5-amino-3-(3-amino-1H-indazol-6-yl)-1-tert-butylpyrazole-4-carboxamide | 1493523-62-8

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并吡唑类
• 英文名称: 5-amino-3-(3-amino-1H-indazol-6-yl)-1-tert-butylpyrazole-4-carboxamide
• CAS: 1493523-62-8
• 化学式: C₁₅H₁₉N₇O
• 分子量: 313.362
• InChiKey: JWPDIUTUSKBAGX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.1
• 重原子数：
  23
• 可旋转键数：
  3
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  142
• 氢给体数：
  4
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  2-氟-4-甲酰基苯甲腈 在 N-溴代丁二酰亚胺(NBS) 、 sodium ethanolate 、 一水合肼 、 N,N-二异丙基乙胺 作用下， 以 乙醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 2.67h， 生成 5-amino-3-(3-amino-1H-indazol-6-yl)-1-tert-butylpyrazole-4-carboxamide
  参考文献：
  名称：

  Potent and Selective Inhibitors of CDPK1 from T. gondii and C. parvum Based on a 5-Aminopyrazole-4-carboxamide Scaffold

  摘要：

  5-Aminopyrazole-4-carboxamide was used as an alternative scaffold to substitute for the pyrazolopyrimidine of a known "bumped kinase inhibitor" to create selective inhibitors of calcium-dependent protein kinase-1 from both Toxoplasma gondii and Cryptosporidium parvum. Compounds with low nanomolar inhibitory potencies against the target enzymes were obtained. The most selective inhibitors also exhibited submicromolar activities in T. gondii cell proliferation assays and were shown to be non-toxic to mammalian cells.

  DOI：

  10.1021/ml400315s

文献信息

• Potent and Selective Inhibitors of CDPK1 from <i>T. gondii</i> and <i>C. parvum</i> Based on a 5-Aminopyrazole-4-carboxamide Scaffold
  作者：Zhongsheng Zhang、Kayode K. Ojo、RamaSubbaRao Vidadala、Wenlin Huang、Jennifer A. Geiger、Suzanne Scheele、Ryan Choi、Molly C. Reid、Katelyn R. Keyloun、Kasey Rivas、Latha Kallur Siddaramaiah、Kenneth M. Comess、Kenneth P. Robinson、Philip J. Merta、Lemma Kifle、Wim G. J. Hol、Marilyn Parsons、Ethan A. Merritt、Dustin J. Maly、Christophe L. M. J. Verlinde、Wesley C. Van Voorhis、Erkang Fan

  DOI：10.1021/ml400315s

  日期：2014.1.9

  5-Aminopyrazole-4-carboxamide was used as an alternative scaffold to substitute for the pyrazolopyrimidine of a known "bumped kinase inhibitor" to create selective inhibitors of calcium-dependent protein kinase-1 from both Toxoplasma gondii and Cryptosporidium parvum. Compounds with low nanomolar inhibitory potencies against the target enzymes were obtained. The most selective inhibitors also exhibited submicromolar activities in T. gondii cell proliferation assays and were shown to be non-toxic to mammalian cells.