N-(3-azidopropyl)-2,3-dihydroxybenzamide

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: N-(3-azidopropyl)-2,3-dihydroxybenzamide
• 化学式: C₁₀H₁₂N₄O₃
• 分子量: 236.23
• InChiKey: KWUCRWUCONVTAK-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.3
• 重原子数：
  17
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  83.9
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  N-(3-azidopropyl)-2,3-dihydroxybenzamide 、 乙酸酐 在 吡啶 作用下， 反应 2.0h， 以54%的产率得到N-(3-azidopropyl)-2,3-diacetoxybenzamide
  参考文献：
  名称：

  Modified Galacto‐ or Fuco‐Clusters Exploiting the Siderophore Pathway to Inhibit the LecA‐ or LecB‐Associated Virulence ofPseudomonas aeruginosa

  摘要：

  AbstractGalacto‐ and fuco‐clusters conjugated with one to three catechol or hydroxamate motifs were synthesised to target LecA and LecB lectins of Pseudomonas aeruginosa (PA) localised in the outer membrane and inside the bacterium. The resulting glycocluster–pseudosiderophore conjugates were evaluated as Trojan horses to cross the outer membrane of PA by iron transport. The data suggest that glycoclusters with catechol moieties are able to hijack the iron transport, whereas those with hydroxamates showed strong nonspecific interactions. Mono‐ and tricatechol galactoclusters (G1C and G3C) were evaluated as inhibitors of infection by PA in comparison with the free galactocluster (G0). All of them exhibited an inhibitory effect between 46 to 75 % at 100 μM, with a higher potency than G0. This result shows that LecA localised in the outer membrane of PA is involved in the infection mechanism.

  DOI：

  10.1002/cbic.202000490
• 作为产物：
  描述：

  3-叠氮基丙胺 、 苯甲酸,二羟基- 在 N,N-二异丙基乙胺 、 (benzotriazo-1-yloxy)tris(dimethylamino)phosphonium hexafluorophosphate 作用下， 以 二氯甲烷 为溶剂， 反应 4.0h， 以50%的产率得到N-(3-azidopropyl)-2,3-dihydroxybenzamide
  参考文献：
  名称：

  Modified Galacto‐ or Fuco‐Clusters Exploiting the Siderophore Pathway to Inhibit the LecA‐ or LecB‐Associated Virulence ofPseudomonas aeruginosa

  摘要：

  AbstractGalacto‐ and fuco‐clusters conjugated with one to three catechol or hydroxamate motifs were synthesised to target LecA and LecB lectins of Pseudomonas aeruginosa (PA) localised in the outer membrane and inside the bacterium. The resulting glycocluster–pseudosiderophore conjugates were evaluated as Trojan horses to cross the outer membrane of PA by iron transport. The data suggest that glycoclusters with catechol moieties are able to hijack the iron transport, whereas those with hydroxamates showed strong nonspecific interactions. Mono‐ and tricatechol galactoclusters (G1C and G3C) were evaluated as inhibitors of infection by PA in comparison with the free galactocluster (G0). All of them exhibited an inhibitory effect between 46 to 75 % at 100 μM, with a higher potency than G0. This result shows that LecA localised in the outer membrane of PA is involved in the infection mechanism.

  DOI：

  10.1002/cbic.202000490

文献信息

• Modified Galacto‐ or Fuco‐Clusters Exploiting the Siderophore Pathway to Inhibit the LecA‐ or LecB‐Associated Virulence of<i>Pseudomonas aeruginosa</i>
  作者：Mimouna Madaoui、Olivier Vidal、Albert Meyer、Mathieu Noël、Jean‐Marie Lacroix、Jean‐Jacques Vasseur、Alberto Marra、François Morvan

  DOI：10.1002/cbic.202000490

  日期：2020.12

  AbstractGalacto‐ and fuco‐clusters conjugated with one to three catechol or hydroxamate motifs were synthesised to target LecA and LecB lectins of Pseudomonas aeruginosa (PA) localised in the outer membrane and inside the bacterium. The resulting glycocluster–pseudosiderophore conjugates were evaluated as Trojan horses to cross the outer membrane of PA by iron transport. The data suggest that glycoclusters with catechol moieties are able to hijack the iron transport, whereas those with hydroxamates showed strong nonspecific interactions. Mono‐ and tricatechol galactoclusters (G1C and G3C) were evaluated as inhibitors of infection by PA in comparison with the free galactocluster (G0). All of them exhibited an inhibitory effect between 46 to 75 % at 100 μM, with a higher potency than G0. This result shows that LecA localised in the outer membrane of PA is involved in the infection mechanism.