(S)-benzyl 2-(4-amino-3-((S)-2-(tert-butoxycarbonylamino)-4-phenylbutanamido)benzamido)-3-methylbutanoate | 1449786-47-3

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: (S)-benzyl 2-(4-amino-3-((S)-2-(tert-butoxycarbonylamino)-4-phenylbutanamido)benzamido)-3-methylbutanoate
• CAS: 1449786-47-3
• 化学式: C₃₄H₄₂N₄O₆
• 分子量: 602.731
• InChiKey: OYRMUGCXNMNDLA-YTMVLYRLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.23
• 重原子数：
  44.0
• 可旋转键数：
  12.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  148.85
• 氢给体数：
  4.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  (S)-benzyl 2-(4-amino-3-((S)-2-(tert-butoxycarbonylamino)-4-phenylbutanamido)benzamido)-3-methylbutanoate 在 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 0.5h， 生成 (S)-benzyl 2-(4-amino-3-((S)-2-amino-4-phenylbutanamido)benzamido)-3-methylbutanoate
  参考文献：
  名称：

  Novel selective inhibitors of aminopeptidases that generate antigenic peptides

  摘要：

  Endoplasmic reticulum aminopeptidases, ERAP1 and ERAP2, as well as Insulin regulated aminopeptidase (IRAP) play key roles in antigen processing, and have recently emerged as biologically important targets for manipulation of antigen presentation. Taking advantage of the available structural and substrate-selectivity data for these enzymes, we have rationally designed a new series of inhibitors that display low micromolar activity. The selectivity profile for these three highly homologous aminopeptidases provides a promising avenue for modulating intracellular antigen processing. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.07.024
• 作为产物：
  描述：

  (S)-methyl 4-amino-3-(2-(tert-butoxycarbonylamino)-4-phenylbutanamido)benzoate 在 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 N,N-二异丙基乙胺 、 lithium hydroxide 作用下， 以 1,4-二氧六环 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 16.0h， 生成 (S)-benzyl 2-(4-amino-3-((S)-2-(tert-butoxycarbonylamino)-4-phenylbutanamido)benzamido)-3-methylbutanoate
  参考文献：
  名称：

  Novel selective inhibitors of aminopeptidases that generate antigenic peptides

  摘要：

  Endoplasmic reticulum aminopeptidases, ERAP1 and ERAP2, as well as Insulin regulated aminopeptidase (IRAP) play key roles in antigen processing, and have recently emerged as biologically important targets for manipulation of antigen presentation. Taking advantage of the available structural and substrate-selectivity data for these enzymes, we have rationally designed a new series of inhibitors that display low micromolar activity. The selectivity profile for these three highly homologous aminopeptidases provides a promising avenue for modulating intracellular antigen processing. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.07.024