4-[2-(Dimethylamino)ethoxy]benzene-1-carbothioamide | 938320-39-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚醚
• 英文名称: 4-[2-(Dimethylamino)ethoxy]benzene-1-carbothioamide
• 英文别名: 4-[2-(dimethylamino)ethoxy]benzenecarbothioamide
• CAS: 938320-39-9
• 化学式: C₁₁H₁₆N₂OS
• mdl: MFCD09717985
• 分子量: 224.327
• InChiKey: KGWSEAQYTYTBCA-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  15
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.363
• 拓扑面积：
  70.6
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  4-[2-(Dimethylamino)ethoxy]benzene-1-carbothioamide 、 (S)-tert-butyl 5-(benzyloxycarbonylamino)-7-bromo-6-oxoheptylcarbamate 在 乙醇 作用下， 生成 (S)-tert-butyl 5-amino-5-(2-(4-(2-(dimethylamino)ethoxy)phenyl)thiazol-4-yl)pentylcarbamate
  参考文献：
  名称：

  Synthesis and evaluation of lysine derived sulfamides as histone deacetylase inhibitors

  摘要：

  We have recently reported on a novel class of histone deacetylase (HDAC) inhibitors bearing a sulfamide group as the zinc-binding unit. Herein, we report on the synthesis of sulfamide based inhibitors designed around a lysine scaffold and their structure-activity relationships against HDAC1 and HDAC6 isotypes as well as 293T cells. Our efforts led us to an improvement of the originally disclosed lysine-based sulfamide, 2a to compound 12h which has equal potency in enzyme and cell-based assays as well as enhanced metabolic stability and PK profile. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2009.02.075

文献信息

• Synthesis and evaluation of lysine derived sulfamides as histone deacetylase inhibitors
  作者：Sukhdev Manku、Martin Allan、Natalie Nguyen、Alain Ajamian、Jacques Rodrigue、Eric Therrien、James Wang、Tim Guo、Jubrail Rahil、Andrea J. Petschner、Alina Nicolescu、Sylvain Lefebvre、Zuomei Li、Marielle Fournel、Jeffrey M. Besterman、Robert Déziel、Amal Wahhab

  DOI：10.1016/j.bmcl.2009.02.075

  日期：2009.4

  We have recently reported on a novel class of histone deacetylase (HDAC) inhibitors bearing a sulfamide group as the zinc-binding unit. Herein, we report on the synthesis of sulfamide based inhibitors designed around a lysine scaffold and their structure-activity relationships against HDAC1 and HDAC6 isotypes as well as 293T cells. Our efforts led us to an improvement of the originally disclosed lysine-based sulfamide, 2a to compound 12h which has equal potency in enzyme and cell-based assays as well as enhanced metabolic stability and PK profile. (C) 2009 Elsevier Ltd. All rights reserved.