(4-Acetoxy-benzyloxycarbonylamino)-acetic acid | 50444-49-0

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚酯
• 英文名称: (4-Acetoxy-benzyloxycarbonylamino)-acetic acid
• 英文别名: 2-[(4-Acetyloxyphenyl)methoxycarbonylamino]acetic acid
• CAS: 50444-49-0
• 化学式: C₁₂H₁₃NO₆
• 分子量: 267.238
• InChiKey: GYMYPIGBICBJCA-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.8
• 重原子数：
  19
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  102
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  (4-Acetoxy-benzyloxycarbonylamino)-acetic acid 在 4-二甲氨基吡啶 、 1-羟基苯并三唑 、 三乙胺 、 N,N'-二环己基碳二亚胺 、 1,4-二巯基-2,3-丁二醇 作用下， 以 四氢呋喃 为溶剂， 生成 (R)-2-[2-(4-Acetoxy-benzyloxycarbonylamino)-acetylamino]-3-hexadecanoylsulfanyl-propionic acid allyl ester
  参考文献：
  名称：

  Chemoenzymatic Synthesis of Fluorescent N-Ras Lipopeptides and Their Use in Membrane Localization Studies in Vivo

  摘要：

  DOI：

  10.1002/anie.199722381
• 作为产物：
  描述：

  4-乙酰氧基苄醇 在 三乙胺 作用下， 以 四氢呋喃 、 甲苯 为溶剂， 反应 13.0h， 生成 (4-Acetoxy-benzyloxycarbonylamino)-acetic acid
  参考文献：
  名称：

  Chemoenzymatic Synthesis of N-Ras Lipopeptides

  摘要：

  For the study of biological phenomena influenced by the plasma-membrane-bound Ras proteins and other lipidated proteins, characteristic peptides which embody the correct lipid modifications of their parent proteins (palmitoyl thioesters and farnesyl thioethers), as well as analogues thereof, may serve as suitable tools. For the construction of such acid- and base-labile peptide conjugates, the enzyme-labile p-acetoxybenzyloxycarbonyl (AcOZ) urethane blocking group was developed. The acetate moiety within the AcOZ group is easily saponified by treatment with acetyl esterase or lipase. After cleavage of the acetate group the resulting quinone methide spontaneously fragments, resulting in the liberation of the desired peptide or peptide conjugates. This enzymatic protecting group technique formed the key step in the synthesis of the characteristic S-palmitoylated and S-farnesylated C-terminus of the human N-Ras protein. Deprotections are so mild that no undesired side reactions of the lipid conjugates are observed (i.e., no hydrolysis or beta-elimination of the thioester and no acid-mediated attack on the double bonds of the farnesyl group). The combination of enzymatic protecting group techniques with classical chemical methods allowed access to various fluorescent-labeled and differently lipid-modified Rns lipopeptides. Their application in biological experiments enabeled the study of the structural requirements for the acylation of Ras sequence motifs in vivo and gave insight into the subcellular site at which these modifications occur. The results indicate that the plasma membrane is a major site of cellular S-acylation. This supports a mechanism for the selective subcellular localization of lipidated proteins, including the Rns proteins themselves, by kinetic targeting to the plasma membrane.

  DOI：

  10.1021/ja9805627