4-(4-oxo-2,3-dihydro-1H-carbazol-9-yl)benzamide | 1043513-64-9

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吲哚及其衍生物
• 英文名称: 4-(4-oxo-2,3-dihydro-1H-carbazol-9-yl)benzamide
• CAS: 1043513-64-9
• 化学式: C₁₉H₁₆N₂O₂
• 分子量: 304.348
• InChiKey: FDKLVNCEPWGQIF-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  23
• 可旋转键数：
  2
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.16
• 拓扑面积：
  65.1
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  在 氢氧化钾 、 水 、 双氧水 、 二甲基亚砜 作用下， 以 乙醇 为溶剂， 反应 2.5h， 生成 4-(4-oxo-2,3-dihydro-1H-carbazol-9-yl)benzamide
  参考文献：
  名称：

  Discovery of benzamide tetrahydro-4H-carbazol-4-ones as novel small molecule inhibitors of Hsp90

  摘要：

  Hsp90 maintains the conformational stability of multiple proteins implicated in oncogenesis and has emerged as a target for chemotherapy. We report here the discovery of a novel small molecule scaffold that inhibits Hsp90. X-ray data show that the scaffold binds competitively at the ATP site on Hsp90. Cellular proliferation and client assays demonstrate that members of the series are able to inhibit Hsp90 at nanomolar concentrations.

  DOI：

  10.1016/j.bmcl.2008.05.023

文献信息

• Novel carbazole and acyl-indole antimitotics
  作者：Thomas E. Barta、Amy F. Barabasz、Briana E. Foley、Lifeng Geng、Steven E. Hall、Gunnar J. Hanson、Matthew Jenks、Wei Ma、John W. Rice、James Veal

  DOI：10.1016/j.bmcl.2009.04.010

  日期：2009.6

  In the course of our Heat Shock 90 program, certain carbazole compounds were identified which had an off-target antiproliferative activity. To understand the off-target activity, we studied one analog with strong activity. We discovered that it had an effect on tubulin polymerization kinetics and was competitive with colchicine. Additional analogs were made, and a number of potent compounds were identified. (C) 2009 Elsevier Ltd. All rights reserved.
• Discovery of benzamide tetrahydro-4H-carbazol-4-ones as novel small molecule inhibitors of Hsp90
  作者：Thomas E. Barta、James M. Veal、John W. Rice、Jeffrey M. Partridge、R. Patrick Fadden、Wei Ma、Matthew Jenks、Lifeng Geng、Gunnar J. Hanson、Kenneth H. Huang、Amy F. Barabasz、Briana E. Foley、James Otto、Steven E. Hall

  DOI：10.1016/j.bmcl.2008.05.023

  日期：2008.6

  Hsp90 maintains the conformational stability of multiple proteins implicated in oncogenesis and has emerged as a target for chemotherapy. We report here the discovery of a novel small molecule scaffold that inhibits Hsp90. X-ray data show that the scaffold binds competitively at the ATP site on Hsp90. Cellular proliferation and client assays demonstrate that members of the series are able to inhibit Hsp90 at nanomolar concentrations.