4-Chloro-6,7-dimethoxy-quinoline-2-carboxylic acid methyl ester | 1406149-44-7

• 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: 4-Chloro-6,7-dimethoxy-quinoline-2-carboxylic acid methyl ester
• 英文别名: Methyl 4-chloro-6,7-dimethoxyquinoline-2-carboxylate
• CAS: 1406149-44-7
• 化学式: C₁₃H₁₂ClNO₄
• mdl: MFCD18953930
• 分子量: 281.696
• InChiKey: ZDLLJVUVWKJFKA-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.9
• 重原子数：
  19
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.23
• 拓扑面积：
  57.6
• 氢给体数：
  0
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  4-Chloro-6,7-dimethoxy-quinoline-2-carboxylic acid methyl ester 在 氢溴酸 、 sodium hydride 作用下， 以 四氢呋喃 为溶剂， 生成 4-(3,4-Dihydroxy-benzyl)-6,7-dihydroxy-quinoline-2-carboxylic acid
  参考文献：
  名称：

  Quinoline-Carboxylic acids are potent inhibitors that inhibit the binding of insulin-Like growth factor (IGF) to IGF-Binding proteins

  摘要：

  4-Benzylquinolines 5, based on a series of isoquinolines 1, were prepared and tested as inhibitors of the IGF/IGFBP-3 complex based on their ability to displace IGF-I from its binding to IGF-binding protein-3. SAR studies on the 6,7-dihydroxy moiety of the quinoline 5a showed that the catecol moiety could be replaced with other functional groups. Computational modeling of the 5a/mini-IGFBP-5 complex revealed the possible binding site of 5a on IGFBP-5. (C) 2003 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(03)00322-6
• 作为产物：
  描述：

  6,7-dimethoxy-4-hydroxy-2-methoxycarbonylquinoline 在 三氯氧磷 作用下， 生成 4-Chloro-6,7-dimethoxy-quinoline-2-carboxylic acid methyl ester
  参考文献：
  名称：

  Quinoline-Carboxylic acids are potent inhibitors that inhibit the binding of insulin-Like growth factor (IGF) to IGF-Binding proteins

  摘要：

  4-Benzylquinolines 5, based on a series of isoquinolines 1, were prepared and tested as inhibitors of the IGF/IGFBP-3 complex based on their ability to displace IGF-I from its binding to IGF-binding protein-3. SAR studies on the 6,7-dihydroxy moiety of the quinoline 5a showed that the catecol moiety could be replaced with other functional groups. Computational modeling of the 5a/mini-IGFBP-5 complex revealed the possible binding site of 5a on IGFBP-5. (C) 2003 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(03)00322-6