5-azido-5-deoxy-1,2-O-isopropylidene-3-O-methoxymethyl-β-L-idofuranose | 845778-49-6

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 5-azido-5-deoxy-1,2-O-isopropylidene-3-O-methoxymethyl-β-L-idofuranose
• CAS: 845778-49-6
• 化学式: C₁₁H₁₉N₃O₆
• 分子量: 289.288
• InChiKey: NJKDXABEEKHPLU-SQXHDICFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.52
• 重原子数：
  20.0
• 可旋转键数：
  6.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  115.14
• 氢给体数：
  1.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  5-azido-5-deoxy-1,2-O-isopropylidene-3-O-methoxymethyl-β-L-idofuranose 在 Amberlite IR-120 、 sodium hydride 作用下， 以 四氢呋喃 、 水 、 N,N-二甲基甲酰胺 、 乙腈 为溶剂， 生成 5-azido-5-deoxy-6-O-(3-phenylpropyl)-3-O-methoxymethyl-β-L-idofuranose
  参考文献：
  名称：

  Probing the aglycon binding site of a β-glucosidase: a collection of C-1-modified 2,5-dideoxy-2,5-imino-d-mannitol derivatives and their structure–activity relationships as competitive inhibitors

  摘要：

  A range of new C-1 modified derivatives of the powerful glucosidase inhibitor 2,5-dideoxy-2,5-imino-D-mannitol has been synthesised and their biological activities probed with the beta-glucosidase from Agrobacterium sp. K-i values are compared with those of previously prepared close relatives. Findings suggest dramatic effects exerted by the aglycon binding site on substrate/ inhibitor binding. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2004.04.037
• 作为产物：
  描述：

  5-azido-6-O-tert-butyldimethylsilyl-5-deoxy-1,2-O-isopropylidene-β-L-idofuranose 在 四丁基氟化铵 、 N,N-二异丙基乙胺 作用下， 以 四氢呋喃 、 甲醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 31.0h， 生成 5-azido-5-deoxy-1,2-O-isopropylidene-3-O-methoxymethyl-β-L-idofuranose
  参考文献：
  名称：

  Probing the aglycon binding site of a β-glucosidase: a collection of C-1-modified 2,5-dideoxy-2,5-imino-d-mannitol derivatives and their structure–activity relationships as competitive inhibitors

  摘要：

  A range of new C-1 modified derivatives of the powerful glucosidase inhibitor 2,5-dideoxy-2,5-imino-D-mannitol has been synthesised and their biological activities probed with the beta-glucosidase from Agrobacterium sp. K-i values are compared with those of previously prepared close relatives. Findings suggest dramatic effects exerted by the aglycon binding site on substrate/ inhibitor binding. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2004.04.037