N-(6-sulfamoylbenzo[d]thiazol-2-yl)-2-((4-sulfamoylphenyl)amino)acetamide

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: N-(6-sulfamoylbenzo[d]thiazol-2-yl)-2-((4-sulfamoylphenyl)amino)acetamide
• 英文别名: 2-(4-sulfamoylanilino)-N-(6-sulfamoyl-1,3-benzothiazol-2-yl)acetamide
• 化学式: C₁₅H₁₅N₅O₅S₃
• 分子量: 441.513
• InChiKey: CUUCLHRCIMVYFM-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.7
• 重原子数：
  28
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.07
• 拓扑面积：
  219
• 氢给体数：
  4
• 氢受体数：
  10

反应信息

• 作为产物：
  描述：

  2-氨基-1,3-苯并噻唑-6-磺酰胺 在 potassium carbonate 作用下， 以 四氢呋喃 、 N,N-二甲基甲酰胺 为溶剂， 反应 72.0h， 生成 N-(6-sulfamoylbenzo[d]thiazol-2-yl)-2-((4-sulfamoylphenyl)amino)acetamide
  参考文献：
  名称：

  Design and synthesis of benzothiazole-6-sulfonamides acting as highly potent inhibitors of carbonic anhydrase isoforms I, II, IX and XII

  摘要：

  A series of novel 2-aminobenzothiazole derivatives bearing sulfonamide at position 6 was designed, synthesized and investigated as inhibitors of four isoforms of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1), the cytosolic CA I and II, and the tumor-associated isozymes CA IX and XII. Docking and binding energy studies were carried out to reveal details regarding the favorable interactions between the scaffolds of these new inhibitors and the active sites of the investigated CA isoforms. Most of the novel compounds were acting as highly potent inhibitors of the tumor-associated hCA IX and hCA XII with K(I)s in the nanomolar range. The ubiquitous and dominant rapid cytosolic isozyme hCA II was also inhibited with K(I)s ranging from 3.5 to 45.4 nM. The favorable interactions between some of the new compounds and the active site of different CA isoforms were delineated by using molecular docking which may be useful for designing compounds with high affinity and selectivity for some CAs with biomedical applications. (C) 2015 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2015.05.019

文献信息

• Design and synthesis of benzothiazole-6-sulfonamides acting as highly potent inhibitors of carbonic anhydrase isoforms I, II, IX and XII
  作者：Diaa A. Ibrahim、Deena S. Lasheen、Maysoun Y. Zaky、Amany W. Ibrahim、Daniela Vullo、Mariangela Ceruso、Claudiu T. Supuran、Dalal A. Abou El Ella

  DOI：10.1016/j.bmc.2015.05.019

  日期：2015.8

  A series of novel 2-aminobenzothiazole derivatives bearing sulfonamide at position 6 was designed, synthesized and investigated as inhibitors of four isoforms of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1), the cytosolic CA I and II, and the tumor-associated isozymes CA IX and XII. Docking and binding energy studies were carried out to reveal details regarding the favorable interactions between the scaffolds of these new inhibitors and the active sites of the investigated CA isoforms. Most of the novel compounds were acting as highly potent inhibitors of the tumor-associated hCA IX and hCA XII with K(I)s in the nanomolar range. The ubiquitous and dominant rapid cytosolic isozyme hCA II was also inhibited with K(I)s ranging from 3.5 to 45.4 nM. The favorable interactions between some of the new compounds and the active site of different CA isoforms were delineated by using molecular docking which may be useful for designing compounds with high affinity and selectivity for some CAs with biomedical applications. (C) 2015 Elsevier Ltd. All rights reserved.