2-amino-6-(3,4-dimethoxyphenyl)pyrimidine-4-thiol | 1374960-25-4

• 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-amino-6-(3,4-dimethoxyphenyl)pyrimidine-4-thiol
• 英文别名: 2-amino-6-(3,4-dimethoxyphenyl)-1H-pyrimidine-4-thione
• CAS: 1374960-25-4
• 化学式: C₁₂H₁₃N₃O₂S
• 分子量: 263.32
• InChiKey: PTCSMONBDOALIH-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.9
• 重原子数：
  18
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.17
• 拓扑面积：
  101
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  3,4-二甲氧基苯甲酰乙酸乙酯 在 劳森试剂 、 potassium carbonate 作用下， 以 乙醇 、 甲苯 为溶剂， 反应 56.0h， 生成 2-amino-6-(3,4-dimethoxyphenyl)pyrimidine-4-thiol
  参考文献：
  名称：

  Identification of novel isocytosine derivatives as xanthine oxidase inhibitors from a set of virtual screening hits

  摘要：

  In recent years, xanthine oxidase has emerged as an important target not only for gout but also for cardiovascular and metabolic disorders involving hyperuricemia. Contrary to popular belief, recent clinical trials with uricosurics have demonstrated that enhanced excretion of uric acid is, by itself, not adequate to treat hyperuricemia; simultaneous inhibition of production of uric acid by inhibition of xanthine oxidase is also important. Virtual screening of in-house synthetic library followed by in vitro and in vivo testing led to the identification of a novel scaffold for xanthine oxidase inhibition. In vitro activity results corroborated the results from molecular docking studies of the virtual screening hits. The isocytosine scaffold maintains key hydrogen bonding and pi-stacking interactions in the deep end of the xanthine-binding pocket, which anchors it in an appropriate pose to inhibit binding of xanthine and shows promise for further lead optimization using structure-based drug design approach. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2012.03.019

文献信息

• Identification of novel isocytosine derivatives as xanthine oxidase inhibitors from a set of virtual screening hits
  作者：Chandrika B-Rao、Asha Kulkarni-Almeida、Kamlesh V. Katkar、Smriti Khanna、Usha Ghosh、Ashish Keche、Pranay Shah、Ankita Srivastava、Vaidehi Korde、Kumar V.S. Nemmani、Nitin J. Deshmukh、Amol Dixit、Manoja K. Brahma、Umakant Bahirat、Lalit Doshi、Rajiv Sharma、H. Sivaramakrishnan

  DOI：10.1016/j.bmc.2012.03.019

  日期：2012.5

  In recent years, xanthine oxidase has emerged as an important target not only for gout but also for cardiovascular and metabolic disorders involving hyperuricemia. Contrary to popular belief, recent clinical trials with uricosurics have demonstrated that enhanced excretion of uric acid is, by itself, not adequate to treat hyperuricemia; simultaneous inhibition of production of uric acid by inhibition of xanthine oxidase is also important. Virtual screening of in-house synthetic library followed by in vitro and in vivo testing led to the identification of a novel scaffold for xanthine oxidase inhibition. In vitro activity results corroborated the results from molecular docking studies of the virtual screening hits. The isocytosine scaffold maintains key hydrogen bonding and pi-stacking interactions in the deep end of the xanthine-binding pocket, which anchors it in an appropriate pose to inhibit binding of xanthine and shows promise for further lead optimization using structure-based drug design approach. (C) 2012 Elsevier Ltd. All rights reserved.