2-氨基-6-喹啉羧酸乙酯 | 342908-16-1

• 物质功能分类: 医药中间体 - 杂环化合物 - 喹啉类化合物
• 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
• 中文名称: 2-氨基-6-喹啉羧酸乙酯
• 中文别名: 2-氨基喹啉-6-甲酸乙酯
• 英文名称: 2-aminoquinoline-6-carboxylic acid ethyl ester
• 英文别名: ethyl 2-aminoquinoline-6-carboxylate
• CAS: 342908-16-1
• 化学式: C₁₂H₁₂N₂O₂
• 分子量: 216.239
• InChiKey: NMSBMFZAJIEPMQ-UHFFFAOYSA-N

物化性质

• 沸点：
  385.8±22.0 °C(Predicted)
• 密度：
  1.246±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.3
• 重原子数：
  16
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.17
• 拓扑面积：
  65.2
• 氢给体数：
  1
• 氢受体数：
  4

安全信息

• 海关编码：
  2933499090

反应信息

• 作为反应物：
  描述：

  2-氨基-6-喹啉羧酸乙酯 在 盐酸 、 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 三乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 3-[4-cyano-2-[2-(2-aminoquinoline-6-carbonyl)aminoethoxy]phenyl]-2-acetamidoacrylic acid methyl ester
  参考文献：
  名称：

  Optimization of a coagulation factor VIIa inhibitor found in factor Xa inhibitor library☆

  摘要：

  An inhibitor of the complex of factor Vila and tissue factor (fVIIa/TF), 2-substituted-4-amidinophenylpyruvic acid la, was structurally modified with the aim of increasing its potency and selectivity. The lead compound la was originally found in our factor Xa (fXa) inhibitor library on the basis of structural similarity of the primary binding sites of tVIIa and fXa. The design was based on computational docking studies using the extracted active site of tVIIa. Compound 1j was found to inhibit factor VIIa/TF at nanomolar concentration with improved selectivity versus fXa and thrombin and it preferentially prolonged the clotting time in the TF-dependent extrinsic pathway. (C) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2004.12.033
• 作为产物：
  描述：

  6-喹啉甲酸乙酯 在 间氯过氧苯甲酸 、 三氯氧磷 、 苯酚 作用下， 以 二氯甲烷 为溶剂， 反应 1.17h， 生成 2-氨基-6-喹啉羧酸乙酯
  参考文献：
  名称：

  Optimization of a coagulation factor VIIa inhibitor found in factor Xa inhibitor library☆

  摘要：

  An inhibitor of the complex of factor Vila and tissue factor (fVIIa/TF), 2-substituted-4-amidinophenylpyruvic acid la, was structurally modified with the aim of increasing its potency and selectivity. The lead compound la was originally found in our factor Xa (fXa) inhibitor library on the basis of structural similarity of the primary binding sites of tVIIa and fXa. The design was based on computational docking studies using the extracted active site of tVIIa. Compound 1j was found to inhibit factor VIIa/TF at nanomolar concentration with improved selectivity versus fXa and thrombin and it preferentially prolonged the clotting time in the TF-dependent extrinsic pathway. (C) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2004.12.033

文献信息

• Amidinophenylpyruvic acid derivatives
  申请人：AJINOMOTO CO. INC

  公开号：US20030109547A1

  公开（公告）日：2003-06-12

  An amidinophenylpyruvic acid derivative of the following formula, analogs thereof and pharmaceutically acceptable salts thereof have an excellent antagonistic effect against activated blood coagulation factor VII. 1

  以下是该公式的一种氨基苯丙酸衍生物，其类似物和药学上可接受的盐具有出色的对激活的凝血因子VII的拮抗作用。
• AMIDINOPHENYLPYRUVIC ACID DERIVATIVE
  申请人：Ajinomoto Co., Inc.

  公开号：EP1236712A1

  公开（公告）日：2002-09-04

  An amidinophenylpyruvic acid derivative of the following formula, analogs thereof and pharmaceutically acceptable salts thereof have an excellent antagonistic effect against activated blood coagulation factor VII.

  下式中的脒苯基丙酮酸衍生物、其类似物和药学上可接受的盐类对活化的凝血因子 VII 有极好的拮抗作用。
• US6710056B2
  申请人：——

  公开号：US6710056B2

  公开（公告）日：2004-03-23
• Optimization of a coagulation factor VIIa inhibitor found in factor Xa inhibitor library☆
  作者：Kazuyuki Sagi、Koichi Fujita、Masayuki Sugiki、Mitsuo Takahashi、Shunji Takehana、Kazumi Tashiro、Takashi Kayahara、Masahiro Yamanashi、Yumiko Fukuda、Seiji Oono

  DOI：10.1016/j.bmc.2004.12.033

  日期：2005.3.1

  An inhibitor of the complex of factor Vila and tissue factor (fVIIa/TF), 2-substituted-4-amidinophenylpyruvic acid la, was structurally modified with the aim of increasing its potency and selectivity. The lead compound la was originally found in our factor Xa (fXa) inhibitor library on the basis of structural similarity of the primary binding sites of tVIIa and fXa. The design was based on computational docking studies using the extracted active site of tVIIa. Compound 1j was found to inhibit factor VIIa/TF at nanomolar concentration with improved selectivity versus fXa and thrombin and it preferentially prolonged the clotting time in the TF-dependent extrinsic pathway. (C) 2005 Elsevier Ltd. All rights reserved.