5-tert-butyl-3-(3-naphthalen-2-ylureido)thiophene-2-carboxylic acid | 1351667-06-5

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: 5-tert-butyl-3-(3-naphthalen-2-ylureido)thiophene-2-carboxylic acid
• CAS: 1351667-06-5
• 化学式: C₂₀H₂₀N₂O₃S
• 分子量: 368.456
• InChiKey: HFUHJHZTKAHWQV-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.54
• 重原子数：
  26.0
• 可旋转键数：
  3.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.2
• 拓扑面积：
  78.43
• 氢给体数：
  3.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  5-tert-butyl-3-(3-naphthalen-2-ylureido)thiophene-2-carboxylic acid 在 硼烷四氢呋喃络合物 、 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 N,N-二异丙基乙胺 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 反应 75.0h， 生成 1-(5-tert-butyl-2-(1,1-dioxothiomorpholin-4-ylmethyl)thiophen-3-yl)-3 naphthalen-2-ylurea
  参考文献：
  名称：

  Discovery of a novel class of non-ATP site DFG-out state p38 inhibitors utilizing computationally assisted virtual fragment-based drug design (vFBDD)

  摘要：

  Discovery of a new class of DFG-out p38α kinase inhibitors with no hinge interaction is described. A computationally assisted, virtual fragment-based drug design (vFBDD) platform was utilized to identify novel non-aromatic fragments which make productive hydrogen bond interactions with Arg 70 on the αC-helix. Molecules incorporating these fragments were found to be potent inhibitors of p38 kinase. X-ray co-crystal structures confirmed the predicted binding modes. A lead compound was identified as a potent (p38α IC(50)=22 nM) and highly selective (≥ 150-fold against 150 kinase panel) DFG-out p38 kinase inhibitor.

  DOI：

  10.1016/j.bmcl.2011.09.078
• 作为产物：
  描述：

  2-氨基-5-叔丁基噻吩-3-羧酸 以 1,4-二氧六环 、 水 、 甲苯 为溶剂， 反应 25.0h， 生成 5-tert-butyl-3-(3-naphthalen-2-ylureido)thiophene-2-carboxylic acid
  参考文献：
  名称：

  Discovery of a novel class of non-ATP site DFG-out state p38 inhibitors utilizing computationally assisted virtual fragment-based drug design (vFBDD)

  摘要：

  Discovery of a new class of DFG-out p38α kinase inhibitors with no hinge interaction is described. A computationally assisted, virtual fragment-based drug design (vFBDD) platform was utilized to identify novel non-aromatic fragments which make productive hydrogen bond interactions with Arg 70 on the αC-helix. Molecules incorporating these fragments were found to be potent inhibitors of p38 kinase. X-ray co-crystal structures confirmed the predicted binding modes. A lead compound was identified as a potent (p38α IC(50)=22 nM) and highly selective (≥ 150-fold against 150 kinase panel) DFG-out p38 kinase inhibitor.

  DOI：

  10.1016/j.bmcl.2011.09.078