1-bromo-3-isothiocyanato-5-(trifluoromethyl)benzene | 955947-86-1

• 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: 1-bromo-3-isothiocyanato-5-(trifluoromethyl)benzene
• 英文别名: 3-Bromo-5-(trifluoromethyl)phenylisothiocyanate
• CAS: 955947-86-1
• 化学式: C₈H₃BrF₃NS
• 分子量: 282.084
• InChiKey: PYUHPMXARCWIAW-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.9
• 重原子数：
  14
• 可旋转键数：
  1
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.12
• 拓扑面积：
  44.4
• 氢给体数：
  0
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  1-bromo-3-isothiocyanato-5-(trifluoromethyl)benzene 在 氢氧化钾 、 溴 作用下， 以 乙酸乙酯 、 N,N-二甲基甲酰胺 为溶剂， 反应 2.5h， 生成 5-[3-Bromo-5-(trifluoromethyl)anilino]-3-oxo-isothiazole-4-carbonitrile
  参考文献：
  名称：

  Isothiazoles as active-site inhibitors of HCV NS5B polymerase

  摘要：

  Isothiazole analogs were discovered as a novel class of active-site inhibitors of HCV NS5B polymerase. The best compound has an IC(50) of 200 nM and EC(50) of 100 nM, which is a significant improvement over the starting inhibitor (1). The X-ray complex structure of 1 with HCV NS5B was obtained at a resolution of 2.2A, revealing that the inhibitor is covalently linked with Cys 366 of the 'primer-grip'. Furthermore, it makes considerable contacts with the C-terminus, beta-loop, and more importantly, to the active-site of the enzyme. The uniqueness of this binding mode offers a new insight for the rational design of novel inhibitors for HCV NS5B polymerase.

  DOI：

  10.1016/j.bmcl.2006.10.002
• 作为产物：
  描述：

  3-氨基-5-溴三氟甲苯 在 三乙烯二胺 、 三光气 作用下， 以 二氯甲烷 、 甲苯 为溶剂， 反应 10.0h， 生成 1-bromo-3-isothiocyanato-5-(trifluoromethyl)benzene
  参考文献：
  名称：

  一种具有抗肿瘤活性的二芳基硫脲化合物及其制备方法和应用

  摘要：

  本发明提供了一种具有抗肿瘤活性的二芳基硫脲化合物及其制备方法和应用，该化合物的结构式为其中R1、R2为卤素基团，或者R1、R2共同形成Ar为吡啶、吲唑或喹唑啉的含氮杂环。该化合物对VEGFR‑2激酶有很好的抑制活性，能够通过抑制VEGFR‑2激酶的活性，阻断其诱导的信号通路，抑制肿瘤细胞的增生和迁移，从而可应用于抗肿瘤药物的制备。且该化合物的制备方法具有原料易得，反应条件温和，反应过程操作简单，所用试剂便宜的优点。

  公开号：

  CN105924385A

文献信息

• 一种具有抗肿瘤活性的二芳基硫脲化合物及其制备方法和应用
  申请人：西安交通大学

  公开号：CN105924385A

  公开（公告）日：2016-09-07

  本发明提供了一种具有抗肿瘤活性的二芳基硫脲化合物及其制备方法和应用，该化合物的结构式为其中R1、R2为卤素基团，或者R1、R2共同形成Ar为吡啶、吲唑或喹唑啉的含氮杂环。该化合物对VEGFR‑2激酶有很好的抑制活性，能够通过抑制VEGFR‑2激酶的活性，阻断其诱导的信号通路，抑制肿瘤细胞的增生和迁移，从而可应用于抗肿瘤药物的制备。且该化合物的制备方法具有原料易得，反应条件温和，反应过程操作简单，所用试剂便宜的优点。
• 10.1016/j.apcata.2024.119806
  作者：Selvaraj, Ramaraj、G, Govinda Rajulu、Arunachalam, Rajendran、Subramanian, Palani S.、Savitha Lakshmi、Mahalakshmi、Suresh, Eringathodi、Ganesh, Krithika、Rajeshwaran, Kasi、Karthik、S, Sandeep

  DOI：10.1016/j.apcata.2024.119806

  日期：——
• Discovery of novel anti-angiogenesis agents. Part 6: Multi-targeted RTK inhibitors
  作者：Lin Zhang、Yuanyuan Shan、Chuansheng Li、Ying Sun、Ping Su、Jinfeng Wang、Lisha Li、Xiaoyan Pan、Jie Zhang

  DOI：10.1016/j.ejmech.2016.12.059

  日期：2017.2

  Angiogenesis is modulated by a multitude of pro-angiogenic factors including VEGFR-2, Tie-2, and EphB4. Moreover, their crosstalk also had been well elaborated. We have identified several diarylureabased VEGFR-2 inhibitors as potential anti-angiogenesis agents. As a continuation to our previous research, two series of diaryl malonamide and diaryl thiourea derivatives have been developed as multiplex VEGFR-2/Tie-2/EphB4 inhibitors. Interestingly, the biological evaluation indicated that several compounds bearing trifluoromethyl or trifluoromethoxyl exhibited promising multiplex inhibition against angiogenesis-related VEGFR-2, Tie-2, and EphB4. The representative compound (18a) displayed both potent multi-targeted RTK inhibition and considerable antiproliferative activities against human umbilical vein endothelial cells (EA.hy926). These results will contribute to the discovery of novel mutitargeted anti-angiogenesis agents. (C) 2017 Elsevier Masson SAS. All rights reserved.
• Isothiazoles as active-site inhibitors of HCV NS5B polymerase
  作者：Shunqi Yan、Todd Appleby、Esmir Gunic、Jae Hoon Shim、Tania Tasu、Hongwoo Kim、Frank Rong、Huaming Chen、Robert Hamatake、Jim Z. Wu、Zhi Hong、Nanhua Yao

  DOI：10.1016/j.bmcl.2006.10.002

  日期：2007.1

  Isothiazole analogs were discovered as a novel class of active-site inhibitors of HCV NS5B polymerase. The best compound has an IC(50) of 200 nM and EC(50) of 100 nM, which is a significant improvement over the starting inhibitor (1). The X-ray complex structure of 1 with HCV NS5B was obtained at a resolution of 2.2A, revealing that the inhibitor is covalently linked with Cys 366 of the 'primer-grip'. Furthermore, it makes considerable contacts with the C-terminus, beta-loop, and more importantly, to the active-site of the enzyme. The uniqueness of this binding mode offers a new insight for the rational design of novel inhibitors for HCV NS5B polymerase.