2,5-di-O-allyl-D-mannaro-1,4:3,6-di-γ-lactone | 654072-04-5

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 内酯类
• 英文名称: 2,5-di-O-allyl-D-mannaro-1,4:3,6-di-γ-lactone
• CAS: 654072-04-5
• 化学式: C₁₂H₁₄O₆
• 分子量: 254.24
• InChiKey: XWCUBYPEEQEZHY-XKNYDFJKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.02
• 重原子数：
  18.0
• 可旋转键数：
  6.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  71.06
• 氢给体数：
  0.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  L-valine N-methylamide 、 2,5-di-O-allyl-D-mannaro-1,4:3,6-di-γ-lactone 以 二氯甲烷 为溶剂， 反应 50.0h， 以75%的产率得到(2S,3S,4S,5S)-N1,N6-bis[(1S)-2-methyl-2-(methylcarbamoyl)propyl]-2,5-di(allyloxy)-3,4-dihydroxyhexane-1,6-diamide
  参考文献：
  名称：

  C2-Symmetric inhibitors of Plasmodium falciparum plasmepsin II: synthesis and theoretical predictions

  摘要：

  A series of C-2-symmetric compounds with a mannitol-based scaffold has been investigated, both theoretically and experimentally, as Plm II inhibitors. Four different stereoisomers with either benzyloxy or allyloxy P1/P1' side chains were studied. Computational ranking of the binding affinities of the eight compounds was carried out using the linear interaction energy (LIE) method relying on a complex previously determined by crystallography. Within both series of isomers the theoretical binding energies were in agreement with the enzymatic measurements, illustrating the power of the LIE method for the prediction of ligand affinities prior to synthesis. The structural models of the enzyme-inhibitor complexes obtained from the MD simulations provided a basis for interpretation of further structure-activity relationships. Hence, the affinity of a structurally similar ligand, but with a different P2/P2' substituent was examined using the same procedure. The predicted improvement in binding constant agreed well with experimental results. (C) 2003 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(03)00339-0
• 作为产物：
  描述：

  2,2,2-三氯乙酰胺烯丙酯 、 D-mannaro-1,4:6,3-dilactone 在 三氟甲磺酸 作用下， 以 1,4-二氧六环 为溶剂， 反应 7.0h， 以51%的产率得到2,5-di-O-allyl-D-mannaro-1,4:3,6-di-γ-lactone
  参考文献：
  名称：

  C2-Symmetric inhibitors of Plasmodium falciparum plasmepsin II: synthesis and theoretical predictions

  摘要：

  A series of C-2-symmetric compounds with a mannitol-based scaffold has been investigated, both theoretically and experimentally, as Plm II inhibitors. Four different stereoisomers with either benzyloxy or allyloxy P1/P1' side chains were studied. Computational ranking of the binding affinities of the eight compounds was carried out using the linear interaction energy (LIE) method relying on a complex previously determined by crystallography. Within both series of isomers the theoretical binding energies were in agreement with the enzymatic measurements, illustrating the power of the LIE method for the prediction of ligand affinities prior to synthesis. The structural models of the enzyme-inhibitor complexes obtained from the MD simulations provided a basis for interpretation of further structure-activity relationships. Hence, the affinity of a structurally similar ligand, but with a different P2/P2' substituent was examined using the same procedure. The predicted improvement in binding constant agreed well with experimental results. (C) 2003 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(03)00339-0