解度：
  乙醇中≤25mg/ml；DMSO 中≤25mg/ml；二甲基甲酰胺中≤30mg/ml

计算性质

• 辛醇/水分配系数(LogP)：
  7.9
• 重原子数：
  40
• 可旋转键数：
  8
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.31
• 拓扑面积：
  109
• 氢给体数：
  2
• 氢受体数：
  12

反应信息

• 作为产物：
  描述：

  三氟甲磺酸酐 、 α,α'-双(4-氨基苯基)-1,4-二异丙基苯 在 碳酸氢钠 作用下， 以 二氯甲烷 为溶剂， 以863 mg的产率得到PTP抑制剂IV
  参考文献：
  名称：

  Structure-Based design and discovery of novel inhibitors of protein tyrosine phosphatases

  摘要：

  Protein tyrosine phosphatases (PTPs) are important in the regulation of signal transduction processes. Certain enzymes of this class are considered as potential therapeutic targets in the treatment of a variety of diseases such as diabetes, inflammation, and cancer. However, many PTP inhibitors identified to date are peptide-based and contain a highly charged phosphate-mimicking component. These compounds usually lack membrane permeability and this limits their utility in the inhibition of intracellular phosphatases. In the present study, we have used structure-based design and modeling techniques to explore catalytic-site directed, reversible inhibitors of PTPs. Employing a non-charged phosphate mimic and non-peptidyl structural components, we have successfully designed and synthesized a novel series of trifluoromethyl sulfonyl and trifluoromethyl sulfonamido compounds as PTP inhibitors. This is the first time that an uncharged phosphate mimic is reported in the literature for general, reversible, and substrate-competitive inhibition of PTPs. It is an important discovery because the finding may provide a paradigm for the development of phosphatase inhibitors that enter cells and modify signal transduction. (C) 2003 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(03)00039-7