4-Hydroxy-2-sulfanylbenzonitrile

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯硫酚类
• 英文名称: 4-Hydroxy-2-sulfanylbenzonitrile
• 英文别名: 4-hydroxy-2-sulfanylbenzonitrile
• 化学式: C₇H₅NOS
• 分子量: 151.189
• InChiKey: DQPOGIUHNFCOLN-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  10
• 可旋转键数：
  0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  45
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  、 4-Hydroxy-2-sulfanylbenzonitrile 在 potassium carbonate 作用下， 以 乙腈 为溶剂， 反应 14.0h， 生成 2-[4-(2,6-Dichloro-3-propan-2-yloxyphenyl)-2-hydroxy-6-oxocyclohexen-1-yl]sulfanyl-4-hydroxybenzonitrile
  参考文献：
  名称：

  Optimization of 5-(2,6-dichlorophenyl)-3-hydroxy-2-mercaptocyclohex-2-enones as potent inhibitors of human lactate dehydrogenase

  摘要：

  Optimization of 5-(2,6-dichlorophenyl)-3-hydroxy-2-mercaptocyclohex-2-enone using structure-based design strategies resulted in inhibitors with considerable improvement in biochemical potency against human lactate dehydrogenase A (LDHA). These potent inhibitors were typically selective for LDHA over LDHB isoform (4-10 fold) and other structurally related malate dehydrogenases, MDH1 and MDH2 (>500 fold). An X-ray crystal structure of enzymatically most potent molecule bound to LDHA revealed two additional interactions associated with enhanced biochemical potency. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2014.11.008
• 作为产物：
  描述：

  2-溴-4-羟基苯甲腈 在 tris-(dibenzylideneacetone)dipalladium(0) 、 sodium ethanolate 、 N,N-二异丙基乙胺 、 4,5-双二苯基膦-9,9-二甲基氧杂蒽 作用下， 以 1,4-二氧六环 、 乙醇 为溶剂， 反应 2.5h， 生成 4-Hydroxy-2-sulfanylbenzonitrile
  参考文献：
  名称：

  Optimization of 5-(2,6-dichlorophenyl)-3-hydroxy-2-mercaptocyclohex-2-enones as potent inhibitors of human lactate dehydrogenase

  摘要：

  Optimization of 5-(2,6-dichlorophenyl)-3-hydroxy-2-mercaptocyclohex-2-enone using structure-based design strategies resulted in inhibitors with considerable improvement in biochemical potency against human lactate dehydrogenase A (LDHA). These potent inhibitors were typically selective for LDHA over LDHB isoform (4-10 fold) and other structurally related malate dehydrogenases, MDH1 and MDH2 (>500 fold). An X-ray crystal structure of enzymatically most potent molecule bound to LDHA revealed two additional interactions associated with enhanced biochemical potency. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2014.11.008