(9H-fluoren-9-yl)methyl (2-((2-(((benzyloxy)(((2R,3R,4S,5S,6S)-3,4,5-tris(benzyloxy)-6-methoxytetrahydro-2H-pyran-2-yl)methoxy)phosphoryl)oxy)ethyl)amino)-2-oxoethyl)carbamate | 1174890-19-7

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: (9H-fluoren-9-yl)methyl (2-((2-(((benzyloxy)(((2R,3R,4S,5S,6S)-3,4,5-tris(benzyloxy)-6-methoxytetrahydro-2H-pyran-2-yl)methoxy)phosphoryl)oxy)ethyl)amino)-2-oxoethyl)carbamate
• CAS: 1174890-19-7
• 化学式: C₅₄H₅₇N₂O₁₂P
• 分子量: 957.027
• InChiKey: DOVXEIBMKLFXKP-JKFGZMBXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  9.13
• 重原子数：
  69.0
• 可旋转键数：
  24.0
• 环数：
  8.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  158.34
• 氢给体数：
  2.0
• 氢受体数：
  12.0

反应信息

• 作为反应物：
  描述：

  (9H-fluoren-9-yl)methyl (2-((2-(((benzyloxy)(((2R,3R,4S,5S,6S)-3,4,5-tris(benzyloxy)-6-methoxytetrahydro-2H-pyran-2-yl)methoxy)phosphoryl)oxy)ethyl)amino)-2-oxoethyl)carbamate 在 1,8-二氮杂双环[5.4.0]十一碳-7-烯 作用下， 以 二氯甲烷 为溶剂， 反应 0.17h， 生成
  参考文献：
  名称：

  Sortase-Catalyzed Peptide−Glycosylphosphatidylinositol Analogue Ligation

  摘要：

  It is demonstrated that sortase A (SrtA) can catalyze efficient coupling of peptides to GPI analogues with a gtycine residue attached to the phosphoethanotamine moiety at the nonreducing end to form GPI-linked peptides. This represents the first chemoenzymatic synthesis of GPI-peptide conjugates and is a proof-of-concept for the potential application of SrtA to the synthesis of more complex GPI-anchored peptides/glycopeptides and GPI-anchored proteins/glycoproteins.

  DOI：

  10.1021/ja903231v
• 作为产物：
  描述：

  2-aminoethyl benzyl (((2R,3R,4S,5S,6S)-3,4,5-tris(benzyloxy)-6-methoxytetrahydro-2H-pyran-2-yl)methyl) phosphate 、 Fmoc-甘氨酸 在 1-羟基苯并三唑 、 N,N'-二异丙基碳二亚胺 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 以80%的产率得到(9H-fluoren-9-yl)methyl (2-((2-(((benzyloxy)(((2R,3R,4S,5S,6S)-3,4,5-tris(benzyloxy)-6-methoxytetrahydro-2H-pyran-2-yl)methoxy)phosphoryl)oxy)ethyl)amino)-2-oxoethyl)carbamate
  参考文献：
  名称：

  Sortase-Catalyzed Peptide−Glycosylphosphatidylinositol Analogue Ligation

  摘要：

  It is demonstrated that sortase A (SrtA) can catalyze efficient coupling of peptides to GPI analogues with a gtycine residue attached to the phosphoethanotamine moiety at the nonreducing end to form GPI-linked peptides. This represents the first chemoenzymatic synthesis of GPI-peptide conjugates and is a proof-of-concept for the potential application of SrtA to the synthesis of more complex GPI-anchored peptides/glycopeptides and GPI-anchored proteins/glycoproteins.

  DOI：

  10.1021/ja903231v