benzyl N-[(2S)-1-[[(1R)-1,2-diamino-2-oxoethyl]amino]-1-oxo-3-phenylpropan-2-yl]carbamate | 1432516-18-1

• 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: benzyl N-[(2S)-1-[[(1R)-1,2-diamino-2-oxoethyl]amino]-1-oxo-3-phenylpropan-2-yl]carbamate
• CAS: 1432516-18-1
• 化学式: C₁₉H₂₂N₄O₄
• 分子量: 370.408
• InChiKey: RDMYFZKEWPNJHO-JKSUJKDBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0
• 重原子数：
  27
• 可旋转键数：
  9
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.21
• 拓扑面积：
  137
• 氢给体数：
  4
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  benzyl N-[(2S)-1-[[(1R)-1,2-diamino-2-oxoethyl]amino]-1-oxo-3-phenylpropan-2-yl]carbamate 在 盐酸 、 水 、 苯酚 作用下， 反应 17.0h， 生成 2,2-diaminoacetic acid 、 L-苯丙氨酸
  参考文献：
  名称：

  Identification of new peptide amides as selective cathepsin L inhibitors: The first step towards selective irreversible inhibitors?

  摘要：

  A small library of peptide amides was designed to profile the cathepsin L active site. Within the cathepsin family of cysteine proteases, the first round of selection was on cathepsin L and cathepsin B, and then selected hits were further evaluated for binding to cathepsin K and cathepsin S. Five highly selective sequences with submicromolar affinities towards cathepsin L were identified. An acyloxymethyl ketone warhead was then attached to these sequences. Although these original irreversible inhibitors inactivate cathepsin L, it appears that the nature of the warhead drastically impact the selectivity profile of the resulting covalent inhibitors. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.03.041

文献信息

• Identification of new peptide amides as selective cathepsin L inhibitors: The first step towards selective irreversible inhibitors?
  作者：Ana Torkar、Brigita Lenarčič、Tamara Lah、Vincent Dive、Laurent Devel

  DOI：10.1016/j.bmcl.2013.03.041

  日期：2013.5

  A small library of peptide amides was designed to profile the cathepsin L active site. Within the cathepsin family of cysteine proteases, the first round of selection was on cathepsin L and cathepsin B, and then selected hits were further evaluated for binding to cathepsin K and cathepsin S. Five highly selective sequences with submicromolar affinities towards cathepsin L were identified. An acyloxymethyl ketone warhead was then attached to these sequences. Although these original irreversible inhibitors inactivate cathepsin L, it appears that the nature of the warhead drastically impact the selectivity profile of the resulting covalent inhibitors. (C) 2013 Elsevier Ltd. All rights reserved.