6-(4-chloro-3-fluorophenyl)-4-oxo-2-sulfanylidene-1H-pyrimidine-5-carbonitrile | 1437691-53-6

• 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: 6-(4-chloro-3-fluorophenyl)-4-oxo-2-sulfanylidene-1H-pyrimidine-5-carbonitrile
• CAS: 1437691-53-6
• 化学式: C₁₁H₅ClFN₃OS
• 分子量: 281.698
• InChiKey: ZNEUPEODGJKOQD-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.9
• 重原子数：
  18
• 可旋转键数：
  1
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  97
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  6-(4-chloro-3-fluorophenyl)-4-oxo-2-sulfanylidene-1H-pyrimidine-5-carbonitrile 、 2-bromo-N-(4-sulfamoylphenyl)propanamide 在 potassium carbonate 作用下， 以 乙醇 为溶剂， 生成 2-[[4-(4-chloro-3-fluorophenyl)-5-cyano-6-oxo-1H-pyrimidin-2-yl]sulfanyl]-N-(4-sulfamoylphenyl)propanamide
  参考文献：
  名称：

  Identification of substituted 2-thio-6-oxo-1,6-dihydropyrimidines as inhibitors of human lactate dehydrogenase

  摘要：

  A novel 2-thio-6-oxo-1,6-dihydropyrimidine-containing inhibitor of human lactate dehydrogenase (LDH) was identified by high-throughput screening (IC50 = 8.1 mu M). Biochemical, surface plasmon resonance, and saturation transfer difference NMR experiments indicated that the compound specifically associated with human LDHA in a manner that required simultaneous binding of the NADH co-factor. Structural variation of the screening hit resulted in significant improvements in LDHA biochemical inhibition activity (best IC50 = 0.48 mu M). A crystal structure of an optimized compound bound to human LDHA was obtained and explained many of the observed structure-activity relationships. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.04.001
• 作为产物：
  描述：

  硫脲 、 氰乙酸乙酯 、 4-氯-3-氟苯甲醛 以 乙醇 为溶剂， 生成 6-(4-chloro-3-fluorophenyl)-4-oxo-2-sulfanylidene-1H-pyrimidine-5-carbonitrile
  参考文献：
  名称：

  Identification of substituted 2-thio-6-oxo-1,6-dihydropyrimidines as inhibitors of human lactate dehydrogenase

  摘要：

  A novel 2-thio-6-oxo-1,6-dihydropyrimidine-containing inhibitor of human lactate dehydrogenase (LDH) was identified by high-throughput screening (IC50 = 8.1 mu M). Biochemical, surface plasmon resonance, and saturation transfer difference NMR experiments indicated that the compound specifically associated with human LDHA in a manner that required simultaneous binding of the NADH co-factor. Structural variation of the screening hit resulted in significant improvements in LDHA biochemical inhibition activity (best IC50 = 0.48 mu M). A crystal structure of an optimized compound bound to human LDHA was obtained and explained many of the observed structure-activity relationships. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.04.001