2-Fluoro-4-isothiocyanato-1-methoxybenzene | 344750-44-3

• 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: 2-Fluoro-4-isothiocyanato-1-methoxybenzene
• CAS: 344750-44-3
• 化学式: C₈H₆FNOS
• 分子量: 183.206
• InChiKey: VQKFGMVWRAHVCT-UHFFFAOYSA-N

物化性质

• 沸点：
  285.6±25.0 °C(Predicted)
• 密度：
  1.18±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.4
• 重原子数：
  12
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.12
• 拓扑面积：
  53.7
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  ethyl 3-amino-4-((2-(trifluoromethyl)benzyl)amino)benzoate 、 2-Fluoro-4-isothiocyanato-1-methoxybenzene 以 N,N-二甲基甲酰胺 为溶剂， 反应 1.0h， 以63%的产率得到
  参考文献：
  名称：

  Structural Insights into a Unique Inhibitor Binding Pocket in Kinesin Spindle Protein

  摘要：

  Human kinesin Eg5 is a target for drug development in cancer chemotherapy with compounds in phase II clinical trials. These agents bind to a well-characterized allosteric pocket involving the loop L5 region, a structural element in kinesin-5 family members thought to provide inhibitor specificity. Using X-ray crystallography, kinetic, and biophysical methods, we have identified and characterized a distinct allosteric pocket in Eg5 able to bind inhibitors with nanomolar K-d. This pocket is formed by key structural elements thought to be pivotal for force generation in kinesins and may represent a novel site for therapeutic intervention in this increasingly well-validated drug target.

  DOI：

  10.1021/ja310377d
• 作为产物：
  描述：

  硫光气 、 3-氟-4-甲氧基苯胺 在 碳酸氢钠 作用下， 以 氯仿 、 水 为溶剂， 反应 2.0h， 以79%的产率得到2-Fluoro-4-isothiocyanato-1-methoxybenzene
  参考文献：
  名称：

  Structural Insights into a Unique Inhibitor Binding Pocket in Kinesin Spindle Protein

  摘要：

  Human kinesin Eg5 is a target for drug development in cancer chemotherapy with compounds in phase II clinical trials. These agents bind to a well-characterized allosteric pocket involving the loop L5 region, a structural element in kinesin-5 family members thought to provide inhibitor specificity. Using X-ray crystallography, kinetic, and biophysical methods, we have identified and characterized a distinct allosteric pocket in Eg5 able to bind inhibitors with nanomolar K-d. This pocket is formed by key structural elements thought to be pivotal for force generation in kinesins and may represent a novel site for therapeutic intervention in this increasingly well-validated drug target.

  DOI：

  10.1021/ja310377d

文献信息

• CAMPAIGNE, E.;KIM, CHUNG, S., J. HETEROCYCL. CHEM., 1983, 20, N 6, 1697-1703
  作者：CAMPAIGNE, E.、KIM, CHUNG, S.

  DOI：——

  日期：——
• Structural Insights into a Unique Inhibitor Binding Pocket in Kinesin Spindle Protein
  作者：Venkatasubramanian Ulaganathan、Sandeep K. Talapatra、Oliver Rath、Andrew Pannifer、David D. Hackney、Frank Kozielski

  DOI：10.1021/ja310377d

  日期：2013.2.13

  Human kinesin Eg5 is a target for drug development in cancer chemotherapy with compounds in phase II clinical trials. These agents bind to a well-characterized allosteric pocket involving the loop L5 region, a structural element in kinesin-5 family members thought to provide inhibitor specificity. Using X-ray crystallography, kinetic, and biophysical methods, we have identified and characterized a distinct allosteric pocket in Eg5 able to bind inhibitors with nanomolar K-d. This pocket is formed by key structural elements thought to be pivotal for force generation in kinesins and may represent a novel site for therapeutic intervention in this increasingly well-validated drug target.