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

文献信息

• Optimization of 5-(2,6-dichlorophenyl)-3-hydroxy-2-mercaptocyclohex-2-enones as potent inhibitors of human lactate dehydrogenase
  作者：Sharada Labadie、Peter S. Dragovich、Jinhua Chen、Benjamin P. Fauber、Jason Boggs、Laura B. Corson、Charles Z. Ding、Charles Eigenbrot、HongXiu Ge、Qunh Ho、Kwong Wah Lai、Shuguang Ma、Shiva Malek、David Peterson、Hans E. Purkey、Kirk Robarge、Laurent Salphati、Steven Sideris、Mark Ultsch、Erica VanderPorten、BinQing Wei、Qing Xu、Ivana Yen、Qin Yue、Huihui Zhang、Xuying Zhang、Aihe Zhou

  DOI：10.1016/j.bmcl.2014.11.008

  日期：2015.1

  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.