2-O-acetyl-3,4-di-O-benzyl-α-L-rhamnopyranosyl-(1->3)-2-O-acetyl-4-O-benzyl-α-L-rhamnopyranosyl trichloroacetimidate | 1239318-81-0

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 2-O-acetyl-3,4-di-O-benzyl-α-L-rhamnopyranosyl-(1->3)-2-O-acetyl-4-O-benzyl-α-L-rhamnopyranosyl trichloroacetimidate
• CAS: 1239318-81-0
• 化学式: C₃₉H₄₄Cl₃NO₁₁
• 分子量: 809.137
• InChiKey: CSODBBBKLVINIL-VSQZDIKGSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.84
• 重原子数：
  54.0
• 可旋转键数：
  14.0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.46
• 拓扑面积：
  141.06
• 氢给体数：
  1.0
• 氢受体数：
  12.0

反应信息

• 作为反应物：
  描述：

  4-戊烯-1-醇 、 2-O-acetyl-3,4-di-O-benzyl-α-L-rhamnopyranosyl-(1->3)-2-O-acetyl-4-O-benzyl-α-L-rhamnopyranosyl trichloroacetimidate 在 三氟甲磺酸三甲基硅酯 作用下， 以 二氯甲烷 为溶剂， 反应 1.5h， 以61%的产率得到pent-4-enyl 2-O-acetyl-3,4-di-O-benzyl-α-L-rhamnopyranosyl-(1->3)-2-O-acetyl-4-O-benzyl-α-L-rhamnopyranosyide
  参考文献：
  名称：

  Molecular Analysis of Carbohydrate−Antibody Interactions: Case Study Using a Bacillus anthracis Tetrasaccharide

  摘要：

  The process for selecting potent and effective carbohydrate antigens is not well-established. A combination of synthetic glycan microarray screening, surface plasmon resonance analysis, and saturation transfer difference NMR spectroscopy was used to dissect the antibody-binding surface of a carbohydrate antigen, revealing crucial binding elements with atomic-level detail. This analysis takes the first step toward uncovering the rules for structure-based design of carbohydrate antigens.

  DOI：

  10.1021/ja104027w
• 作为产物：
  描述：

  、 三氯乙腈 在 sodium hydride 作用下， 以 二氯甲烷 为溶剂， 以88%的产率得到2-O-acetyl-3,4-di-O-benzyl-α-L-rhamnopyranosyl-(1->3)-2-O-acetyl-4-O-benzyl-α-L-rhamnopyranosyl trichloroacetimidate
  参考文献：
  名称：

  Molecular Analysis of Carbohydrate−Antibody Interactions: Case Study Using a Bacillus anthracis Tetrasaccharide

  摘要：

  The process for selecting potent and effective carbohydrate antigens is not well-established. A combination of synthetic glycan microarray screening, surface plasmon resonance analysis, and saturation transfer difference NMR spectroscopy was used to dissect the antibody-binding surface of a carbohydrate antigen, revealing crucial binding elements with atomic-level detail. This analysis takes the first step toward uncovering the rules for structure-based design of carbohydrate antigens.

  DOI：

  10.1021/ja104027w