Boc-Phe-(DMT)-A | 1333389-11-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 三苯基化合物
• 英文名称: Boc-Phe-(DMT)-A
• 英文别名: (S)-(2R,3R,4R,5R)-2-(6-amino-9H-purin-9-yl)-5-((bis(4-methoxyphenyl)(phenyl)methoxy)methyl)-4-hydroxytetrahydrofuran-3-yl 2-((tert-butoxycarbonyl)amino)-3-phenylpropanoate
• CAS: 1333389-11-9
• 化学式: C₄₅H₄₈N₆O₉
• 分子量: 816.911
• InChiKey: LOOLWWKJXLEQQW-GCJHUVJRSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.74
• 重原子数：
  60.0
• 可旋转键数：
  14.0
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.31
• 拓扑面积：
  191.4
• 氢给体数：
  3.0
• 氢受体数：
  14.0

反应信息

• 作为反应物：
  描述：

  Boc-Phe-(DMT)-A 在 三异丙基硅烷 、 三氟乙酸 作用下， 以 四氢呋喃 为溶剂， 反应 12.0h， 以53.5%的产率得到(S)-(2R,3R,4R,5R)-2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl 2-amino-3-phenylpropanoate
  参考文献：
  名称：

  N-Terminal Protein Modification Using Simple Aminoacyl Transferase Substrates

  摘要：

  Methods for synthetically manipulating protein structure enable greater flexibility in the study of protein function. Previous characterization of the Escherichia coli aminoacyl tRNA transferase (AaT) has shown that it can modify the N-terminus of a protein with an amino acid from a tRNA or a synthetic oligonucleotide donor. Here, we demonstrate that AaT can efficiently use a minimal adenosine substrate, which can be synthesized in one to two steps from readily available starting materials. We have characterized the enzymatic activity of AaT with aminoacyl adenosyl donors and found that reaction products do not inhibit AaT. The use of adenosyl donors removes the substrate limitations imposed by the use of synthetases for tRNA charging and avoids the complex synthesis of an oligonucleotide donor. Thus, our AaT donors increase the potential substrate scope and reaction scale for N-terminal protein modification under conditions that maintain folding.

  DOI：

  10.1021/ja2055098
• 作为产物：
  描述：

  BOC-L-苯丙氨酸 在 四丁基醋酸铵 、 N,N-二异丙基乙胺 作用下， 以 四氢呋喃 为溶剂， 生成 Boc-Phe-(DMT)-A
  参考文献：
  名称：

  N-Terminal Protein Modification Using Simple Aminoacyl Transferase Substrates

  摘要：

  Methods for synthetically manipulating protein structure enable greater flexibility in the study of protein function. Previous characterization of the Escherichia coli aminoacyl tRNA transferase (AaT) has shown that it can modify the N-terminus of a protein with an amino acid from a tRNA or a synthetic oligonucleotide donor. Here, we demonstrate that AaT can efficiently use a minimal adenosine substrate, which can be synthesized in one to two steps from readily available starting materials. We have characterized the enzymatic activity of AaT with aminoacyl adenosyl donors and found that reaction products do not inhibit AaT. The use of adenosyl donors removes the substrate limitations imposed by the use of synthetases for tRNA charging and avoids the complex synthesis of an oligonucleotide donor. Thus, our AaT donors increase the potential substrate scope and reaction scale for N-terminal protein modification under conditions that maintain folding.

  DOI：

  10.1021/ja2055098