2-(3-hydroxypropyl)quinolin-4(1H)-one | 1380391-50-3

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 喹啉及其衍生物
• 英文名称: 2-(3-hydroxypropyl)quinolin-4(1H)-one
• 英文别名: 2-(3-hydroxypropyl)-1H-quinolin-4-one
• CAS: 1380391-50-3
• 化学式: C₁₂H₁₃NO₂
• 分子量: 203.241
• InChiKey: VWTLFKMWUGGXGI-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  15
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  49.3
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  3-氧代己二酸二乙酯 在 dowtherm A 、 dimethyl sulfide borane 、 硫酸 作用下， 以 四氢呋喃 为溶剂， 反应 48.33h， 生成 2-(3-hydroxypropyl)quinolin-4(1H)-one
  参考文献：
  名称：

  4-Quinolones as Noncovalent Inhibitors of High Molecular Mass Penicillin-Binding Proteins

  摘要：

  Penicillin-binding proteins (PBPs) are important bacterial enzymes that carry out the final steps of bacterial cell wall assembly. Their DD-transpeptidase activity accomplishes the essential peptide cross linking step of the cell wall. To date, all attempts to discover effective inhibitors of PBPs, apart from beta-lactams, have not led to new antibiotics. Therefore, the need for new classes of efficient inhibitors of these enzymes remains. Guided by a computational fragment based docking procedure, carried out on Escherichia cob PBPS, we have designed and synthesized a series of 4-quinolones as potential inhibitors of PBPs. We describe their binding to the PBPs of E cob and Bacillus subtilis. Notably, these compounds bind quite tightly to the essential high molecular mass PBPs.

  DOI：

  10.1021/ml3001006

文献信息

• 4-Quinolones as Noncovalent Inhibitors of High Molecular Mass Penicillin-Binding Proteins
  作者：Abbas G. Shilabin、Liudmila Dzhekieva、Pushpa Misra、B. Jayaram、R. F. Pratt

  DOI：10.1021/ml3001006

  日期：2012.7.12

  Penicillin-binding proteins (PBPs) are important bacterial enzymes that carry out the final steps of bacterial cell wall assembly. Their DD-transpeptidase activity accomplishes the essential peptide cross linking step of the cell wall. To date, all attempts to discover effective inhibitors of PBPs, apart from beta-lactams, have not led to new antibiotics. Therefore, the need for new classes of efficient inhibitors of these enzymes remains. Guided by a computational fragment based docking procedure, carried out on Escherichia cob PBPS, we have designed and synthesized a series of 4-quinolones as potential inhibitors of PBPs. We describe their binding to the PBPs of E cob and Bacillus subtilis. Notably, these compounds bind quite tightly to the essential high molecular mass PBPs.