2-[[5-cyano-4-(3,4-dichlorophenyl)-6-oxo-1H-pyrimidin-2-yl]sulfanyl]-N-(4-sulfamoylphenyl)propanamide | 1437691-41-2

• 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: 2-[[5-cyano-4-(3,4-dichlorophenyl)-6-oxo-1H-pyrimidin-2-yl]sulfanyl]-N-(4-sulfamoylphenyl)propanamide
• CAS: 1437691-41-2
• 化学式: C₂₀H₁₅Cl₂N₅O₄S₂
• 分子量: 524.408
• InChiKey: YDJOCTZRWDYNJT-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.9
• 重原子数：
  33
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.1
• 拓扑面积：
  188
• 氢给体数：
  3
• 氢受体数：
  8

反应信息

• 作为产物：
  描述：

  3,4-二氯苯甲醛 在 potassium carbonate 作用下， 以 乙醇 为溶剂， 生成 2-[[5-cyano-4-(3,4-dichlorophenyl)-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

文献信息

• Identification of substituted 2-thio-6-oxo-1,6-dihydropyrimidines as inhibitors of human lactate dehydrogenase
  作者：Peter S. Dragovich、Benjamin P. Fauber、Laura B. Corson、Charles Z. Ding、Charles Eigenbrot、HongXiu Ge、Anthony M. Giannetti、Thomas Hunsaker、Sharada Labadie、Yichin Liu、Shiva Malek、Borlan Pan、David Peterson、Keith Pitts、Hans E. Purkey、Steve Sideris、Mark Ultsch、Erica VanderPorten、BinQing Wei、Qing Xu、Ivana Yen、Qin Yue、Huihui Zhang、Xuying Zhang

  DOI：10.1016/j.bmcl.2013.04.001

  日期：2013.6

  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.