6-(3,5-dimethylisoxazol-4-yl)-N-(thiophen-2-ylmethyl)quinazolin-4-amine | 959562-48-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二氮杂萘
• 英文名称: 6-(3,5-dimethylisoxazol-4-yl)-N-(thiophen-2-ylmethyl)quinazolin-4-amine
• 英文别名: 6-(3,5-dimethyl-1,2-oxazol-4-yl)-N-(thiophen-2-ylmethyl)quinazolin-4-amine
• CAS: 959562-48-2
• 化学式: C₁₈H₁₆N₄OS
• 分子量: 336.417
• InChiKey: SFOUDLQYBQLSRX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.9
• 重原子数：
  24
• 可旋转键数：
  4
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.17
• 拓扑面积：
  92.1
• 氢给体数：
  1
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  3,5-二甲基异恶唑-4-硼酸 、 6-bromo-N-(thiophen-2-ylmethyl)quinazolin-4-amine 在 四(三苯基膦)钯 、 sodium carbonate 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 1.0h， 生成 6-(3,5-dimethylisoxazol-4-yl)-N-(thiophen-2-ylmethyl)quinazolin-4-amine
  参考文献：
  名称：

  Evaluation of substituted 6-arylquinazolin-4-amines as potent and selective inhibitors of cdc2-like kinases (Clk)

  摘要：

  A series of substituted 6-arylquinazolin-4-amines were prepared and analyzed as inhibitors of Clk4. Synthesis, structure-activity relationships and the selectivity of a potent analogue against a panel of 402 kinases are presented. Inhibition of Clk4 by these agents at varied concentrations of assay substrates (ATP and receptor peptide) highly suggests that this chemotype is an ATP competitive inhibitor. Molecular docking provides further evidence that inhibition is the result of binding at the kinase hinge region. Selected compounds represent novel tools capable of potent and selective inhibition of Clk1, Clk4, and Dyrk1A. Published by Elsevier Ltd.

  DOI：

  10.1016/j.bmcl.2009.09.121

文献信息

• Evaluation of substituted 6-arylquinazolin-4-amines as potent and selective inhibitors of cdc2-like kinases (Clk)
  作者：Bryan T. Mott、Cordelle Tanega、Min Shen、David J. Maloney、Paul Shinn、William Leister、Juan J. Marugan、James Inglese、Christopher P. Austin、Tom Misteli、Douglas S. Auld、Craig J. Thomas

  DOI：10.1016/j.bmcl.2009.09.121

  日期：2009.12

  A series of substituted 6-arylquinazolin-4-amines were prepared and analyzed as inhibitors of Clk4. Synthesis, structure-activity relationships and the selectivity of a potent analogue against a panel of 402 kinases are presented. Inhibition of Clk4 by these agents at varied concentrations of assay substrates (ATP and receptor peptide) highly suggests that this chemotype is an ATP competitive inhibitor. Molecular docking provides further evidence that inhibition is the result of binding at the kinase hinge region. Selected compounds represent novel tools capable of potent and selective inhibition of Clk1, Clk4, and Dyrk1A. Published by Elsevier Ltd.