1-methyl-2-phenyl-N-pyridin-3-ylbenzimidazole-5-carboxamide | 1552311-88-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并咪唑类
• 英文名称: 1-methyl-2-phenyl-N-pyridin-3-ylbenzimidazole-5-carboxamide
• CAS: 1552311-88-2
• 化学式: C₂₀H₁₆N₄O
• 分子量: 328.373
• InChiKey: ZMTGLPRTNGYFNR-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.9
• 重原子数：
  25
• 可旋转键数：
  3
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.05
• 拓扑面积：
  59.8
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  3-氨基吡啶 、 1-methyl-2-phenyl-1H-benzo[d]imidazole-5-carboxylic acid 在 N,N-二异丙基乙胺 、 Methanaminium,N-[(dimethylamino)(3H-1,2,3-triazolo[4,5-b]pyridin-3-yloxy)methylene]-N-methyl-, hexafluorophosphate(1-) 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 1-methyl-2-phenyl-N-pyridin-3-ylbenzimidazole-5-carboxamide
  参考文献：
  名称：

  Fragment-based design of 3-aminopyridine-derived amides as potent inhibitors of human nicotinamide phosphoribosyltransferase (NAMPT)

  摘要：

  The fragment-based identification of two novel and potent biochemical inhibitors of the nicotinamide phosphoribosyltransferase (NAMPT) enzyme is described. These compounds (51 and 63) incorporate an amide moiety derived from 3-aminopyridine, and are thus structurally distinct from other known anti-NAMPT agents. Each exhibits potent inhibition of NAMPT biochemical activity (IC50=19 and 15 nM, respectively) as well as robust antiproliferative properties in A2780 cell culture experiments (IC50=121 and 99 nM, respectively). However, additional biological studies indicate that only inhibitor 51 exerts its A2780 cell culture effects via a NAMPT-mediated mechanism. The crystal structures of both 51 and 63 in complex with NAMPT are also independently described.

  DOI：

  10.1016/j.bmcl.2013.12.062

文献信息

• Fragment-based design of 3-aminopyridine-derived amides as potent inhibitors of human nicotinamide phosphoribosyltransferase (NAMPT)
  作者：Peter S. Dragovich、Guiling Zhao、Timm Baumeister、Brandon Bravo、Anthony M. Giannetti、Yen-Ching Ho、Rongbao Hua、Guangkun Li、Xiaorong Liang、Xiaolei Ma、Thomas O’Brien、Angela Oh、Nicholas J. Skelton、Chengcheng Wang、Weiru Wang、Yunli Wang、Yang Xiao、Po-wai Yuen、Mark Zak、Qiang Zhao、Xiaozhang Zheng

  DOI：10.1016/j.bmcl.2013.12.062

  日期：2014.2

  The fragment-based identification of two novel and potent biochemical inhibitors of the nicotinamide phosphoribosyltransferase (NAMPT) enzyme is described. These compounds (51 and 63) incorporate an amide moiety derived from 3-aminopyridine, and are thus structurally distinct from other known anti-NAMPT agents. Each exhibits potent inhibition of NAMPT biochemical activity (IC50=19 and 15 nM, respectively) as well as robust antiproliferative properties in A2780 cell culture experiments (IC50=121 and 99 nM, respectively). However, additional biological studies indicate that only inhibitor 51 exerts its A2780 cell culture effects via a NAMPT-mediated mechanism. The crystal structures of both 51 and 63 in complex with NAMPT are also independently described.