N-isopropyl-10H-phenothiazine-10-carboxamide | 81225-58-3

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并噻嗪类
• 英文名称: N-isopropyl-10H-phenothiazine-10-carboxamide
• 英文别名: N-propan-2-ylphenothiazine-10-carboxamide
• CAS: 81225-58-3
• 化学式: C₁₆H₁₆N₂OS
• 分子量: 284.382
• InChiKey: DIHZRSIYRBANNR-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.6
• 重原子数：
  20
• 可旋转键数：
  1
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.19
• 拓扑面积：
  57.6
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  吩噻嗪-10-碳酰氯 、 异丙胺 以 二氯甲烷 为溶剂， 以68%的产率得到N-isopropyl-10H-phenothiazine-10-carboxamide
  参考文献：
  名称：

  Differential binding of phenothiazine urea derivatives to wild-type human cholinesterases and butyrylcholinesterase mutants

  摘要：

  A series of N-10 urea derivatives of phenothiazine was synthesized and each compound was evaluated for its ability to inhibit human cholinesterases. Most were specific inhibitors of BuChE. However, the potent inhibitory effects on both cholinesterases of one sub-class, the cationic aminoureas, provide an additional binding mechanism to cholinesterases for these compounds. The comparative effects of aminoureas on wild-type BuChE and several BuChE mutants indicate a binding process involving salt linkage with the aspartate of the cholinesterase peripheral anionic site. The effect of such compounds on cholinesterase activity at high substrate concentration supports ionic interaction of aminoureas at the peripheral anionic site. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2010.01.066

文献信息

• KATSUURA, YASUXIRO;NAJTO, IBIN;XORIUTI, TOKIO;UMIRODZAVA, KU;MORIGUTI, UT+
  作者：KATSUURA, YASUXIRO、NAJTO, IBIN、XORIUTI, TOKIO、UMIRODZAVA, KU、MORIGUTI, UT+

  DOI：——

  日期：——
• JPS56166183A
  申请人：——

  公开号：JPS56166183A

  公开（公告）日：1981-12-21
• Differential binding of phenothiazine urea derivatives to wild-type human cholinesterases and butyrylcholinesterase mutants
  作者：Sultan Darvesh、Ian R. Pottie、Katherine V. Darvesh、Robert S. McDonald、Ryan Walsh、Sarah Conrad、Andrea Penwell、Diane Mataija、Earl Martin

  DOI：10.1016/j.bmc.2010.01.066

  日期：2010.3

  A series of N-10 urea derivatives of phenothiazine was synthesized and each compound was evaluated for its ability to inhibit human cholinesterases. Most were specific inhibitors of BuChE. However, the potent inhibitory effects on both cholinesterases of one sub-class, the cationic aminoureas, provide an additional binding mechanism to cholinesterases for these compounds. The comparative effects of aminoureas on wild-type BuChE and several BuChE mutants indicate a binding process involving salt linkage with the aspartate of the cholinesterase peripheral anionic site. The effect of such compounds on cholinesterase activity at high substrate concentration supports ionic interaction of aminoureas at the peripheral anionic site. (C) 2010 Elsevier Ltd. All rights reserved.