{[4-(Benzyloxycarbonylamino-methyl)-benzoyl]-tert-butoxycarbonylmethyl-amino}-acetic acid tert-butyl ester | 851513-73-0

• 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: {[4-(Benzyloxycarbonylamino-methyl)-benzoyl]-tert-butoxycarbonylmethyl-amino}-acetic acid tert-butyl ester
• CAS: 851513-73-0
• 化学式: C₂₈H₃₆N₂O₇
• 分子量: 512.603
• InChiKey: IKTDLMRPPLOMJB-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.24
• 重原子数：
  37.0
• 可旋转键数：
  9.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  111.24
• 氢给体数：
  1.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  {[4-(Benzyloxycarbonylamino-methyl)-benzoyl]-tert-butoxycarbonylmethyl-amino}-acetic acid tert-butyl ester 在 palladium on activated charcoal 氢气 作用下， 以 甲醇 为溶剂， 反应 4.0h， 以250 mg的产率得到di-t-butyl N-(4-aminomethyl-benzoyl)iminodiacetate
  参考文献：
  名称：

  Directed Denaturation:  Room Temperature and Stoichiometric Unfolding of Cytochrome c by a Metalloporphyrin Dimer

  摘要：

  Using circular dichroism, UV-vis, and trypsin proteolysis, we have shown how a metalloporphyrin dimer induces the unfolding of a protein, cytochrome c, under physiologically relevant conditions and accelerates its rate of proteolytic degradation.

  DOI：

  10.1021/ja028574m
• 作为产物：
  描述：

  氯甲酸苄酯 在 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 作用下， 以 二氯甲烷 、 水 为溶剂， 反应 20.0h， 生成 {[4-(Benzyloxycarbonylamino-methyl)-benzoyl]-tert-butoxycarbonylmethyl-amino}-acetic acid tert-butyl ester
  参考文献：
  名称：

  Directed Denaturation:  Room Temperature and Stoichiometric Unfolding of Cytochrome c by a Metalloporphyrin Dimer

  摘要：

  Using circular dichroism, UV-vis, and trypsin proteolysis, we have shown how a metalloporphyrin dimer induces the unfolding of a protein, cytochrome c, under physiologically relevant conditions and accelerates its rate of proteolytic degradation.

  DOI：

  10.1021/ja028574m

文献信息

• Catalytic Unfolding and Proteolysis of Cytochrome <i>c</i> Induced by Synthetic Binding Agents
  作者：Kevin Groves、Andrew J. Wilson、Andrew D. Hamilton

  DOI：10.1021/ja0317731

  日期：2004.10.1

  A class of polyanionic copper porphyrin dimers is shown to selectively increase the susceptibility of cytochrome c to proteolysis through binding-induced disruption of tertiary and secondary structure. The free energy of the protein conformation leading to proteolytic attack is stabilized by about 2.4 kcal/mol in the bound state. The proteolytic acceleration is catalytic in nature, requiring only a fraction of an equivalent of metalloporphyrin to effect complete, rapid digestion in the presence of a protease.