5-(3-Methyl-butoxy)-1-phenyl-1H-pyrazole-4-carboxylic acid | 706819-86-5

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 唑类
• 英文名称: 5-(3-Methyl-butoxy)-1-phenyl-1H-pyrazole-4-carboxylic acid
• 英文别名: 5-(3-Methylbutoxy)-1-phenylpyrazole-4-carboxylic acid
• CAS: 706819-86-5
• 化学式: C₁₅H₁₈N₂O₃
• 分子量: 274.32
• InChiKey: QLJJTNAZETUXJD-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.4
• 重原子数：
  20
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  64.4
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  5-(3-Methyl-butoxy)-1-phenyl-1H-pyrazole-4-carboxylic acid 在 草酰氯 、 N,N-二甲基甲酰胺 作用下， 以 二氯甲烷 、 丙酮 为溶剂， 反应 9.0h， 生成 4-{4-[5-(3-Methyl-butoxy)-1-phenyl-1H-pyrazol-4-yl]-thiazol-2-yl}-5-methylsulfanyl-thiophene-2-carboxylic acid methyl ester
  参考文献：
  名称：

  A novel series of potent and selective small molecule inhibitors of the complement component C1s

  摘要：

  Activation of the classical pathway of complement has been implicated in disease states such as hereditary angioedema, ischemia-reperfusion injury and acute transplant rejection. The trypsin-like serine protease C1s represents a pivotal upstream point of control in the classical pathway of complement activation and is therefore likely to be a useful target in the therapeutic intervention of these disease states. A series of thiopheneamidine-based inhibitors of C1s has been optimized to give a 70 nM inhibitor that inhibits the classical pathway of complement activation in vitro. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2004.04.034
• 作为产物：
  描述：

  3-oxo-2-phenyl-2,3-dihydro-1H-pyrazole-4-carboxylic acid ethyl ester 在 sodium hydroxide 、 三苯基膦 、 偶氮二甲酸二乙酯 作用下， 以 四氢呋喃 、 甲醇 为溶剂， 反应 4.0h， 生成 5-(3-Methyl-butoxy)-1-phenyl-1H-pyrazole-4-carboxylic acid
  参考文献：
  名称：

  A novel series of potent and selective small molecule inhibitors of the complement component C1s

  摘要：

  Activation of the classical pathway of complement has been implicated in disease states such as hereditary angioedema, ischemia-reperfusion injury and acute transplant rejection. The trypsin-like serine protease C1s represents a pivotal upstream point of control in the classical pathway of complement activation and is therefore likely to be a useful target in the therapeutic intervention of these disease states. A series of thiopheneamidine-based inhibitors of C1s has been optimized to give a 70 nM inhibitor that inhibits the classical pathway of complement activation in vitro. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2004.04.034

文献信息

• A novel series of potent and selective small molecule inhibitors of the complement component C1s
  作者：Nalin L. Subasinghe、Farah Ali、Carl R. Illig、M. Jonathan Rudolph、Scott Klein、Ehab Khalil、Richard M. Soll、Roger F. Bone、John C. Spurlino、Renee L. DesJarlais、Carl S. Crysler、Maxwell D. Cummings、Philip E. Morris、John M. Kilpatrick、Y. Sudhakara Babu

  DOI：10.1016/j.bmcl.2004.04.034

  日期：2004.6

  Activation of the classical pathway of complement has been implicated in disease states such as hereditary angioedema, ischemia-reperfusion injury and acute transplant rejection. The trypsin-like serine protease C1s represents a pivotal upstream point of control in the classical pathway of complement activation and is therefore likely to be a useful target in the therapeutic intervention of these disease states. A series of thiopheneamidine-based inhibitors of C1s has been optimized to give a 70 nM inhibitor that inhibits the classical pathway of complement activation in vitro. (C) 2004 Elsevier Ltd. All rights reserved.