[5-Amino-1-(benzenesulfonyl)pyrazol-3-yl] thiophene-2-carboxylate

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: [5-Amino-1-(benzenesulfonyl)pyrazol-3-yl] thiophene-2-carboxylate
• 化学式: C₁₄H₁₁N₃O₄S₂
• 分子量: 349.391
• InChiKey: RZXMQAUOJUDTRO-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.4
• 重原子数：
  23
• 可旋转键数：
  5
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  141
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  cyanoacetyl-N-phenylsulfonylhydrazide 在 sodium hydroxide 、 三乙胺 作用下， 以 氯仿 为溶剂， 反应 2.5h， 生成 [5-Amino-1-(benzenesulfonyl)pyrazol-3-yl] thiophene-2-carboxylate
  参考文献：
  名称：

  Identification and characterization of 3-substituted pyrazolyl esters as alternate substrates for cathepsin B: The confounding effects of DTT and cysteine in biological assays

  摘要：

  Substituted pyrazole esters were identified as hits in a high hroughput screen (HTS) of the NIH Molecular Libraries Small Molecule Repository (MLSMR) to identify inhibitors of the enzyme cathepsin B. Members of this class, along with functional group analogs, were synthesized in an effort to define the structural requirements for activity. Analog characterization was hampered by the need to include a reducing agent such as dithiothreitol (DTT) or cysteine in the assay, highlighting the caution required in interpreting biological data gathered in the presence of such nucleophiles. Despite the confounding effects of DTT and cysteine, our studies demonstrate that the pyrazole I acts as alternate substrate for cathepsin B, rather than as an inhibitor. (c) 2007 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2007.06.091

文献信息

• Identification and characterization of 3-substituted pyrazolyl esters as alternate substrates for cathepsin B: The confounding effects of DTT and cysteine in biological assays
  作者：Michael C. Myers、Andrew D. Napper、Nuzhat Motlekar、Parag P. Shah、Chun-Hao Chiu、Mary Pat Beavers、Scott L. Diamond、Donna M. Huryn、Amos B. Smith

  DOI：10.1016/j.bmcl.2007.06.091

  日期：2007.9

  Substituted pyrazole esters were identified as hits in a high hroughput screen (HTS) of the NIH Molecular Libraries Small Molecule Repository (MLSMR) to identify inhibitors of the enzyme cathepsin B. Members of this class, along with functional group analogs, were synthesized in an effort to define the structural requirements for activity. Analog characterization was hampered by the need to include a reducing agent such as dithiothreitol (DTT) or cysteine in the assay, highlighting the caution required in interpreting biological data gathered in the presence of such nucleophiles. Despite the confounding effects of DTT and cysteine, our studies demonstrate that the pyrazole I acts as alternate substrate for cathepsin B, rather than as an inhibitor. (c) 2007 Elsevier Ltd. All rights reserved.