1-(2-chlorophenyl)-3-[3-(trifluoromethyl)phenyl]urea | 91286-93-0

• 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-(2-chlorophenyl)-3-[3-(trifluoromethyl)phenyl]urea
• 英文别名: 1-(2-Chlorophenyl)-3-(alpha,alpha,alpha-trifluoro-M-tolyl)urea
• CAS: 91286-93-0
• 化学式: C₁₄H₁₀ClF₃N₂O
• 分子量: 314.694
• InChiKey: SUFULCJGYIVCAS-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4
• 重原子数：
  21
• 可旋转键数：
  2
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.07
• 拓扑面积：
  41.1
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  1-(2-chlorophenyl)-3-[3-(trifluoromethyl)phenyl]urea 、 3-氯-2-氯甲基丙烯 生成 1-(2-Chlorophenyl)-5-methylidene-3-[3-(trifluoromethyl)phenyl]-1,3-diazinan-2-one
  参考文献：
  名称：

  KNOPS, H. J.;HEINEMANN, U.;BABCZINSKI, P.;EUE, L.;SCHMIDT, R.

  摘要：

  DOI：
• 作为产物：
  描述：

  邻氯苯胺 、 3-(三氟甲基)异氰酸苯酯 在 三乙胺 作用下， 以 四氢呋喃 为溶剂， 反应 16.0h， 以50%的产率得到1-(2-chlorophenyl)-3-[3-(trifluoromethyl)phenyl]urea
  参考文献：
  名称：

  A Back-to-Front Fragment-Based Drug Design Search Strategy Targeting the DFG-Out Pocket of Protein Tyrosine Kinases

  摘要：

  We present a straightforward process for the discovery of novel back pocket-binding fragment molecules against protein tyrosine kinases. The approach begins by screening against the nonphosphorylated target kinase with subsequent counterscreening of hits against the phosphorylated enzyme. Back pocket-binding fragments are inactive against the phosphorylated kinase. Fragment molecules are of insufficient size to span both regions of the ATP binding pocket; thus, the outcome is binary (back pocket-binding or hinge-binding). Next, fragments with the appropriate binding profile are assayed in combination with a known hinge-binding fragment and subsequently with a known back pocket-binding fragment. Confirmation of back pocket-binding by Yonetani-Theorell plot analysis progresses candidate fragments to crystallization trials. The method is exemplified by a fragment screening campaign against vascular endothelial growth factor receptor 2, and a novel back pocket-binding fragment is presented.

  DOI：

  10.1021/ml3000403

文献信息

• Phosphate transport inhibitors
  申请人：Jozefiak H. Thomas

  公开号：US20070021509A1

  公开（公告）日：2007-01-25

  Disclosed are compounds which have been identified as inhibitors of phosphate transport. Many of the compounds are represented by Structural Formula (I): Ar 1 —W—X—Y—Ar 2 ; or a pharmaceutically acceptable salt thereof. Ar 1 and Ar 2 are independently a substituted or unsubstituted aryl group or an optionally substituted five membered or six membered non-aromatic heterocylic group fused to an optionally substituted monocylic aryl group. W and Y are independently a covalent bond or a C1-C3 substituted or unsubstituted alkylene group. X is a heteroatom-containing functional group, an aromatic heterocyclic group, substituted aromatic heterocyclic group, non-aromatic heterocyclic group, substituted non-aromatic heterocyclic group, an olefin group or a substituted olefin group. Also disclosed are methods of treating a subject with a disease associated with hyperphosphatemia, as well as a disease mediated by phosphate-transport function. The methods comprise the step of administering an effective amount of the one of the compounds described above.

  本发明涉及已被鉴定为磷酸盐转运抑制剂的化合物。其中许多化合物由结构式（I）表示：Ar1-W-X-Y-Ar2；或其药学上可接受的盐。其中，Ar1和Ar2独立地为取代或未取代的芳基团或可选取代的五元或六元非芳基杂环团与可选取代的单环芳基团融合。W和Y独立地为共价键或C1-C3取代或未取代的烷基链。X为含杂原子的官能团、芳基杂环团、取代的芳基杂环团、非芳基杂环团、取代的非芳基杂环团、烯烃基或取代的烯烃基。本发明还涉及治疗与高磷血症相关的疾病以及由磷酸盐转运功能介导的疾病的方法。该方法包括给予上述化合物之一的有效量。
• KNOPS, H. J.;HEINEMANN, U.;BABCZINSKI, P.;EUE, L.;SCHMIDT, R.
  作者：KNOPS, H. J.、HEINEMANN, U.、BABCZINSKI, P.、EUE, L.、SCHMIDT, R.

  DOI：——

  日期：——
• US4514210A
  申请人：——

  公开号：US4514210A

  公开（公告）日：1985-04-30
• A Back-to-Front Fragment-Based Drug Design Search Strategy Targeting the DFG-Out Pocket of Protein Tyrosine Kinases
  作者：Hidehisa Iwata、Hideyuki Oki、Kengo Okada、Terufumi Takagi、Michiko Tawada、Yasushi Miyazaki、Shinichi Imamura、Akira Hori、J. David Lawson、Mark S. Hixon、Hiroyuki Kimura、Hiroshi Miki

  DOI：10.1021/ml3000403

  日期：2012.4.12

  We present a straightforward process for the discovery of novel back pocket-binding fragment molecules against protein tyrosine kinases. The approach begins by screening against the nonphosphorylated target kinase with subsequent counterscreening of hits against the phosphorylated enzyme. Back pocket-binding fragments are inactive against the phosphorylated kinase. Fragment molecules are of insufficient size to span both regions of the ATP binding pocket; thus, the outcome is binary (back pocket-binding or hinge-binding). Next, fragments with the appropriate binding profile are assayed in combination with a known hinge-binding fragment and subsequently with a known back pocket-binding fragment. Confirmation of back pocket-binding by Yonetani-Theorell plot analysis progresses candidate fragments to crystallization trials. The method is exemplified by a fragment screening campaign against vascular endothelial growth factor receptor 2, and a novel back pocket-binding fragment is presented.