tert-butyl (3S)-4-(1,3-benzoxazol-2-yl)-4-hydroxy-3-(phenylmethoxycarbonylamino)butanoate | 195072-01-6

• 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: tert-butyl (3S)-4-(1,3-benzoxazol-2-yl)-4-hydroxy-3-(phenylmethoxycarbonylamino)butanoate
• CAS: 195072-01-6
• 化学式: C₂₃H₂₆N₂O₆
• 分子量: 426.469
• InChiKey: QJLHQQMNUTXHPL-DIMJTDRSSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3
• 重原子数：
  31
• 可旋转键数：
  10
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  111
• 氢给体数：
  2
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  tert-butyl (3S)-4-(1,3-benzoxazol-2-yl)-4-hydroxy-3-(phenylmethoxycarbonylamino)butanoate 在 palladium on activated charcoal 氢气 作用下， 以 乙醇 为溶剂， 反应 12.0h， 以85%的产率得到tert-butyl (3S)-3-amino-4-(1,3-benzoxazol-2-yl)-4-hydroxybutanoate
  参考文献：
  名称：

  Expanding the scope of PNA-encoded libraries: divergent synthesis of libraries targeting cysteine, serine and metallo-proteases as well as tyrosine phosphatases

  摘要：

  Seven PNA-encoded combinatorial libraries targeting proteases and phosphatases with covalent reversible and irreversible mechanism-based inhibitors were prepared. The libraries were synthesized using modified PNA monomers, which dramatically increase the water solubility of the libraries in biologically relevant buffers. The libraries were shown to selectively inhibit targeted enzymes. (c) 2007 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tet.2007.03.033
• 作为产物：
  描述：

  N-苄氧羰基-L-天门冬氨酸 4-叔丁酯 在 草酰氯 、 异丙基氯化镁 、 二甲基亚砜 、 三乙胺 、 氯甲酸异丁酯 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 反应 6.17h， 生成 tert-butyl (3S)-4-(1,3-benzoxazol-2-yl)-4-hydroxy-3-(phenylmethoxycarbonylamino)butanoate
  参考文献：
  名称：

  Expanding the scope of PNA-encoded libraries: divergent synthesis of libraries targeting cysteine, serine and metallo-proteases as well as tyrosine phosphatases

  摘要：

  Seven PNA-encoded combinatorial libraries targeting proteases and phosphatases with covalent reversible and irreversible mechanism-based inhibitors were prepared. The libraries were synthesized using modified PNA monomers, which dramatically increase the water solubility of the libraries in biologically relevant buffers. The libraries were shown to selectively inhibit targeted enzymes. (c) 2007 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tet.2007.03.033

文献信息

• Inhibitors of interleukin-1 beta converting enzyme
  申请人：Vertex Pharmaceuticals Incorporated

  公开号：US20020099042A1

  公开（公告）日：2002-07-25

  The present invention relates to novel classes of compounds which are inhibitors of interleukin-1&bgr; converting enzyme. The ICE inhibitors of this invention are characterized by specific structural and physicochemical features. This invention also relates to pharmaceutical compositions comprising these compounds. The compounds and pharmaceutical compositions of this invention are particularly well suited for inhibiting ICE activity and consequently, may be advantageously used as agents against interleukin-1 mediated diseases, including inflammatory diseases, autoimmune diseases and neurodegenerative diseases. This invention also relates to methods for inhibiting ICE activity and methods for treating interleukin-1 mediated diseases using the compounds and compositions of this invention.

  本发明涉及一种新型化合物类别，其为白细胞介素-1β转化酶抑制剂。本发明的ICE抑制剂具有特定的结构和物理化学特征。本发明还涉及包含这些化合物的制药组合物。本发明的化合物和制药组合物特别适用于抑制ICE活性，因此可以优势地用作对白细胞介素-1介导的疾病，包括炎症性疾病、自身免疫疾病和神经退行性疾病的治疗剂。本发明还涉及使用本发明的化合物和组合物抑制ICE活性的方法和治疗白细胞介素-1介导疾病的方法。
• US6420522B1
  申请人：——

  公开号：US6420522B1

  公开（公告）日：2002-07-16
• US7288624B2
  申请人：——

  公开号：US7288624B2

  公开（公告）日：2007-10-30
• Expanding the scope of PNA-encoded libraries: divergent synthesis of libraries targeting cysteine, serine and metallo-proteases as well as tyrosine phosphatases
  作者：François Debaene、Julien A. Da Silva、Zbigniew Pianowski、Fernando J. Duran、Nicolas Winssinger

  DOI：10.1016/j.tet.2007.03.033

  日期：2007.7

  Seven PNA-encoded combinatorial libraries targeting proteases and phosphatases with covalent reversible and irreversible mechanism-based inhibitors were prepared. The libraries were synthesized using modified PNA monomers, which dramatically increase the water solubility of the libraries in biologically relevant buffers. The libraries were shown to selectively inhibit targeted enzymes. (c) 2007 Elsevier Ltd. All rights reserved.