N-(2,3-dihydro-1H-inden-1-yl)-2,3,4,5,6-pentafluorobenzamide | 1026913-79-0

• 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: N-(2,3-dihydro-1H-inden-1-yl)-2,3,4,5,6-pentafluorobenzamide
• CAS: 1026913-79-0
• 化学式: C₁₆H₁₀F₅NO
• 分子量: 327.254
• InChiKey: JQTHWGBKNVJIFM-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.1
• 重原子数：
  23
• 可旋转键数：
  2
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.19
• 拓扑面积：
  29.1
• 氢给体数：
  1
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  N-(2,3-dihydro-1H-inden-1-yl)-2,3,4,5,6-pentafluorobenzamide 在 氯磺酸 、 ammonium hydroxide 作用下， 以 四氢呋喃 为溶剂， 反应 2.0h， 生成 2,3,4,5,6-Pentafluoro-N-(5-sulfamoyl-indan-1-yl)-benzamide
  参考文献：
  名称：

  Indanesulfonamides as Carbonic Anhydrase Inhibitors. Toward Structure-Based Design of Selective Inhibitors of the Tumor-Associated Isozyme CA IX

  摘要：

  Carbonic anhydrases are ubiquitous metalloenzymes which are involved in fundamental processes (i.e., acid-base regulation, respiration, calcification, etc.). The carbonic anhydrase isozyme IX becomes an interesting pharmacological target due to its overexpression in cancer and its absence in normal tissue. Therefore, several indanesulfonamides were synthesized and tested for their inhibition both against the human CA IX and against two other biologically relevant isozymes (CA I and II). Structure-activity relationships are discussed and point out different compounds for its selectivity and activity against CA IX. To establish preliminary hypothesis for the design of new isozyme-selective CA IX inhibitors, we conducted molecular modeling. We describe here the first human CA IX model built by homology with another CA isozyme already crystallized. Docking studies were performed to explore the binding mode of our indanesulfonamide derivatives.

  DOI：

  10.1021/jm0600287
• 作为产物：
  描述：

  五氟苯甲酰氯 、 1-氨基茚满 以 氯仿 为溶剂， 生成 N-(2,3-dihydro-1H-inden-1-yl)-2,3,4,5,6-pentafluorobenzamide
  参考文献：
  名称：

  Indanesulfonamides as Carbonic Anhydrase Inhibitors. Toward Structure-Based Design of Selective Inhibitors of the Tumor-Associated Isozyme CA IX

  摘要：

  Carbonic anhydrases are ubiquitous metalloenzymes which are involved in fundamental processes (i.e., acid-base regulation, respiration, calcification, etc.). The carbonic anhydrase isozyme IX becomes an interesting pharmacological target due to its overexpression in cancer and its absence in normal tissue. Therefore, several indanesulfonamides were synthesized and tested for their inhibition both against the human CA IX and against two other biologically relevant isozymes (CA I and II). Structure-activity relationships are discussed and point out different compounds for its selectivity and activity against CA IX. To establish preliminary hypothesis for the design of new isozyme-selective CA IX inhibitors, we conducted molecular modeling. We describe here the first human CA IX model built by homology with another CA isozyme already crystallized. Docking studies were performed to explore the binding mode of our indanesulfonamide derivatives.

  DOI：

  10.1021/jm0600287

文献信息

• Indanesulfonamides as Carbonic Anhydrase Inhibitors. Toward Structure-Based Design of Selective Inhibitors of the Tumor-Associated Isozyme CA IX
  作者：Anne Thiry、Marie Ledecq、Alessandro Cecchi、Jean-Michel Dogné、Johan Wouters、Claudiu T. Supuran、Bernard Masereel

  DOI：10.1021/jm0600287

  日期：2006.5.1

  Carbonic anhydrases are ubiquitous metalloenzymes which are involved in fundamental processes (i.e., acid-base regulation, respiration, calcification, etc.). The carbonic anhydrase isozyme IX becomes an interesting pharmacological target due to its overexpression in cancer and its absence in normal tissue. Therefore, several indanesulfonamides were synthesized and tested for their inhibition both against the human CA IX and against two other biologically relevant isozymes (CA I and II). Structure-activity relationships are discussed and point out different compounds for its selectivity and activity against CA IX. To establish preliminary hypothesis for the design of new isozyme-selective CA IX inhibitors, we conducted molecular modeling. We describe here the first human CA IX model built by homology with another CA isozyme already crystallized. Docking studies were performed to explore the binding mode of our indanesulfonamide derivatives.