| 1019330-79-0

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 苯丙酸
• CAS: 1019330-79-0
• 化学式: C₂₅H₄₀N₃O₇P
• 分子量: 525.582
• InChiKey: DLVMPKGHNGGETK-KBWCOIMZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.17
• 重原子数：
  36.0
• 可旋转键数：
  12.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.64
• 拓扑面积：
  159.26
• 氢给体数：
  4.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  、 乙酸酐 在 吡啶 作用下， 反应 12.0h， 生成
  参考文献：
  名称：

  Development of Potent and Selective Phosphinic Peptide Inhibitors of Angiotensin-Converting Enzyme 2

  摘要：

  Arimotensin-converting enzyme 2 (ACE2), a recently identified human homologue of angiotensin-converting enzyme, is a zinc metallocarboxypeptidase which may play a unique role in cardiovascular and renal function. Here we report the discovery of potent and selective inhibitors of ACE2, which have been identified by evaluating a series of phosphinic di- and tripeptides of the general formula: Z-Xaa(PO2-CH2)YaaOH and Ac-Zaa-Xaa(PO2-CH2)YaaOH. The most potent inhibitor in this series is a tripeptide that displays a K-i value of 0.4 nM toward ACE2 and is 3 orders of magnitude less potent toward carboxypeptidase A. Phosphinic tripeptides exhibit high potency exclusively when the Xaa position is occupied by a pseudoproline. A model of interaction between one inhibitor of this series and ACE2 suggests that the critical role played by a proline in inhibitors, but also for substrates hydrolysis, may rely on the presence of Tyr(510) in the ACE2 active site.

  DOI：

  10.1021/jm701275z
• 作为产物：
  描述：

  在 palladium on activated charcoal 氢气 、 溶剂黄146 作用下， 以 甲醇 、 水 为溶剂， 20.0 ℃ 、101.33 kPa 条件下， 反应 2.0h， 生成
  参考文献：
  名称：

  Development of Potent and Selective Phosphinic Peptide Inhibitors of Angiotensin-Converting Enzyme 2

  摘要：

  Arimotensin-converting enzyme 2 (ACE2), a recently identified human homologue of angiotensin-converting enzyme, is a zinc metallocarboxypeptidase which may play a unique role in cardiovascular and renal function. Here we report the discovery of potent and selective inhibitors of ACE2, which have been identified by evaluating a series of phosphinic di- and tripeptides of the general formula: Z-Xaa(PO2-CH2)YaaOH and Ac-Zaa-Xaa(PO2-CH2)YaaOH. The most potent inhibitor in this series is a tripeptide that displays a K-i value of 0.4 nM toward ACE2 and is 3 orders of magnitude less potent toward carboxypeptidase A. Phosphinic tripeptides exhibit high potency exclusively when the Xaa position is occupied by a pseudoproline. A model of interaction between one inhibitor of this series and ACE2 suggests that the critical role played by a proline in inhibitors, but also for substrates hydrolysis, may rely on the presence of Tyr(510) in the ACE2 active site.

  DOI：

  10.1021/jm701275z