N-naphthalen-1-yl-2-[3-(trifluoromethyl)phenyl]acetamide | 360772-94-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: N-naphthalen-1-yl-2-[3-(trifluoromethyl)phenyl]acetamide
• CAS: 360772-94-7
• 化学式: C₁₉H₁₄F₃NO
• 分子量: 329.321
• InChiKey: MVULTMYMJOFXFE-UHFFFAOYSA-N

物化性质

• 沸点：
  500.0±50.0 °C(Predicted)
• 密度：
  1.312±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.8
• 重原子数：
  24
• 可旋转键数：
  3
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.11
• 拓扑面积：
  29.1
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  N-naphthalen-1-yl-2-[3-(trifluoromethyl)phenyl]acetamide 在 dimethyl sulfide borane 作用下， 以94%的产率得到N-[2-[3-(trifluoromethyl)phenyl]ethyl]naphthalen-1-amine
  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：

  间三氟甲基苯乙酸 在 草酰氯 、 N,N-二甲基甲酰胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 N-naphthalen-1-yl-2-[3-(trifluoromethyl)phenyl]acetamide
  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

文献信息

• Identification of novel potent hydroxamic acid inhibitors of peptidyl deformylase and the importance of the hydroxamic acid functionality on inhibition
  作者：Atli Thorarensen、Martin R. Douglas, Jr.、Douglas C. Rohrer、Anne F. Vosters、Anthony W. Yem、Vincent D. Marshall、Janet C. Lynn、Michael J. Bohanon、Paul K. Tomich、Gary E. Zurenko、Michael T. Sweeney、Randy M. Jensen、James W. Nielsen、Eric P. Seest、Lester A. Dolak

  DOI：10.1016/s0960-894x(01)00242-6

  日期：2001.6

  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.