3-[6-(2,4-difluorophenyl)sulfanyl-[1,2,4]triazolo[4,3-a]pyridin-3-yl]-N-(2-hydroxyethyl)-4-methylbenzamide;hydrochloride | 1207533-81-0

• 分子结构分类: 有机化合物 - 有机硫化合物 - 硫醚类
• 英文名称: 3-[6-(2,4-difluorophenyl)sulfanyl-[1,2,4]triazolo[4,3-a]pyridin-3-yl]-N-(2-hydroxyethyl)-4-methylbenzamide;hydrochloride
• CAS: 1207533-81-0
• 化学式: C₂₂H₁₈F₂N₄O₂S*ClH
• 分子量: 476.934
• InChiKey: FIBKNBRHNMFARZ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.28
• 重原子数：
  32
• 可旋转键数：
  6
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.14
• 拓扑面积：
  105
• 氢给体数：
  3
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  3-{6-[(2,4-difluorophenyl)thio][1,2,4]triazolo[4,3-a]pyridin-3-yl}-N-(2-hydroxyethyl)-4-methylbenzamide 在 盐酸 作用下， 以 1,4-二氧六环 为溶剂， 生成 3-[6-(2,4-difluorophenyl)sulfanyl-[1,2,4]triazolo[4,3-a]pyridin-3-yl]-N-(2-hydroxyethyl)-4-methylbenzamide;hydrochloride
  参考文献：
  名称：

  Continued exploration of the triazolopyridine scaffold as a platform for p38 MAP kinase inhibition

  摘要：

  The structure based drug design, synthesis and structure-activity relationship of a series of C6 sulfur linked triazolopyridine based p38 inhibitors are described. The metabolic deficiencies of this series were overcome through changes in the C6 linker from sulfur to methylene, which was predicted by molecular modeling to be bioisosteric. X-ray of the ethylene linked compound 61 confirmed the predicted binding orientation of the scaffold in the p38 enzyme. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2009.11.114

文献信息

• Continued exploration of the triazolopyridine scaffold as a platform for p38 MAP kinase inhibition
  作者：Kevin D. Jerome、Paul V. Rucker、Li Xing、Huey S. Shieh、John E. Baldus、Shaun R. Selness、Michael A. Letavic、John F. Braganza、Kim F. McClure

  DOI：10.1016/j.bmcl.2009.11.114

  日期：2010.1

  The structure based drug design, synthesis and structure-activity relationship of a series of C6 sulfur linked triazolopyridine based p38 inhibitors are described. The metabolic deficiencies of this series were overcome through changes in the C6 linker from sulfur to methylene, which was predicted by molecular modeling to be bioisosteric. X-ray of the ethylene linked compound 61 confirmed the predicted binding orientation of the scaffold in the p38 enzyme. (C) 2009 Elsevier Ltd. All rights reserved.