N-(6-Chloro-3-pyridazinyl)guanidine | 425376-95-0

• 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: N-(6-Chloro-3-pyridazinyl)guanidine
• 英文别名: 2-(6-chloropyridazin-3-yl)guanidine
• CAS: 425376-95-0
• 化学式: C₅H₆ClN₅
• 分子量: 171.589
• InChiKey: CYLOVBUDQYGUGV-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.4
• 重原子数：
  11
• 可旋转键数：
  1
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  90.2
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  N-(6-Chloro-3-pyridazinyl)guanidine 在 palladium on activated charcoal 氢气 作用下， 以 乙醇 为溶剂， 生成 pyridazin-3-yl guanidin
  参考文献：
  名称：

  Selective urokinase-type plasminogen activator (uPA) inhibitors. Part 1: 2-Pyridinylguanidines

  摘要：

  The identification of 2-pyridinylguanidines (e.g. 27 and 28) as selective inhibitors of urokinase-type plasminogen activator (uPA) is described. The X-ray crystal structure of 27 has been determined, and modelling has been used to predict binding in the enzyme active site. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(01)00701-6
• 作为产物：
  描述：

  3,6-二氯哒嗪 、 胍 以 二甲基亚砜 为溶剂， 生成 N-(6-Chloro-3-pyridazinyl)guanidine
  参考文献：
  名称：

  Selective urokinase-type plasminogen activator (uPA) inhibitors. Part 1: 2-Pyridinylguanidines

  摘要：

  The identification of 2-pyridinylguanidines (e.g. 27 and 28) as selective inhibitors of urokinase-type plasminogen activator (uPA) is described. The X-ray crystal structure of 27 has been determined, and modelling has been used to predict binding in the enzyme active site. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(01)00701-6

文献信息

• Selective urokinase-type plasminogen activator (uPA) inhibitors. Part 1: 2-Pyridinylguanidines
  作者：Christopher G Barber、Roger P Dickinson、Valerie A Horne

  DOI：10.1016/s0960-894x(01)00701-6

  日期：2002.1

  The identification of 2-pyridinylguanidines (e.g. 27 and 28) as selective inhibitors of urokinase-type plasminogen activator (uPA) is described. The X-ray crystal structure of 27 has been determined, and modelling has been used to predict binding in the enzyme active site. (C) 2002 Elsevier Science Ltd. All rights reserved.