N-propyl-5-(2-(pyridin-2-yl)pyrimidin-4-yl)thiazol-2-amine | 1254353-05-3

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪类
• 英文名称: N-propyl-5-(2-(pyridin-2-yl)pyrimidin-4-yl)thiazol-2-amine
• 英文别名: N-propyl-5-(2-pyridin-2-ylpyrimidin-4-yl)-1,3-thiazol-2-amine
• CAS: 1254353-05-3
• 化学式: C₁₅H₁₅N₅S
• 分子量: 297.384
• InChiKey: HXKNDDUSBPXWJF-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.8
• 重原子数：
  21
• 可旋转键数：
  5
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.2
• 拓扑面积：
  91.8
• 氢给体数：
  1
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  吡啶-2-羧酰胺 、 5-(prop-1-en-1-yl)-N-propylthiazol-2-amine 在 sodium methylate 作用下， 以 乙醇 为溶剂， 生成 N-propyl-5-(2-(pyridin-2-yl)pyrimidin-4-yl)thiazol-2-amine
  参考文献：
  名称：

  Utilization of a nitrogen–sulfur nonbonding interaction in the design of new 2-aminothiazol-5-yl-pyrimidines as p38α MAP kinase inhibitors

  摘要：

  The design, synthesis, and structure-activity relationships (SAR) of a series of 2-aminothiazol-5-yl-pyrimidines as novel p38α MAP kinase inhibitors are described. These efforts led to the identification of 41 as a potent p38α inhibitor that utilizes a unique nitrogen-sulfur intramolecular nonbonding interaction to stabilize the conformation required for binding to the p38α active site. X-ray crystallographic studies that confirm the proposed binding mode of this class of inhibitors in p38 α and provide evidence for the proposed intramolecular nitrogen-sulfur interaction are discussed.

  DOI：

  10.1016/j.bmcl.2010.07.102

文献信息

• Utilization of a nitrogen–sulfur nonbonding interaction in the design of new 2-aminothiazol-5-yl-pyrimidines as p38α MAP kinase inhibitors
  作者：Shuqun Lin、Stephen T. Wrobleski、John Hynes、Sidney Pitt、Rosemary Zhang、Yi Fan、Arthur M. Doweyko、Kevin F. Kish、John S. Sack、Mary F. Malley、Susan E. Kiefer、John A. Newitt、Murray McKinnon、James Trzaskos、Joel C. Barrish、John H. Dodd、Gary L. Schieven、Katerina Leftheris

  DOI：10.1016/j.bmcl.2010.07.102

  日期：2010.10

  The design, synthesis, and structure-activity relationships (SAR) of a series of 2-aminothiazol-5-yl-pyrimidines as novel p38α MAP kinase inhibitors are described. These efforts led to the identification of 41 as a potent p38α inhibitor that utilizes a unique nitrogen-sulfur intramolecular nonbonding interaction to stabilize the conformation required for binding to the p38α active site. X-ray crystallographic studies that confirm the proposed binding mode of this class of inhibitors in p38 α and provide evidence for the proposed intramolecular nitrogen-sulfur interaction are discussed.