CT-GlcNAc2-LC-biotin | 1196042-66-6

• 分子结构分类: 有机化合物 - 有机聚合物 - 多糖
• 英文名称: CT-GlcNAc2-LC-biotin
• CAS: 1196042-66-6
• 化学式: C₇₈H₁₃₀N₈O₄₈S
• 分子量: 1979.98
• InChiKey: GVOVBCWLVWKXLF-VHYLSAJFSA-N

物化性质

• 密度：
  1.67±0.1 g/cm3(Temp: 20 °C; Press: 760 Torr)(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -18.53
• 重原子数：
  135.0
• 可旋转键数：
  41.0
• 环数：
  11.0
• sp3杂化的碳原子比例：
  0.91
• 拓扑面积：
  858.16
• 氢给体数：
  32.0
• 氢受体数：
  49.0

反应信息

• 作为反应物：
  描述：

  CT-GlcNAc2-LC-biotin 在 β-1,4-galactosidase from Bacteroides fragilis 作用下， 反应 24.0h， 以100%的产率得到GlcNAc2Man3GlcNAc2-LC-biotin
  参考文献：
  名称：

  Chemoenzymatic Synthesis and Lectin Array Characterization of a Class of N-Glycan Clusters

  摘要：

  N-Glycans are major components of many glycoproteins. These sugar moieties are frequently involved in important physiological and disease processes via their interactions with a variety of glycan-binding proteins (GBP). Clustering effect is an important feature in many glycan-lectin interactions. We describe in this paper a chemoenzymatic synthesis of novel N-glycan clusters using a tandem endoglycosidase-catalyzed transglycosylation. It was found that the internal beta-1,2-linked GlcNAc moieties in the N-glycan core, once exposed in the nonreducing terminus, was able to serve as acceptors for transglycosylation catalyzed by Endo-A and EndoM-N175A. This efficient chemoenzymatic method allows a quick extension of the sugar chains to form a class of glycan clusters in which sugar residues are all connected by native glycosidic linkages found in natural N-glycans. In addition, a discriminative enzymatic reaction at the two GlcNAc residues could be fulfilled to afford novel hybrid clusters. Lectin microarray studies revealed unusual properties in glyco-epitope expression by this panel of structurally well-defined synthetic N-glycans. These new compounds are likely valuable for functional glycomics studies to unveil new functions of both glycans and carbohydrate-binding proteins.

  DOI：

  10.1021/ja9078539
• 作为产物：
  描述：

  CT-ox 、 GlcNAc-LC-biotin 在 EndoM-N₁₇₅A 作用下， 反应 8.0h， 以72%的产率得到CT-GlcNAc2-LC-biotin
  参考文献：
  名称：

  Chemoenzymatic Synthesis and Lectin Array Characterization of a Class of N-Glycan Clusters

  摘要：

  N-Glycans are major components of many glycoproteins. These sugar moieties are frequently involved in important physiological and disease processes via their interactions with a variety of glycan-binding proteins (GBP). Clustering effect is an important feature in many glycan-lectin interactions. We describe in this paper a chemoenzymatic synthesis of novel N-glycan clusters using a tandem endoglycosidase-catalyzed transglycosylation. It was found that the internal beta-1,2-linked GlcNAc moieties in the N-glycan core, once exposed in the nonreducing terminus, was able to serve as acceptors for transglycosylation catalyzed by Endo-A and EndoM-N175A. This efficient chemoenzymatic method allows a quick extension of the sugar chains to form a class of glycan clusters in which sugar residues are all connected by native glycosidic linkages found in natural N-glycans. In addition, a discriminative enzymatic reaction at the two GlcNAc residues could be fulfilled to afford novel hybrid clusters. Lectin microarray studies revealed unusual properties in glyco-epitope expression by this panel of structurally well-defined synthetic N-glycans. These new compounds are likely valuable for functional glycomics studies to unveil new functions of both glycans and carbohydrate-binding proteins.

  DOI：

  10.1021/ja9078539