N-methyl-N-[[4-(trifluoromethylsulfanyl)phenyl]methyl]carbamoyl chloride | 211619-45-3

• 分子结构分类: 有机化合物 - 有机硫化合物 - 硫醚类
• 英文名称: N-methyl-N-[[4-(trifluoromethylsulfanyl)phenyl]methyl]carbamoyl chloride
• CAS: 211619-45-3
• 化学式: C₁₀H₉ClF₃NOS
• 分子量: 283.702
• InChiKey: FXLRMSHAFIDPGL-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4
• 重原子数：
  17
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  45.6
• 氢给体数：
  0
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  N-methyl-N-[[4-(trifluoromethylsulfanyl)phenyl]methyl]carbamoyl chloride 在 Oxone 、 双(三甲基硅烷基)氨基钾 作用下， 以 甲醇 、 水 、 丙酮 为溶剂， 反应 2.33h， 生成 (S)-2-Benzyl-4-oxo-azetidine-1-carboxylic acid methyl-(4-trifluoromethanesulfinyl-benzyl)-amide
  参考文献：
  名称：

  β-Lactam Derivatives as Inhibitors of Human Cytomegalovirus Protease

  摘要：

  The development of novel monobactam inhibitors of HCMV protease incorporating a carbon side chain at C-4 and a urea function at N-1 is described. Substitution with small groups at the C-3 position of the beta-lactam ring gave an increase in enzymatic activity and in stability; however, a lack of selectivity against other serine proteases was noted. The use of both tri- and tetrasubstituted urea functionalities gave effective inhibitors of HCMV protease. Benzyl substitution of the urea moiety was beneficial, especially when strong electron-withdrawing groups where attached at the para position. Modest antiviral activity was found in a plaque reduction assay.

  DOI：

  10.1021/jm980131z
• 作为产物：
  描述：

  光气 、 Methyl({4-[(trifluoromethyl)sulfanyl]phenyl}methyl)amine hydrochloride 在 N,N-二异丙基乙胺 作用下， 以 二氯甲烷 、 甲苯 为溶剂， 反应 2.0h， 生成 N-methyl-N-[[4-(trifluoromethylsulfanyl)phenyl]methyl]carbamoyl chloride
  参考文献：
  名称：

  β-Lactam Derivatives as Inhibitors of Human Cytomegalovirus Protease

  摘要：

  The development of novel monobactam inhibitors of HCMV protease incorporating a carbon side chain at C-4 and a urea function at N-1 is described. Substitution with small groups at the C-3 position of the beta-lactam ring gave an increase in enzymatic activity and in stability; however, a lack of selectivity against other serine proteases was noted. The use of both tri- and tetrasubstituted urea functionalities gave effective inhibitors of HCMV protease. Benzyl substitution of the urea moiety was beneficial, especially when strong electron-withdrawing groups where attached at the para position. Modest antiviral activity was found in a plaque reduction assay.

  DOI：

  10.1021/jm980131z

文献信息

• β-Lactam Derivatives as Inhibitors of Human Cytomegalovirus Protease
  作者：Christiane Yoakim、William W. Ogilvie、Dale R. Cameron、Catherine Chabot、Ingrid Guse、Bruno Haché、Julie Naud、Jeff A. O'Meara、Raymond Plante、Robert Déziel

  DOI：10.1021/jm980131z

  日期：1998.7.1

  The development of novel monobactam inhibitors of HCMV protease incorporating a carbon side chain at C-4 and a urea function at N-1 is described. Substitution with small groups at the C-3 position of the beta-lactam ring gave an increase in enzymatic activity and in stability; however, a lack of selectivity against other serine proteases was noted. The use of both tri- and tetrasubstituted urea functionalities gave effective inhibitors of HCMV protease. Benzyl substitution of the urea moiety was beneficial, especially when strong electron-withdrawing groups where attached at the para position. Modest antiviral activity was found in a plaque reduction assay.