O-[(2,3,4-tri-O-benzyl-6-O-acetyl-α-D-mannopyranosyl)-(1->2)-(3,4,6-tri-O-benzyl-α-D-mannopyranosyl)-(1->6)-(2,3,4-tri-O-benzyl-α-D-mannopyranose)] trichloroacetimidate | 1208120-43-7

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: O-[(2,3,4-tri-O-benzyl-6-O-acetyl-α-D-mannopyranosyl)-(1->2)-(3,4,6-tri-O-benzyl-α-D-mannopyranosyl)-(1->6)-(2,3,4-tri-O-benzyl-α-D-mannopyranose)] trichloroacetimidate
• CAS: 1208120-43-7
• 化学式: C₈₅H₈₈Cl₃NO₁₇
• 分子量: 1501.99
• InChiKey: NFKBWQOQMYWSOK-CNNSBXQGSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  15.39
• 重原子数：
  106.0
• 可旋转键数：
  36.0
• 环数：
  12.0
• sp3杂化的碳原子比例：
  0.34
• 拓扑面积：
  188.6
• 氢给体数：
  1.0
• 氢受体数：
  18.0

反应信息

• 作为反应物：
  描述：

  O-[(2,3,4-tri-O-benzyl-6-O-acetyl-α-D-mannopyranosyl)-(1->2)-(3,4,6-tri-O-benzyl-α-D-mannopyranosyl)-(1->6)-(2,3,4-tri-O-benzyl-α-D-mannopyranose)] trichloroacetimidate 、 (2-azido-3,6-di-O-benzyl-2-deoxy-α-D-glucopyranosyl)-(1->6)-2,3,4,5-tetra-O-benzyl-1-O-(4-methoxybenzyl)-D-myo-inositol 在 三氟甲磺酸三甲基硅酯 作用下， 以 乙醚 为溶剂， 生成
  参考文献：
  名称：

  Sortase A-mediated chemoenzymatic synthesis of complex glycosylphosphatidylinositol-anchored protein

  摘要：

  合成了绿色荧光蛋白和含有共同核心结构和脂质链的糖基磷脂酰肌醇（GPI）锚，然后偶联在一起以促进细菌分选酶A（SrtA），这是合成全尺寸GPI的第一个例子-SrtA 锚定蛋白，证明这可能是 GPI 锚定蛋白合成的普遍有用的方法。

  DOI：

  10.1039/c3cc47229a
• 作为产物：
  描述：

  Bn(-2)[Bn(-3)][Bn(-4)]Man6Ac(a1-2)[Bn(-3)][Bn(-4)][Bn(-6)]Man(a1-6)[Bn(-2)][Bn(-3)][Bn(-4)]a-Man 、 三氯乙腈 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， 以85%的产率得到O-[(2,3,4-tri-O-benzyl-6-O-acetyl-α-D-mannopyranosyl)-(1->2)-(3,4,6-tri-O-benzyl-α-D-mannopyranosyl)-(1->6)-(2,3,4-tri-O-benzyl-α-D-mannopyranose)] trichloroacetimidate
  参考文献：
  名称：

  Sortase A-Catalyzed Transpeptidation of Glycosylphosphatidylinositol Derivatives for Chemoenzymatic Synthesis of GPI-Anchored Proteins

  摘要：

  Several peptides/small proteins and glycosylphosphatidylinositol (GPI) derivatives were synthesized and compared as substrates of sortase A (SrtA), a bacterial transpeptidase, for enzymatic coupling. It was observed that peptides containing the LPKTGGS and LPKTGGRS sequences as sorting signals at the peptide C-terminus were effectively coupled to GPI derivatives having one or two glycine residues attached to the phosphoethanolamine group at the nonreducing end. This reaction was employed to prepare several analogues of the human CD52 and CD24 antigens, which are naturally GPI-anchored glycopeptides/glycoproteins. It was further observed that the trisaccharide GPI analogues 5 and 6 were better SrtA substrates than monosaccharide GPI analogue 4, suggesting that steric hindrance of the GPI analogues does not affect their peptidation reaction mediated by SrtA. Therefore, this synthetic strategy may be useful for the preparation of more complex GPI-anchored peptides, glycopeptides, proteins, and glycoproteins.

  DOI：

  10.1021/ja906611x

文献信息

• Chemoenzymatic Synthesis of the Human CD52 and CD24 Antigen Analogues
  作者：Zhimeng Wu、Xueqing Guo、Guofeng Gu、Zhongwu Guo

  DOI：10.1021/ol4028144

  日期：2013.11.15

  Analogs of the human CD52 and CO24 antigens carrying the common core structure of glycosylphosphatidylinositol (GPI) anchors and the intact polypeptide sequences of CD52 and CD24 were chemoenzymatically synthesized. CD52 and CD24 proteins were obtained by solid-phase peptide synthesis and then coupled to chemically synthesized GPI anchors under the influence of a bacterial enzyme, sortase A, to afford the target molecules in good yields.