(6R)-1-aza-6-[(tert-butyldimethylsiloxy)methyl]-3-hydroxy-4-phenyl-2-oxobicyclo[4.3.0]non-3-ene | 325460-67-1

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡咯啉
• 英文名称: (6R)-1-aza-6-[(tert-butyldimethylsiloxy)methyl]-3-hydroxy-4-phenyl-2-oxobicyclo[4.3.0]non-3-ene
• CAS: 325460-67-1
• 化学式: C₂₁H₃₁NO₃Si
• 分子量: 373.568
• InChiKey: DNVIBAVVKWDKQY-OAQYLSRUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.74
• 重原子数：
  26.0
• 可旋转键数：
  4.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.57
• 拓扑面积：
  49.77
• 氢给体数：
  1.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  (6R)-1-aza-6-[(tert-butyldimethylsiloxy)methyl]-3-hydroxy-4-phenyl-2-oxobicyclo[4.3.0]non-3-ene 在 氨 作用下， 以 甲醇 为溶剂， 反应 144.0h， 以69%的产率得到(6R)-1-aza-3-amino-6-[(tert-butyldimethylsiloxy)methyl]-4-phenyl-2-oxobicyclo[4.3.0]non-3-ene
  参考文献：
  名称：

  Constrained Peptidomimetics for TRH: cis-Peptide Bond Analogs

  摘要：

  Two constrained analogs of the tripeptide hormone thyroliberin (TRH) have been synthesized. In both, the HisPro peptide bond of the hormone has been 'locked' into a cis-conformation. In the first analog, the constraint used was identical to the constraint used in an earlier trans-peptide bond analog that was a potent agonist for the TRH endocrine receptor TRH-R-1. The second analog was built in order to take advantage of a tetrazole ring as the cis-peptide bond constraint. Neither analog showed agonist or antagonist behavior toward TRH-R1 suggesting that the cis-peptide bond conformation may not play a role in the affinity of TRH for TRH-R1. (C) 2000 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0040-4020(00)00886-3
• 作为产物：
  描述：

  (6R)-1-aza-6-hydroxymethyl-4-phenyl-2-oxobicyclo[4.3.0]nonane 在 2,6-二甲基吡啶 、 双(三甲基硅烷基)氨基钾 作用下， 以 二氯甲烷 、 甲苯 为溶剂， 反应 2.02h， 生成 (6R)-1-aza-6-[(tert-butyldimethylsiloxy)methyl]-3-hydroxy-4-phenyl-2-oxobicyclo[4.3.0]non-3-ene
  参考文献：
  名称：

  Constrained Peptidomimetics for TRH: cis-Peptide Bond Analogs

  摘要：

  Two constrained analogs of the tripeptide hormone thyroliberin (TRH) have been synthesized. In both, the HisPro peptide bond of the hormone has been 'locked' into a cis-conformation. In the first analog, the constraint used was identical to the constraint used in an earlier trans-peptide bond analog that was a potent agonist for the TRH endocrine receptor TRH-R-1. The second analog was built in order to take advantage of a tetrazole ring as the cis-peptide bond constraint. Neither analog showed agonist or antagonist behavior toward TRH-R1 suggesting that the cis-peptide bond conformation may not play a role in the affinity of TRH for TRH-R1. (C) 2000 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0040-4020(00)00886-3