4-(4-(sulfamoylamino)phenylsulfonamido)-benzoic acid | 1387556-05-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 4-(4-(sulfamoylamino)phenylsulfonamido)-benzoic acid
• 英文别名: 4-[[4-(Sulfamoylamino)phenyl]sulfonylamino]benzoic acid；4-[[4-(sulfamoylamino)phenyl]sulfonylamino]benzoic acid
• CAS: 1387556-05-9
• 化学式: C₁₃H₁₃N₃O₆S₂
• 分子量: 371.395
• InChiKey: MBKXCEVYDOUJPV-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.6
• 重原子数：
  24
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  172
• 氢给体数：
  4
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  4-(4-(sulfamoylamino)phenylsulfonamido)-benzoic acid 、 4-(2-氨乙基)苯磺酰胺 在 4-二甲氨基吡啶 、 N,N'-二环己基碳二亚胺 作用下， 以 乙腈 为溶剂， 以45%的产率得到4-(4-(sulfamoylamino)phenylsulfonamido)-N-(4-sulfamoyl-phenethyl)benzamide
  参考文献：
  名称：

  Development of Potent Carbonic Anhydrase Inhibitors Incorporating Both Sulfonamide and Sulfamide Groups

  摘要：

  A series of compounds incorporating both sulfonamide and sulfamide as zinc-binding groups (ZBGs) are reported as inhibitors of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1). Crystallographic studies on the complex of hCA II with the lead compound of this series, namely, 4-sulfamido-benzenesulfonamide, revealed the binding of two molecules in the enzyme active site cavity, the first one canonically coordinated to the zinc ion by means of the sulfonamide group and the second one located at the entrance of the cavity. This observation led to the design of elongated molecules incorporating these two ZBGs, separated by a linker of proper length, to allow the simultaneous binding to these different sites. The "long" inhibitors indeed showed around 10 times better enzyme inhibitory properties as compared to the shorter molecules against four physiologically relevant human (h) isoforms, hCA I, II, IX, and XII.

  DOI：

  10.1021/jm300818k
• 作为产物：
  描述：

  4-磺胺酰胺基苯甲酸 在 氨基磺酰氯 作用下， 以 N,N-二甲基乙酰胺 为溶剂， 以56%的产率得到4-(4-(sulfamoylamino)phenylsulfonamido)-benzoic acid
  参考文献：
  名称：

  Development of Potent Carbonic Anhydrase Inhibitors Incorporating Both Sulfonamide and Sulfamide Groups

  摘要：

  A series of compounds incorporating both sulfonamide and sulfamide as zinc-binding groups (ZBGs) are reported as inhibitors of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1). Crystallographic studies on the complex of hCA II with the lead compound of this series, namely, 4-sulfamido-benzenesulfonamide, revealed the binding of two molecules in the enzyme active site cavity, the first one canonically coordinated to the zinc ion by means of the sulfonamide group and the second one located at the entrance of the cavity. This observation led to the design of elongated molecules incorporating these two ZBGs, separated by a linker of proper length, to allow the simultaneous binding to these different sites. The "long" inhibitors indeed showed around 10 times better enzyme inhibitory properties as compared to the shorter molecules against four physiologically relevant human (h) isoforms, hCA I, II, IX, and XII.

  DOI：

  10.1021/jm300818k

文献信息

• Development of Potent Carbonic Anhydrase Inhibitors Incorporating Both Sulfonamide and Sulfamide Groups
  作者：Katia D'Ambrosio、Fatma-Zhora Smaine、Fabrizio Carta、Giuseppina De Simone、Jean-Yves Winum、Claudiu T. Supuran

  DOI：10.1021/jm300818k

  日期：2012.8.9

  A series of compounds incorporating both sulfonamide and sulfamide as zinc-binding groups (ZBGs) are reported as inhibitors of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1). Crystallographic studies on the complex of hCA II with the lead compound of this series, namely, 4-sulfamido-benzenesulfonamide, revealed the binding of two molecules in the enzyme active site cavity, the first one canonically coordinated to the zinc ion by means of the sulfonamide group and the second one located at the entrance of the cavity. This observation led to the design of elongated molecules incorporating these two ZBGs, separated by a linker of proper length, to allow the simultaneous binding to these different sites. The "long" inhibitors indeed showed around 10 times better enzyme inhibitory properties as compared to the shorter molecules against four physiologically relevant human (h) isoforms, hCA I, II, IX, and XII.