S-2-dodecylphenyl dimethylcarbamothioate | 29688-04-8

• 分子结构分类: 有机化合物 - 有机硫化合物 - 硫醚类
• 英文名称: S-2-dodecylphenyl dimethylcarbamothioate
• 英文别名: S-(o-Dodecylphenyl)dimethylthiocarbamat
• CAS: 29688-04-8
• 化学式: C₂₁H₃₅NOS
• 分子量: 349.581
• InChiKey: YGGUAUCTSICPSP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.92
• 重原子数：
  24.0
• 可旋转键数：
  12.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  20.31
• 氢给体数：
  0.0
• 氢受体数：
  2.0

反应信息

• 作为反应物：
  描述：

  S-2-dodecylphenyl dimethylcarbamothioate 在 甲酸 、 双氧水 、 三氯氧磷 作用下， 生成 2-十二烷基苯磺酰氯
  参考文献：
  名称：

  Development of sulfonamide AKT PH domain inhibitors

  摘要：

  Disruption of the phosphatidylinositol 3-kinase/AKT signaling pathway can lead to apoptosis in cancer cells. Previously we identified a lead sulfonamide that selectively bound to the pleckstrin homology (PH) domain of AKT and induced apoptosis when present at low micromolar concentrations. To examine the effects of structural modification, a set of sulfonamides related to the lead compound was designed, synthesized, and tested for binding to the expressed PH domain of AKT using a surface plasmon resonance-based competitive binding assay. Cellular activity was determined by means of an assay for pAKT production and a cell killing assay using BxPC-3 cells. The most active compounds in the set are lipophilic and possess an aliphatic chain of the proper length. Results were interpreted with the aid of computational modeling. This paper represents the first structure-activity relationship (SAR) study of a large family of AKT PH domain inhibitors. Information obtained will be used in the design of the next generation of inhibitors of AKT PH domain function. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2011.01.049
• 作为产物：
  描述：

  2-十二烷基酚 在 sodium hydride 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 13.5h， 生成 S-2-dodecylphenyl dimethylcarbamothioate
  参考文献：
  名称：

  Development of sulfonamide AKT PH domain inhibitors

  摘要：

  Disruption of the phosphatidylinositol 3-kinase/AKT signaling pathway can lead to apoptosis in cancer cells. Previously we identified a lead sulfonamide that selectively bound to the pleckstrin homology (PH) domain of AKT and induced apoptosis when present at low micromolar concentrations. To examine the effects of structural modification, a set of sulfonamides related to the lead compound was designed, synthesized, and tested for binding to the expressed PH domain of AKT using a surface plasmon resonance-based competitive binding assay. Cellular activity was determined by means of an assay for pAKT production and a cell killing assay using BxPC-3 cells. The most active compounds in the set are lipophilic and possess an aliphatic chain of the proper length. Results were interpreted with the aid of computational modeling. This paper represents the first structure-activity relationship (SAR) study of a large family of AKT PH domain inhibitors. Information obtained will be used in the design of the next generation of inhibitors of AKT PH domain function. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2011.01.049