4-[(1,5-dimethyl-2-oxo-1,2-dihydro-3H-indol-3-ylidene)amino]benzenesulfonamide

• 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-[(1,5-dimethyl-2-oxo-1,2-dihydro-3H-indol-3-ylidene)amino]benzenesulfonamide
• 英文别名: 4-[(1,5-Dimethyl-2-oxoindol-3-ylidene)amino]benzenesulfonamide；4-[(1,5-dimethyl-2-oxoindol-3-ylidene)amino]benzenesulfonamide
• 化学式: C₁₆H₁₅N₃O₃S
• 分子量: 329.379
• InChiKey: BPVJQFHJSHSVCL-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  23
• 可旋转键数：
  2
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.12
• 拓扑面积：
  101
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  1,5-二甲基靛红 、 磺胺 在 溶剂黄146 作用下， 反应 6.0h， 以20%的产率得到4-[(1,5-dimethyl-2-oxo-1,2-dihydro-3H-indol-3-ylidene)amino]benzenesulfonamide
  参考文献：
  名称：

  Discovery of novel isatin-based sulfonamides with potent and selective inhibition of the tumor-associated carbonic anhydrase isoforms IX and XII

  摘要：

  一系列2/3/4-[(2-氧代-1,2-二氢-3H-吲哚-3-基)氨基]苯磺酰胺，由取代异香草酮和2-、3-或4-氨基苯磺酰胺得到，表现出对肿瘤相关的碳酸酐酶IX和XII的低纳摩尔抑制活性。

  DOI：

  10.1039/c5ob00688k

文献信息

• Discovery of novel isatin-based sulfonamides with potent and selective inhibition of the tumor-associated carbonic anhydrase isoforms IX and XII
  作者：Özlen Güzel-Akdemir、Atilla Akdemir、Nilgün Karalı、Claudiu T. Supuran

  DOI：10.1039/c5ob00688k

  日期：——

  A series of 2/3/4-[(2-oxo-1,2-dihydro-3H-indol-3-ylidene)amino]benzenesulfonamides, obtained from substituted isatins and 2-, 3- or 4-aminobenzenesulfonamide, showed low nanomolar inhibitory activity against the tumor associated carbonic anhydrases IX and XII.

  一系列2/3/4-[(2-氧代-1,2-二氢-3H-吲哚-3-基)氨基]苯磺酰胺，由取代异香草酮和2-、3-或4-氨基苯磺酰胺得到，表现出对肿瘤相关的碳酸酐酶IX和XII的低纳摩尔抑制活性。
• Isatin analogs as novel inhibitors of Candida spp. β-carbonic anhydrase enzymes
  作者：Atilla Akdemir、Özlen Güzel-Akdemir、Nilgün Karalı、Claudiu T. Supuran

  DOI：10.1016/j.bmc.2016.02.036

  日期：2016.4

  Enzyme inhibition data of structurally novel isatin-containing sulfonamides were determined for two carbonic anhydrases (CAs, EC 4.2.1.1) from pathogenic Candida species (CaNce103 from C. albicans and CgNce103 from C. glabrata). The compounds show K-I values in the low nanomolar range for the fungal CAs, while they have significantly higher K-I values for the human CAs. Homology models were constructed for the CaNce103 and CgNce103 and subsequently the ligands were docked into these models to rationalize their enzyme inhibitory properties. (C) 2016 Elsevier Ltd. All rights reserved.