N-甲基-4-氯苄胺盐酸盐 | 65542-24-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 中文名称: N-甲基-4-氯苄胺盐酸盐
• 中文别名: 4-氯-N-甲基苯甲胺盐酸盐
• 英文名称: (4-chloro-benzyl)-methyl-amine; hydrochloride
• 英文别名: (4-Chlor-benzyl)-methyl-amin; Hydrochlorid；(4-Chlorophenyl)methyl-methylazanium;chloride
• CAS: 65542-24-7
• 化学式: C₈H₁₀ClN*ClH
• 分子量: 192.088
• InChiKey: APSVTQIASNIYIM-UHFFFAOYSA-N

物化性质

• 熔点：
  194-195 °C

计算性质

• 辛醇/水分配系数(LogP)：
  2.48
• 重原子数：
  11
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  12
• 氢给体数：
  2
• 氢受体数：
  1

安全信息

• 海关编码：
  2921499090
• 危险性防范说明：
  P261,P305+P351+P338
• 危险性描述：
  H302,H315,H319,H335

反应信息

• 作为反应物：
  描述：

  N-甲基-4-氯苄胺盐酸盐 在 双(三甲基硅烷基)氨基钾 、 N,N-二异丙基乙胺 作用下， 以 二氯甲烷 、 甲苯 为溶剂， 反应 4.33h， 生成 (S)-2-Benzyl-4-oxo-azetidine-1-carboxylic acid (4-chloro-benzyl)-methyl-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

文献信息

• Vicarini; Carmellino; Borgna, Farmaco, Edizione Scientifica, 1982, vol. 37, # 9, p. 627 - 632
  作者：Vicarini、Carmellino、Borgna

  DOI：——

  日期：——
• 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.