2-iodoethyl 2-O-(3-azido-2,3,6-trideoxy-α-L-ribo-hexopyranosyl)-β-D-glucopyranoside | 499115-52-5

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 2-iodoethyl 2-O-(3-azido-2,3,6-trideoxy-α-L-ribo-hexopyranosyl)-β-D-glucopyranoside
• CAS: 499115-52-5
• 化学式: C₁₄H₂₄IN₃O₈
• 分子量: 489.264
• InChiKey: FHIRATPFPVDPEA-RRITXHOZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.56
• 重原子数：
  26.0
• 可旋转键数：
  7.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  166.6
• 氢给体数：
  4.0
• 氢受体数：
  9.0

反应信息

• 作为反应物：
  描述：

  N-alloc-tri-O-allyl vancomycin aglycon allyl ester 、 2-iodoethyl 2-O-(3-azido-2,3,6-trideoxy-α-L-ribo-hexopyranosyl)-β-D-glucopyranoside 在 caesium carbonate 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 12.0h， 以82%的产率得到
  参考文献：
  名称：

  Structural requirements for VanA activity of vancomycin analogues

  摘要：

  We have prepared several sets of glycopeptide analogues in order to probe the molecular basis for the activity of derivatives that overcome vanA resistance. The results described in this paper provide compelling evidence that good vanA activity is due to a mechanism of action that does not involve peptide binding. Hypothesizing that this mechanism of action involves an interaction of the disaccharide portion of vancomycin analogues with bacterial transglycosylases, we have prepared a compound in which the vancomycin aglycone is coupled to a known transglycosylase inhibitor that is structurally unrelated to the disaccharides that have been previously investigated. The activity of this compound is excellent. This work provides a clear prescription for the design of better glycopeptide analogues. (C) 2002 Published by Elsevier Science Ltd.

  DOI：

  10.1016/s0040-4020(02)00743-3
• 作为产物：
  描述：

  2-chloroethyl 2-O-(3-azido-4-O-acetyl-2,3,6-trideoxy-L-ribo-hexopyranosyl)-3,4,6-tri-O-acetyl-β-D-glucopyranoside 在 sodium methylate 、 sodium iodide 作用下， 以 甲醇 、 丙酮 为溶剂， 反应 75.5h， 生成 2-iodoethyl 2-O-(3-azido-2,3,6-trideoxy-α-L-ribo-hexopyranosyl)-β-D-glucopyranoside
  参考文献：
  名称：

  Structural requirements for VanA activity of vancomycin analogues

  摘要：

  We have prepared several sets of glycopeptide analogues in order to probe the molecular basis for the activity of derivatives that overcome vanA resistance. The results described in this paper provide compelling evidence that good vanA activity is due to a mechanism of action that does not involve peptide binding. Hypothesizing that this mechanism of action involves an interaction of the disaccharide portion of vancomycin analogues with bacterial transglycosylases, we have prepared a compound in which the vancomycin aglycone is coupled to a known transglycosylase inhibitor that is structurally unrelated to the disaccharides that have been previously investigated. The activity of this compound is excellent. This work provides a clear prescription for the design of better glycopeptide analogues. (C) 2002 Published by Elsevier Science Ltd.

  DOI：

  10.1016/s0040-4020(02)00743-3