5-(4-(4-(trifluoromethyl)phenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)thiophene-2-carbaldehyde | 1595282-85-1

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪类
• 英文名称: 5-(4-(4-(trifluoromethyl)phenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)thiophene-2-carbaldehyde
• CAS: 1595282-85-1
• 化学式: C₁₈H₁₀F₃N₃OS
• 分子量: 373.358
• InChiKey: GURMGVAJXCVKFL-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.98
• 重原子数：
  26.0
• 可旋转键数：
  3.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.06
• 拓扑面积：
  47.78
• 氢给体数：
  0.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  5-(4-(4-(trifluoromethyl)phenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)thiophene-2-carbaldehyde 、 间氨基苯甲酸 在 sodium cyanoborohydride 、 对甲苯磺酸 作用下， 以 甲醇 、 二氯甲烷 为溶剂， 反应 24.0h， 以38%的产率得到3-((5-(4-(4-(trifluoromethyl)phenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)thiophen-2-yl)methylamino)benzoic acid
  参考文献：
  名称：

  Using ‘biased-privileged’ scaffolds to identify lysine methyltransferase inhibitors

  摘要：

  Methylation of histones by lysine methyltransferases (KMTases) plays important roles in regulating chromatin function. It is also now clear that improper KMTases activity is linked to human diseases, such as cancer. We report an approach that employs drug-like 'privileged' scaffolds biased with motifs present in S-adenosyl methionine, the cofactor used by KMTases, to efficiently generate inhibitors for Set7, a biochemically well-characterized KMTase. Setin-1, the most potent inhibitor of Set7 we have developed also inhibits the KMTase G9a. Together these data suggest that these inhibitors should provide good starting points to generate useful probes for KMTase biology and guide the design of KMTase inhibitors with drug-like properties. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2014.02.024
• 作为产物：
  描述：

  4-三氟甲基苯硼酸 在 potassium phosphate 、 copper(l) iodide 、 1,1'-双(二苯膦基)二茂铁二氯化钯(II)二氯甲烷复合物 、 potassium carbonate 、 (1R,2R)-(-)-N,N'-二甲基-1,2-环己二胺 作用下， 以 1,4-二氧六环 、 水 为溶剂， 反应 48.0h， 生成 5-(4-(4-(trifluoromethyl)phenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)thiophene-2-carbaldehyde
  参考文献：
  名称：

  Using ‘biased-privileged’ scaffolds to identify lysine methyltransferase inhibitors

  摘要：

  Methylation of histones by lysine methyltransferases (KMTases) plays important roles in regulating chromatin function. It is also now clear that improper KMTases activity is linked to human diseases, such as cancer. We report an approach that employs drug-like 'privileged' scaffolds biased with motifs present in S-adenosyl methionine, the cofactor used by KMTases, to efficiently generate inhibitors for Set7, a biochemically well-characterized KMTase. Setin-1, the most potent inhibitor of Set7 we have developed also inhibits the KMTase G9a. Together these data suggest that these inhibitors should provide good starting points to generate useful probes for KMTase biology and guide the design of KMTase inhibitors with drug-like properties. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2014.02.024