4-Amino-2-cyclopentyloxy-6-(2-fluorocyclohexyl)oxypyrimidine-5-carboxamide | 1381757-76-1

• 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: 4-Amino-2-cyclopentyloxy-6-(2-fluorocyclohexyl)oxypyrimidine-5-carboxamide
• CAS: 1381757-76-1
• 化学式: C₁₆H₂₃FN₄O₃
• 分子量: 338.382
• InChiKey: RZOBFPPQBGMJTQ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.8
• 重原子数：
  24
• 可旋转键数：
  5
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.69
• 拓扑面积：
  113
• 氢给体数：
  2
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  4-Amino-2-bromo-6-(methylthio)pyrimidine-5-carbonitrile 在 oxone(R) 、 双氧水 、 sodium hydride 、 potassium carbonate 、 N,N-二异丙基乙胺 、 间氯过氧苯甲酸 作用下， 以 四氢呋喃 、 二甲基亚砜 为溶剂， 生成 4-Amino-2-cyclopentyloxy-6-(2-fluorocyclohexyl)oxypyrimidine-5-carboxamide
  参考文献：
  名称：

  Design, synthesis and biological evaluation of potent NAD+-dependent DNA ligase inhibitors as potential antibacterial agents. Part I: Aminoalkoxypyrimidine carboxamides

  摘要：

  A series of 2,6-disubstituted aminoalkoxypyrimidine carboxamides (AAPCs) with potent inhibition of bacterial NAD(+)-dependent DNA ligase was discovered through the use of structure-guided design. Two subsites in the NAD(+)-binding pocket were explored to modulate enzyme inhibitory potency: a hydrophobic selectivity region was explored through a series of 2-alkoxy substituents while the sugar (ribose) binding region of NAD(+) was explored via 6-alkoxy substituents. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2012.04.037

文献信息

• Design, synthesis and biological evaluation of potent NAD+-dependent DNA ligase inhibitors as potential antibacterial agents. Part I: Aminoalkoxypyrimidine carboxamides
  作者：Wenxin Gu、Tiansheng Wang、Francois Maltais、Brian Ledford、Joseph Kennedy、Yunyi Wei、Christian H. Gross、Jonathan Parsons、Leonard Duncan、S.J. Ryan Arends、Cameron Moody、Emanuele Perola、Jeremy Green、Paul S. Charifson

  DOI：10.1016/j.bmcl.2012.04.037

  日期：2012.6

  A series of 2,6-disubstituted aminoalkoxypyrimidine carboxamides (AAPCs) with potent inhibition of bacterial NAD(+)-dependent DNA ligase was discovered through the use of structure-guided design. Two subsites in the NAD(+)-binding pocket were explored to modulate enzyme inhibitory potency: a hydrophobic selectivity region was explored through a series of 2-alkoxy substituents while the sugar (ribose) binding region of NAD(+) was explored via 6-alkoxy substituents. (C) 2012 Elsevier Ltd. All rights reserved.