| 1443011-81-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• CAS: 1443011-81-1
• 化学式: C₁₈H₁₇N₃O₂
• 分子量: 307.352
• InChiKey: POPPQLUQVJXWJK-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.64
• 重原子数：
  23.0
• 可旋转键数：
  3.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.06
• 拓扑面积：
  101.37
• 氢给体数：
  4.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  糠醛 、 在 sodium cyanoborohydride 、 zinc(II) chloride 作用下， 以 甲醇 为溶剂， 反应 1.5h， 以49%的产率得到3,5-bis[(furan-2-ylmethyl)amino]-4-hydroxy-N-(naphthalen-2-ylmethyl)benzamide
  参考文献：
  名称：

  Structural basis for the design and synthesis of selective HDAC inhibitors

  摘要：

  Histone Deacetylases are considered promising targets for cancer epigenetic therapy, and small molecules able to modulate their biological function have recently gained an increasing interest as potential anticancer agents. In spite of their potential application in cancer therapy, most HDAC inhibitors unselectively bind the several HDAC isoforms, giving rise to different side-effects. In this context, we have traced out the structural elements responsible of selective binding for the therapeutically relevant different HDAC isoforms. The structural analysis has been carried out by molecular modeling, docking in the binding pockets of HDAC1-4 and HDAC6-8, 36 inhibitors presenting a well defined selectivity for the different isoforms. As quick proof of evidence, we have designed, synthesized and experimentally tested three selective ligands. The experimental data suggest that the obtained structural guidelines can be useful tools for the rational design of new potent inhibitors against selected HDAC isoforms. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2013.04.036
• 作为产物：
  描述：

  萘-2-甲胺 在 tin(II) chloride dihdyrate 、 1-羟基苯并三唑 、 三乙胺 、 N,N'-二异丙基碳二亚胺 作用下， 以 乙醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 48.5h， 生成
  参考文献：
  名称：

  Structural basis for the design and synthesis of selective HDAC inhibitors

  摘要：

  Histone Deacetylases are considered promising targets for cancer epigenetic therapy, and small molecules able to modulate their biological function have recently gained an increasing interest as potential anticancer agents. In spite of their potential application in cancer therapy, most HDAC inhibitors unselectively bind the several HDAC isoforms, giving rise to different side-effects. In this context, we have traced out the structural elements responsible of selective binding for the therapeutically relevant different HDAC isoforms. The structural analysis has been carried out by molecular modeling, docking in the binding pockets of HDAC1-4 and HDAC6-8, 36 inhibitors presenting a well defined selectivity for the different isoforms. As quick proof of evidence, we have designed, synthesized and experimentally tested three selective ligands. The experimental data suggest that the obtained structural guidelines can be useful tools for the rational design of new potent inhibitors against selected HDAC isoforms. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2013.04.036