N-[2-[(2R,3R,4R,5S,6R)-3,4-dihydroxy-6-(hydroxymethyl)-5-[(2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-2-yl]oxyethyl]-3-[methyl(pyridin-4-yl)amino]propanamide | 1004988-74-2

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: N-[2-[(2R,3R,4R,5S,6R)-3,4-dihydroxy-6-(hydroxymethyl)-5-[(2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-2-yl]oxyethyl]-3-[methyl(pyridin-4-yl)amino]propanamide
• CAS: 1004988-74-2
• 化学式: C₂₃H₃₇N₃O₁₂
• 分子量: 547.56
• InChiKey: PDOPXMMCUKNCCK-SJBFRSNJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4.2
• 重原子数：
  38
• 可旋转键数：
  12
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.74
• 拓扑面积：
  224
• 氢给体数：
  8
• 氢受体数：
  14

反应信息

• 作为产物：
  描述：

  3-<甲基(4-吡啶基)氨基>丙酸 、 2-aminoethyl β-D-galactopyranosyl-(1->4)-O-β-D-glucopyranoside 在 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 、 N,N-二异丙基乙胺 作用下， 以 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 10.0h， 生成 N-[2-[(2R,3R,4R,5S,6R)-3,4-dihydroxy-6-(hydroxymethyl)-5-[(2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-2-yl]oxyethyl]-3-[methyl(pyridin-4-yl)amino]propanamide
  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

文献信息

• Target-Specific Chemical Acylation of Lectins by Ligand-Tethered DMAP Catalysts
  作者：Yoichiro Koshi、Eiji Nakata、Masayoshi Miyagawa、Shinya Tsukiji、Tomohisa Ogawa、Itaru Hamachi

  DOI：10.1021/ja075684q

  日期：2008.1.1

  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.