N-(1-naphthylmethyl)-3-nitrobenzenesulfonamide | 303780-50-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: N-(1-naphthylmethyl)-3-nitrobenzenesulfonamide
• 英文别名: N-(naphthalen-1-ylmethyl)-3-nitrobenzenesulfonamide
• CAS: 303780-50-9
• 化学式: C₁₇H₁₄N₂O₄S
• 分子量: 342.375
• InChiKey: QEKJEMSQESKCBI-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.5
• 重原子数：
  24
• 可旋转键数：
  4
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.06
• 拓扑面积：
  100
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  N-(1-naphthylmethyl)-3-nitrobenzenesulfonamide 在 tin(ll) chloride 作用下， 以 乙酸乙酯 为溶剂， 反应 2.0h， 以86%的产率得到3-amino-N-(1-naphthylmethyl)benzenesulfonamide
  参考文献：
  名称：

  Design, synthesis and early structure–activity relationship of farnesyltransferase inhibitors which mimic both the peptidic and the prenylic substrate

  摘要：

  Inhibition of the farnesylation of ras proteins has been identified as a promising target in tumor therapy. Only a few farnesyltransferase inhibitors are bisubstrate analogues displaying features of both substrates, the farnesylpyrophosphate and the C-terminal CAAX-tetrapeptide sequence of the res protein. These known bisubstrate analogues consist of an AAX-tripeptide and a farnesyl residue connected through various linkers. We have developed a class of novel compounds that mimic a bisubstrate inhibitor structure and that differ from the known ones by lacking peptidic or farnesylic substructures. Long chain fatty acids and aryl-substituted carboxylic acids were used as farnesyl surrogates. These structures were linked to isoleucine amide, benzoic acid amide, N-substituted aminobenzenesulfonamides and N-alpha-aryl-substituted methionine derivatives, respectively, which function as AA- or AAX-mimetics. (C) 2000 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(00)00138-3
• 作为产物：
  描述：

  1-萘甲基胺 、 3-硝基苯磺酰氯 在 N-甲基吗啉 作用下， 以 二氯甲烷 为溶剂， 以64%的产率得到N-(1-naphthylmethyl)-3-nitrobenzenesulfonamide
  参考文献：
  名称：

  Design, synthesis and early structure–activity relationship of farnesyltransferase inhibitors which mimic both the peptidic and the prenylic substrate

  摘要：

  Inhibition of the farnesylation of ras proteins has been identified as a promising target in tumor therapy. Only a few farnesyltransferase inhibitors are bisubstrate analogues displaying features of both substrates, the farnesylpyrophosphate and the C-terminal CAAX-tetrapeptide sequence of the res protein. These known bisubstrate analogues consist of an AAX-tripeptide and a farnesyl residue connected through various linkers. We have developed a class of novel compounds that mimic a bisubstrate inhibitor structure and that differ from the known ones by lacking peptidic or farnesylic substructures. Long chain fatty acids and aryl-substituted carboxylic acids were used as farnesyl surrogates. These structures were linked to isoleucine amide, benzoic acid amide, N-substituted aminobenzenesulfonamides and N-alpha-aryl-substituted methionine derivatives, respectively, which function as AA- or AAX-mimetics. (C) 2000 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(00)00138-3

文献信息

• Design, synthesis and early structure–activity relationship of farnesyltransferase inhibitors which mimic both the peptidic and the prenylic substrate
  作者：Martin Schlitzer、Markus Böhm、Isabel Sattler、Hans-Martin Dahse

  DOI：10.1016/s0968-0896(00)00138-3

  日期：2000.8

  Inhibition of the farnesylation of ras proteins has been identified as a promising target in tumor therapy. Only a few farnesyltransferase inhibitors are bisubstrate analogues displaying features of both substrates, the farnesylpyrophosphate and the C-terminal CAAX-tetrapeptide sequence of the res protein. These known bisubstrate analogues consist of an AAX-tripeptide and a farnesyl residue connected through various linkers. We have developed a class of novel compounds that mimic a bisubstrate inhibitor structure and that differ from the known ones by lacking peptidic or farnesylic substructures. Long chain fatty acids and aryl-substituted carboxylic acids were used as farnesyl surrogates. These structures were linked to isoleucine amide, benzoic acid amide, N-substituted aminobenzenesulfonamides and N-alpha-aryl-substituted methionine derivatives, respectively, which function as AA- or AAX-mimetics. (C) 2000 Elsevier Science Ltd. All rights reserved.