n-pent-4-enyl 2,3,4-tri-O-acetyl-α-L-rhamnopyranoside | 1239318-71-8

• 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: n-pent-4-enyl 2,3,4-tri-O-acetyl-α-L-rhamnopyranoside
• 英文别名: pent-4-enyl 2,3,4-tri-O-acetyl-α-L-rhamnopyranoside
• CAS: 1239318-71-8
• 化学式: C₁₇H₂₆O₈
• 分子量: 358.389
• InChiKey: OZEFJZGUCDLOJI-MJQUHVBXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.51
• 重原子数：
  25.0
• 可旋转键数：
  8.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  97.36
• 氢给体数：
  0.0
• 氢受体数：
  8.0

反应信息

• 作为反应物：
  描述：

  n-pent-4-enyl 2,3,4-tri-O-acetyl-α-L-rhamnopyranoside 在 ruthenium trichloride 、 sodium periodate 、 水 作用下， 以 二氯甲烷 、 乙腈 为溶剂， 反应 18.0h， 以98%的产率得到4-(((2R,3R,4R,5S,6S)-3,4,5-triacetoxy-6-methyltetrahydro-2H-pyran-2-yl)oxy)butanoic acid
  参考文献：
  名称：

  Synthesis of a Single-Molecule l-Rhamnose-Containing Three-Component Vaccine and Evaluation of Antigenicity in the Presence of Anti-l-Rhamnose Antibodies

  摘要：

  Carbohydrates are generally considered to be poorly immunogenic. Therefore, new approaches for enhancing their immunogenicity are important for the development of carbohydrates as vaccine components. We hypothesized that conjugation of an L-rhamnose (Rha) moiety to a carbohydrate antigen would enhance the antigenicity of the antigen in mice possessing anti-Rha antibodies via an antibody-dependent antigen uptake mechanism. To explore this hypothesis, we synthesized a single-molecule three-component vaccine containing the GalNAc-O-Thr (Tn) tumor-specific antigen, a 20 amino acid helper T-cell epitope (YAF) derived from an outer-membrane protein of Neisseria meningitides, and a Rha moiety. The vaccine was synthesized by automated Fmoc-based solid-phase peptide synthesis and deacetylated by brief treatment with NaOMe. Groups of female BALB/c mice were immunized and boosted with Rha-ovalbumin (Rha-OVA) formulated with either TiterMax Gold or Sigma Adjuvant System for a period of 35 days in order to determine optimal conditions for generating anti-Rha titers in mice. Anti-Rha antibody titers were > 100 fold higher in groups of mice immunized with Rha-OVA than in the control groups. Mice producing anti-Rha were challenged with Rha-YAF-Tn or YAF-Tn. Sera collected from the groups initially immunized with Rha-OVA and later challenged with Rha-YAF-Tn showed a 2-fold increase in anti-Tn titer at 1/100 serum dilution relative to mice not immunized with Rha-OVA. An in vitro T-cell proliferation study using cells primed with either Rha-YAF-Tn or YAF-Tn was done to examine possible differences in antigen uptake and presentation due to anti-Rha antibody and chemical modification. Proliferation of T cells was stimulated by a 10-fold lower antigen concentration in the presence of Rha antibodies. The results strongly suggest that T cells present in the spleen were presented with higher concentrations of Rha-YAF-Tn as a result of the presence of the anti-Rha antibodies.

  DOI：

  10.1021/ja107029z
• 作为产物：
  描述：

  L-rhamnopyranose 在 吡啶 、 三氟化硼乙醚 作用下， 以 二氯甲烷 为溶剂， 反应 24.0h， 生成 n-pent-4-enyl 2,3,4-tri-O-acetyl-α-L-rhamnopyranoside
  参考文献：
  名称：

  Organoboron-Promoted Regioselective Glycosylations in the Synthesis of a Saponin-Derived Pentasaccharide from Spergularia ramosa

  摘要：

  Organoboron-mediated regioselective glycosylations were employed as key steps in the total synthesis of a branched pentasaccharide from a saponin natural product. The ability to use organoboron activation to differentiate OH groups in an unprotected glycosyl acceptor, followed by substrate-controlled reactions of the obtained disaccharide, enabled a streamlining of the synthesis relative to a protective group-based approach. This study revealed a matching/mismatching effect of the relative configuration of donor and acceptor on the efficiency of a regioselective glycosylation reaction, a problem that was solved through the development of a novel boronic acid-amine copromoter system for glycosyl acceptor activation.

  DOI：

  10.1021/acs.joc.5b00950

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.