Naphthalen-1-yl-(3-trifluoromethyl-benzylamino)-acetonitrile | 360772-89-0

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: Naphthalen-1-yl-(3-trifluoromethyl-benzylamino)-acetonitrile
• CAS: 360772-89-0
• 化学式: C₂₀H₁₅F₃N₂
• 分子量: 340.348
• InChiKey: GVVCWBQVHWUZPC-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.21
• 重原子数：
  25.0
• 可旋转键数：
  4.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.15
• 拓扑面积：
  35.82
• 氢给体数：
  1.0
• 氢受体数：
  2.0

反应信息

• 作为反应物：
  描述：

  Naphthalen-1-yl-(3-trifluoromethyl-benzylamino)-acetonitrile 在 sodium hydroxide 、 双氧水 作用下， 生成 Naphthalen-1-yl-(3-trifluoromethyl-benzylamino)-acetic acid
  参考文献：
  名称：

  Identification of novel potent hydroxamic acid inhibitors of peptidyl deformylase and the importance of the hydroxamic acid functionality on inhibition

  摘要：

  Peptidyl deformylase (PDF) is a metallo protease that catalyzes the removal of a formyl group from the N-termini of prokaryotic prepared polypeptides, an essential step in bacterial protein synthesis. Screening of our compound collection using Staphylococcus aureus PDF afforded a very potent inhibitor with an IC50 in the low nanomolar range. Unfortunately, the compound that contains a hydroxamic acid did not exhibit antibacterial activity (MIC). In order to address the lack of activity in the MIC assay and to determine what portion of the molecule was responsible for binding to PDF, we prepared several analogues. This paper describes our findings that the hydroxamic acid functionality found in 1 is mainly responsible for the high affinity to PDF. In addition, we identified an alternative class of PDF inhibitors, the N-hydroxy urea 18, which has both PDF and antibacterial activity. (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(01)00242-6
• 作为产物：
  描述：

  3-(三氟甲基)苯甲胺 、 氰化钠 、 1-萘甲醛 在 盐酸 作用下， 以44%的产率得到Naphthalen-1-yl-(3-trifluoromethyl-benzylamino)-acetonitrile
  参考文献：
  名称：

  Identification of novel potent hydroxamic acid inhibitors of peptidyl deformylase and the importance of the hydroxamic acid functionality on inhibition

  摘要：

  Peptidyl deformylase (PDF) is a metallo protease that catalyzes the removal of a formyl group from the N-termini of prokaryotic prepared polypeptides, an essential step in bacterial protein synthesis. Screening of our compound collection using Staphylococcus aureus PDF afforded a very potent inhibitor with an IC50 in the low nanomolar range. Unfortunately, the compound that contains a hydroxamic acid did not exhibit antibacterial activity (MIC). In order to address the lack of activity in the MIC assay and to determine what portion of the molecule was responsible for binding to PDF, we prepared several analogues. This paper describes our findings that the hydroxamic acid functionality found in 1 is mainly responsible for the high affinity to PDF. In addition, we identified an alternative class of PDF inhibitors, the N-hydroxy urea 18, which has both PDF and antibacterial activity. (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(01)00242-6