2'-(5-fluoro-2-pyridyl)-6-benzo[b]thiophenecarbonitrile | 1207731-37-0

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并噻吩类
• 英文名称: 2'-(5-fluoro-2-pyridyl)-6-benzo[b]thiophenecarbonitrile
• 英文别名: 2-(5-Fluoropyridin-2-yl)-1-benzothiophene-6-carbonitrile
• CAS: 1207731-37-0
• 化学式: C₁₄H₇FN₂S
• 分子量: 254.287
• InChiKey: OXHSBURIMXJUTP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.4
• 重原子数：
  18
• 可旋转键数：
  1
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  64.9
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  2'-(5-fluoro-2-pyridyl)-6-benzo[b]thiophenecarbonitrile 在 硫酸 、 三氟乙酸 、 水 作用下， 以 正己烷 、 二氯甲烷 为溶剂， 反应 24.0h， 以92%的产率得到2'-(5-fluoro-2-pyridyl)-6-benzo[b]thiophenecarboxamide
  参考文献：
  名称：

  Synthesis and Biological Evaluation of Botulinum Neurotoxin A Protease Inhibitors

  摘要：

  NSC 240898 was previously identified as a botulinum neurotoxin A light chain (BoNT/A LC) endopeptidase inhibitor by screening the National Cancer Institute Open Repository diversity set. Two types of analogues have been synthesized and shown to inhibit BoNT/A LC in a FRET-based enzyme assay, with confirmation in an HPLC-based assay. These two series of compounds have also been evaluated for inhibition of anthrax lethal factor (LF), an unrelated metalloprotease, to examine enzyme specificity of the BoNT/A LC inhibition. The most potent inhibitor against BoNT/A LC in these two series is compound 12 (IC50 = 2.5 mu M, FRET assay), which is 4.4-fold more potent than the lead structure and 11.2-fold more selective for BoNT/A LC versus the anthrax LF metalloproteinase. Structure-activity relationship studies have revealed structural features important to potency and enzyme specificity.

  DOI：

  10.1021/jm901852f
• 作为产物：
  描述：

  2-溴-5-氟吡啶 、 6-氰基苯并[b]噻吩-2-基硼酸 在 四(三苯基膦)钯 、 sodium carbonate 作用下， 以 乙醇 、 水 、 甲苯 为溶剂， 生成 2'-(5-fluoro-2-pyridyl)-6-benzo[b]thiophenecarbonitrile
  参考文献：
  名称：

  Synthesis and Biological Evaluation of Botulinum Neurotoxin A Protease Inhibitors

  摘要：

  NSC 240898 was previously identified as a botulinum neurotoxin A light chain (BoNT/A LC) endopeptidase inhibitor by screening the National Cancer Institute Open Repository diversity set. Two types of analogues have been synthesized and shown to inhibit BoNT/A LC in a FRET-based enzyme assay, with confirmation in an HPLC-based assay. These two series of compounds have also been evaluated for inhibition of anthrax lethal factor (LF), an unrelated metalloprotease, to examine enzyme specificity of the BoNT/A LC inhibition. The most potent inhibitor against BoNT/A LC in these two series is compound 12 (IC50 = 2.5 mu M, FRET assay), which is 4.4-fold more potent than the lead structure and 11.2-fold more selective for BoNT/A LC versus the anthrax LF metalloproteinase. Structure-activity relationship studies have revealed structural features important to potency and enzyme specificity.

  DOI：

  10.1021/jm901852f