rac,cis-N-tert-butoxycarbonyl-7-azabicyclo<4.2.0>-oct-4-en-8-one

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 氮杂环丁烷
• 英文名称: rac,cis-N-tert-butoxycarbonyl-7-azabicyclo<4.2.0>-oct-4-en-8-one
• 英文别名: tert-butyl (1S,6R)-8-oxo-7-azabicyclo[4.2.0]oct-4-ene-7-carboxylate
• 化学式: C₁₂H₁₇NO₃
• 分子量: 223.272
• InChiKey: DIRYFKYIEKHZOA-DTWKUNHWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  16
• 可旋转键数：
  2
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  46.6
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  rac,cis-N-tert-butoxycarbonyl-7-azabicyclo<4.2.0>-oct-4-en-8-one 在 lithium hydroxide 作用下， 以 四氢呋喃 为溶剂， 反应 7.0h， 以91%的产率得到(1R*,2S*)-2-(tert-butoxycarbonylamino)cyclohex-3-enecarboxylic acid
  参考文献：
  名称：

  Structure-Based Design, Synthesis, and X-ray Crystallography of a High-Affinity Antagonist of the Grb2-SH2 Domain Containing an Asparagine Mimetic

  摘要：

  Previous efforts in the search for molecules capable of blocking the associations between the activated tyrosine kinase growth factor receptors and the SH2 domain of Grb2 had resulted in the identification of 3-amino-Z-pTyr-Ac(6)c-Asn-NH2, a high-affinity and selective antagonist of this SH2 domain. In the present paper, we report the successful replacement of asparagine in this compound by a beta-amino acid mimetic, which brings us closer to our objective of identifying a Grb2-SH2 antagonist suitable for pharmacological investigations.

  DOI：

  10.1021/jm991013u
• 作为产物：
  描述：

  二碳酸二叔丁酯 、 7-azabicyclo[4.2.0]oct-4-en-8-one 在 4-二甲氨基吡啶 、 三乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 6.0h， 以82%的产率得到rac,cis-N-tert-butoxycarbonyl-7-azabicyclo<4.2.0>-oct-4-en-8-one
  参考文献：
  名称：

  Structure-Based Design, Synthesis, and X-ray Crystallography of a High-Affinity Antagonist of the Grb2-SH2 Domain Containing an Asparagine Mimetic

  摘要：

  Previous efforts in the search for molecules capable of blocking the associations between the activated tyrosine kinase growth factor receptors and the SH2 domain of Grb2 had resulted in the identification of 3-amino-Z-pTyr-Ac(6)c-Asn-NH2, a high-affinity and selective antagonist of this SH2 domain. In the present paper, we report the successful replacement of asparagine in this compound by a beta-amino acid mimetic, which brings us closer to our objective of identifying a Grb2-SH2 antagonist suitable for pharmacological investigations.

  DOI：

  10.1021/jm991013u

文献信息

• Structure-Based Design, Synthesis, and X-ray Crystallography of a High-Affinity Antagonist of the Grb2-SH2 Domain Containing an Asparagine Mimetic
  作者：Pascal Furet、Carlos García-Echeverría、Brigitte Gay、Joseph Schoepfer、Martin Zeller、Joseph Rahuel

  DOI：10.1021/jm991013u

  日期：1999.7.1

  Previous efforts in the search for molecules capable of blocking the associations between the activated tyrosine kinase growth factor receptors and the SH2 domain of Grb2 had resulted in the identification of 3-amino-Z-pTyr-Ac(6)c-Asn-NH2, a high-affinity and selective antagonist of this SH2 domain. In the present paper, we report the successful replacement of asparagine in this compound by a beta-amino acid mimetic, which brings us closer to our objective of identifying a Grb2-SH2 antagonist suitable for pharmacological investigations.