ethyl 3-<(1H,4H-quinoline-4-one)-2-yl>propionate | 110830-31-4

• 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: ethyl 3-<(1H,4H-quinoline-4-one)-2-yl>propionate
• 英文别名: ethyl 3-(1,4-dihydro-4-oxoquinolin-2-yl)propanoate；Ethyl 3-(4-oxo-1,4-dihydro-2-quinolinyl)propanoate；ethyl 3-(4-oxo-1H-quinolin-2-yl)propanoate
• CAS: 110830-31-4
• 化学式: C₁₄H₁₅NO₃
• 分子量: 245.278
• InChiKey: DGZRRTHWFKZOOH-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2
• 重原子数：
  18
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  55.4
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  ethyl 3-<(1H,4H-quinoline-4-one)-2-yl>propionate 在 dimethyl sulfide borane 作用下， 以 四氢呋喃 为溶剂， 以58.5%的产率得到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
• 作为产物：
  描述：

  3-氧代己二酸二乙酯 在 dowtherm A 、 硫酸 作用下， 反应 48.33h， 生成 ethyl 3-<(1H,4H-quinoline-4-one)-2-yl>propionate
  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

• Synthesis and Spectroscopic Studies of Some Novel Quinoline Derivatives
  作者：Hamad Z. Alkhathlan

  DOI：10.1080/00397919208021666

  日期：1992.9

  Abstract An intramolecular Wittig reaction of some substituted aminoacetophenones was used for the synthesis of novel quinoline derivatives. In addition, the base induced cyclization of the aminoacetophenones was investigated. The IR and NMR spectra of the quinoline derivatives are reported.

  摘要 一些取代氨基苯乙酮的分子内Wittig反应用于合成新型喹啉衍生物。此外，研究了碱诱导的氨基苯乙酮环化。报告了喹啉衍生物的 IR 和 NMR 光谱。
• Deady, Leslie W.; Werden, Dianne M., Synthetic Communications, 1987, vol. 17, # 3, p. 319 - 328
  作者：Deady, Leslie W.、Werden, Dianne M.

  DOI：——

  日期：——
• DEADY L. W.; WERDEN D. M., SYNTH. COMMUN., 1987, 17, N 3, 319-328
  作者：DEADY L. W.、 WERDEN D. M.

  DOI：——

  日期：——
• 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.