tert-butyl 4-(7-hydroxy-2-oxo-2H-chromene-3-carboxamido)butanoate | 1004988-90-2

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 香豆素及其衍生物
• 英文名称: tert-butyl 4-(7-hydroxy-2-oxo-2H-chromene-3-carboxamido)butanoate
• CAS: 1004988-90-2
• 化学式: C₁₈H₂₁NO₆
• 分子量: 347.368
• InChiKey: RRTPVOMLKFRRMX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.35
• 重原子数：
  25.0
• 可旋转键数：
  5.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.39
• 拓扑面积：
  105.84
• 氢给体数：
  2.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  tert-butyl 4-(7-hydroxy-2-oxo-2H-chromene-3-carboxamido)butanoate 在 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 1.0h， 生成
  参考文献：
  名称：

  Target-Specific Chemical Acylation of Lectins by Ligand-Tethered DMAP Catalysts

  摘要：

  Because sugar-binding proteins, so-called lectins, play important roles in many biological phenomena, the lectin-selective labeling should be useful for investigating biological processes involving lectins as well as providing molecular tools for analysis of saccharides and these derivatives. We describe herein a new strategy for lectin-selective labeling based on an acyl transfer reaction directed by ligand-tethered DIVIAP (4-dimethylaminopyridine). DIVIAP is an effective acyl transfer catalyst, which can activate an acyl ester for its transfer to a nucleophilic residue. To direct the acyl transfer reaction to a lectin of interest, we attached the DIVIAP to a saccharide ligand specific for the target lectin. It was clearly demonstrated by biochemical analyses that the target-selective labeling of Congerin II, an animal lectin having selective affinity for Lactose/LacNAc (N-acetyllactosamine), was achieved in the presence of Lac-tethered DMAPs and acyl donors containing probes such as fluorescent molecules or biotin. Conventional peptide mapping experiments using HPLC and tandem mass-mass analysis revealed that the acyl transfer reaction site-specifically occurred at Tyr 51 of Cong II. This strategy was successfully extended to other lectins by changing the ligand part of the ligand-tethered DMAP. We also demonstrated that this labeling method is applicable not only to purified lectin in test tubes, but also to crude mixtures such as E coli lysates or homogenized animal tissue samples expressing Congerin.

  DOI：

  10.1021/ja075684q
• 作为产物：
  描述：

  4-氨基酸叔丁酯 、 7-羟基香豆素-3-羧酸 在 (benzotriazo-1-yloxy)tris(dimethylamino)phosphonium hexafluorophosphate 、 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 1.0h， 以58%的产率得到tert-butyl 4-(7-hydroxy-2-oxo-2H-chromene-3-carboxamido)butanoate
  参考文献：
  名称：

  Target-Specific Chemical Acylation of Lectins by Ligand-Tethered DMAP Catalysts

  摘要：

  Because sugar-binding proteins, so-called lectins, play important roles in many biological phenomena, the lectin-selective labeling should be useful for investigating biological processes involving lectins as well as providing molecular tools for analysis of saccharides and these derivatives. We describe herein a new strategy for lectin-selective labeling based on an acyl transfer reaction directed by ligand-tethered DIVIAP (4-dimethylaminopyridine). DIVIAP is an effective acyl transfer catalyst, which can activate an acyl ester for its transfer to a nucleophilic residue. To direct the acyl transfer reaction to a lectin of interest, we attached the DIVIAP to a saccharide ligand specific for the target lectin. It was clearly demonstrated by biochemical analyses that the target-selective labeling of Congerin II, an animal lectin having selective affinity for Lactose/LacNAc (N-acetyllactosamine), was achieved in the presence of Lac-tethered DMAPs and acyl donors containing probes such as fluorescent molecules or biotin. Conventional peptide mapping experiments using HPLC and tandem mass-mass analysis revealed that the acyl transfer reaction site-specifically occurred at Tyr 51 of Cong II. This strategy was successfully extended to other lectins by changing the ligand part of the ligand-tethered DMAP. We also demonstrated that this labeling method is applicable not only to purified lectin in test tubes, but also to crude mixtures such as E coli lysates or homogenized animal tissue samples expressing Congerin.

  DOI：

  10.1021/ja075684q