N-(5-tert-butyl-3-cyano-2-methoxyphenyl)-2-oxo-2-(4-(pyridin-4-ylamino)naphthalene-1-yl)acetamide | 1041051-35-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: N-(5-tert-butyl-3-cyano-2-methoxyphenyl)-2-oxo-2-(4-(pyridin-4-ylamino)naphthalene-1-yl)acetamide
• 英文别名: N-(5-tert-butyl-3-cyano-2-methoxyphenyl)-2-oxo-2-(4-(pyridin-4-ylamino)naphthalen-1-yl)acetamide；N-(5-tert-butyl-3-cyano-2-methoxyphenyl)-2-oxo-2-[4-(pyridin-4-ylamino)naphthalen-1-yl]acetamide
• CAS: 1041051-35-7
• 化学式: C₂₉H₂₆N₄O₃
• 分子量: 478.55
• InChiKey: LZIAGZLGKVTFMX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.7
• 重原子数：
  36
• 可旋转键数：
  7
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.17
• 拓扑面积：
  104
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  3-amino-5-(tert-butyl)-2-methoxybenzonitrile 、 2-oxo-2-(4-(pyridin-4-ylamino)naphthalen-1-yl)acetic acid 在 benzotriazol-1-yloxyl-tris-(pyrrolidino)-phosphonium hexafluorophosphate 、 1-羟基苯并三唑 、 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 16.0h， 生成 N-(5-tert-butyl-3-cyano-2-methoxyphenyl)-2-oxo-2-(4-(pyridin-4-ylamino)naphthalene-1-yl)acetamide
  参考文献：
  名称：

  Optimization of α-ketoamide based p38 inhibitors through modifications to the region that binds to the allosteric site

  摘要：

  We have optimized a novel series of potent p38 MAP kinase inhibitors based on an alpha-ketoamide scaffold through structure based design that due to their extended molecular architecture bind, in addition to the ATP site, to an allosteric pocket. In vitro ADME, in vivo PK and efficacy studies show these compounds to have drug-like characteristics and have resulted in the nomination of a development candidate which is currently in phase II clinical trials for the oral treatment of inflammatory conditions. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2010.06.102

文献信息

• Optimization of α-ketoamide based p38 inhibitors through modifications to the region that binds to the allosteric site
  作者：Antonio Garrido Montalban、Erik Boman、Chau-Dung Chang、Susana Conde Ceide、Russell Dahl、David Dalesandro、Nancy G.J. Delaet、Eric Erb、Justin T. Ernst、Andrew Gibbs、Jeffrey Kahl、Linda Kessler、Jeff Kucharski、Christopher Lum、Jan Lundström、Stephen Miller、Hiroshi Nakanishi、Edward Roberts、Eddine Saiah、Robert Sullivan、Jan Urban、Zhijun Wang、Christopher J. Larson

  DOI：10.1016/j.bmcl.2010.06.102

  日期：2010.8

  We have optimized a novel series of potent p38 MAP kinase inhibitors based on an alpha-ketoamide scaffold through structure based design that due to their extended molecular architecture bind, in addition to the ATP site, to an allosteric pocket. In vitro ADME, in vivo PK and efficacy studies show these compounds to have drug-like characteristics and have resulted in the nomination of a development candidate which is currently in phase II clinical trials for the oral treatment of inflammatory conditions. (C) 2010 Elsevier Ltd. All rights reserved.