ethyl 2-acetamido-7-phenylheptanoate | 167113-41-9

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: ethyl 2-acetamido-7-phenylheptanoate
• CAS: 167113-41-9
• 化学式: C₁₇H₂₅NO₃
• 分子量: 291.39
• InChiKey: WBQHBFHHRLOWTL-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.1
• 重原子数：
  21
• 可旋转键数：
  10
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  55.4
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  ethyl 2-acetamido-7-phenylheptanoate 在 CoCl₂ 氢氧化钾 作用下， 以 乙醇 、 水 为溶剂， 反应 73.5h， 生成 L-2-amino-7-phenylheptanoic acid
  参考文献：
  名称：

  Design and Synthesis of Renin Inhibitors: Incorporation of Transition-State Isostere Side Chains That Span from the S1 to the S3 Binding Pockets and Examination of P3-Modified Renin Inhibitors

  摘要：

  A series of renin inhibitors were designed to examine the topography of the contiguous binding pocket of renin that is normally occupied by the P1 and P3 side chains. Molecular modeling suggested that extending the P1 hydrophobic side chain into the adjacent hydrophobic S3 enzyme pocket was feasible. Novel transition state isosteres with modified P1-->P3 side chains were synthesized and provided enhanced binding affinity when incorporated into renin inhibitors in which the P3 Phe was substituted by Gly. In a complementary approach, the binding affinities of a variety of P3-P4-modified peptidomimetic renin inhibitors that lacked substantial hydrophobic side chains at these sites were measured.

  DOI：

  10.1021/jm00015a012
• 作为产物：
  描述：

  (5-溴正戊基)苯 在 氢氧化钾 、 sodium ethanolate 作用下， 以 1,4-二氧六环 、 乙醇 为溶剂， 反应 4.0h， 生成 ethyl 2-acetamido-7-phenylheptanoate
  参考文献：
  名称：

  Design and Synthesis of Renin Inhibitors: Incorporation of Transition-State Isostere Side Chains That Span from the S1 to the S3 Binding Pockets and Examination of P3-Modified Renin Inhibitors

  摘要：

  A series of renin inhibitors were designed to examine the topography of the contiguous binding pocket of renin that is normally occupied by the P1 and P3 side chains. Molecular modeling suggested that extending the P1 hydrophobic side chain into the adjacent hydrophobic S3 enzyme pocket was feasible. Novel transition state isosteres with modified P1-->P3 side chains were synthesized and provided enhanced binding affinity when incorporated into renin inhibitors in which the P3 Phe was substituted by Gly. In a complementary approach, the binding affinities of a variety of P3-P4-modified peptidomimetic renin inhibitors that lacked substantial hydrophobic side chains at these sites were measured.

  DOI：

  10.1021/jm00015a012