(4-(4-Bromo-3,5-bis(trifluoromethyl)phenylcarbamoyl)phenyl)difluoromethylphosphonic acid | 1204733-25-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: (4-(4-Bromo-3,5-bis(trifluoromethyl)phenylcarbamoyl)phenyl)difluoromethylphosphonic acid
• 英文别名: [[4-[[4-bromo-3,5-bis(trifluoromethyl)phenyl]carbamoyl]phenyl]-difluoromethyl]phosphonic acid
• CAS: 1204733-25-4
• 化学式: C₁₆H₉BrF₈NO₄P
• 分子量: 542.117
• InChiKey: OMTCUGCCALSKMD-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.9
• 重原子数：
  31
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.19
• 拓扑面积：
  86.6
• 氢给体数：
  3
• 氢受体数：
  12

反应信息

• 作为产物：
  描述：

  在 三甲基硅咪唑 作用下， 以 氯仿 为溶剂， 反应 3.0h， 以41%的产率得到(4-(4-Bromo-3,5-bis(trifluoromethyl)phenylcarbamoyl)phenyl)difluoromethylphosphonic acid
  参考文献：
  名称：

  Fragment-based discovery of selective inhibitors of the Mycobacterium tuberculosis protein tyrosine phosphatase PtpA

  摘要：

  The development of low mu M inhibitors of the Mycobacterium tuberculosis phosphatase PtpA is reported. The most potent of these inhibitors (K-i = 1.4 +/- 0.3 mu M) was found to be selective when tested against a panel of human tyrosine and dual-specificity phosphatases (11-fold vs the highly homologous HCPtpA, and >70-fold vs all others tested). Modeling the inhibitor-PtpA complexes explained the structure-activity relationships observed in vitro and revealed further possibilities for compound development. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2009.10.090

文献信息

• Fragment-based discovery of selective inhibitors of the Mycobacterium tuberculosis protein tyrosine phosphatase PtpA
  作者：Katherine A. Rawls、P. Therese Lang、Jun Takeuchi、Shinichi Imamura、Tyler D. Baguley、Christoph Grundner、Tom Alber、Jonathan A. Ellman

  DOI：10.1016/j.bmcl.2009.10.090

  日期：2009.12

  The development of low mu M inhibitors of the Mycobacterium tuberculosis phosphatase PtpA is reported. The most potent of these inhibitors (K-i = 1.4 +/- 0.3 mu M) was found to be selective when tested against a panel of human tyrosine and dual-specificity phosphatases (11-fold vs the highly homologous HCPtpA, and >70-fold vs all others tested). Modeling the inhibitor-PtpA complexes explained the structure-activity relationships observed in vitro and revealed further possibilities for compound development. (C) 2009 Elsevier Ltd. All rights reserved.