5-sulfanylpentanyl 4,6-dideoxy-4-(3-hydroxy-3-methylbutanamido)-β-D-glucopyranosyl-(1->3)-α-L-rhamnopyranoside | 1239318-63-8

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: 5-sulfanylpentanyl 4,6-dideoxy-4-(3-hydroxy-3-methylbutanamido)-β-D-glucopyranosyl-(1->3)-α-L-rhamnopyranoside
• 英文别名: N-[(2R,3S,4S,5R,6S)-6-[(2S,3S,4R,5R,6R)-3,5-dihydroxy-2-methyl-6-(5-sulfanylpentoxy)oxan-4-yl]oxy-4,5-dihydroxy-2-methyloxan-3-yl]-3-hydroxy-3-methylbutanamide
• CAS: 1239318-63-8
• 化学式: C₂₂H₄₁NO₁₀S
• 分子量: 511.634
• InChiKey: VORPQQSTQISUGR-JYNKNBEHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.9
• 重原子数：
  34
• 可旋转键数：
  11
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.95
• 拓扑面积：
  168
• 氢给体数：
  7
• 氢受体数：
  11

反应信息

• 作为产物：
  描述：

  5-thioacetylpentyl 4,6-dideoxy-4-(3-hydroxy-3-methylbutanamido)-β-D-glucopyranosyl-(1->3)-α-L-rhamnopyranoside 在 sodium methylate 作用下， 以 甲醇 为溶剂， 以97%的产率得到5-sulfanylpentanyl 4,6-dideoxy-4-(3-hydroxy-3-methylbutanamido)-β-D-glucopyranosyl-(1->3)-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

文献信息

• Molecular Analysis of Carbohydrate−Antibody Interactions: Case Study Using a <i>Bacillus anthracis</i> Tetrasaccharide
  作者：Matthias A. Oberli、Marco Tamborrini、Yu-Hsuan Tsai、Daniel B. Werz、Tim Horlacher、Alexander Adibekian、Dominik Gauss、Heiko M. Möller、Gerd Pluschke、Peter H. Seeberger

  DOI：10.1021/ja104027w

  日期：2010.8.4

  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.