4-methoxyphenyl 2-O-acetyl-3,4-di-O-benzyl-α-L-rhamnopyranosyl-(1->3)-2-O-acetyl-4-O-benzyl-α-L-rhamnopyranoside | 1239318-80-9

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 4-methoxyphenyl 2-O-acetyl-3,4-di-O-benzyl-α-L-rhamnopyranosyl-(1->3)-2-O-acetyl-4-O-benzyl-α-L-rhamnopyranoside
• CAS: 1239318-80-9
• 化学式: C₄₄H₅₀O₁₂
• 分子量: 770.874
• InChiKey: ZWLWMKLNLQSZPG-UBHIDCPXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.57
• 重原子数：
  56.0
• 可旋转键数：
  16.0
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.41
• 拓扑面积：
  126.44
• 氢给体数：
  0.0
• 氢受体数：
  12.0

反应信息

• 作为反应物：
  描述：

  4-methoxyphenyl 2-O-acetyl-3,4-di-O-benzyl-α-L-rhamnopyranosyl-(1->3)-2-O-acetyl-4-O-benzyl-α-L-rhamnopyranoside 在 ammonium cerium (IV) nitrate 作用下， 以 水 、 乙腈 为溶剂， 反应 2.0h， 以92%的产率得到
  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：

  4-methoxyphenyl 2-O-acetyl-4-O-benzyl-α-L-rhamnopyranoside 、 2-O-acetyl-3,4-di-O-benzyl-α-L-rhamnosyl 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98%的产率得到4-methoxyphenyl 2-O-acetyl-3,4-di-O-benzyl-α-L-rhamnopyranosyl-(1->3)-2-O-acetyl-4-O-benzyl-α-L-rhamnopyranoside
  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