2-oxoethyl β-D-galactopyranosyl-(1→4)-β-D-glucopyranoside-O-2-[2-[2-(biotinylaminoethoxy)ethoxy]ethoxy]-4-[3-(trifluoromethyl)-3H-diazirin-3-yl]benzyloxime

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 生物素及其衍生物
• 英文名称: 2-oxoethyl β-D-galactopyranosyl-(1→4)-β-D-glucopyranoside-O-2-[2-[2-(biotinylaminoethoxy)ethoxy]ethoxy]-4-[3-(trifluoromethyl)-3H-diazirin-3-yl]benzyloxime
• 英文别名: 5-[(3aS,4S,6aR)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]-N-[2-[2-[2-[2-[[(Z)-[(2S,3R,4S,5R)-2-acetamido-3,5,6-trihydroxy-4-[(2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyhexylidene]amino]oxymethyl]-5-[3-(trifluoromethyl)diazirin-3-yl]phenoxy]ethoxy]ethoxy]ethyl]pentanamide
• 化学式: C₃₉H₅₈F₃N₇O₁₆S
• 分子量: 969.988
• InChiKey: FTAGJRXOHSJPHB-VFRLNIIWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.4
• 重原子数：
  66
• 可旋转键数：
  28
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.74
• 拓扑面积：
  359
• 氢给体数：
  11
• 氢受体数：
  23

反应信息

• 作为产物：
  描述：

  Affilight-CHO 在 三乙胺 、 三氟乙酸 作用下， 以 二氯甲烷 、 甲苯 、 乙腈 为溶剂， 反应 21.0h， 生成 2-oxoethyl β-D-galactopyranosyl-(1→4)-β-D-glucopyranoside-O-2-[2-[2-(biotinylaminoethoxy)ethoxy]ethoxy]-4-[3-(trifluoromethyl)-3H-diazirin-3-yl]benzyloxime 、 2-oxoethyl β-D-galactopyranosyl-(1→4)-β-D-glucopyranoside-O-2-[2-[2-(biotinylaminoethoxy)ethoxy]ethoxy]-4-[3-(trifluoromethyl)-3H-diazirin-3-yl]benzyloxime
  参考文献：
  名称：

  The development of new molecular tools containing a chemically synthesized carbohydrate ligand for the elucidation of carbohydrate roles via photoaffinity labeling: Carbohydrate–protein interactions are affected by the structures of the glycosidic bonds and the reducing-end sugar

  摘要：

  Photoaffinity labeling technology is a highly efficient method for cloning carbohydrate-binding proteins. When the carbohydrate probes are synthesized according to conventional methods, however, the reducing terminus of the sugar is opened to provide an acyclic structure. Our continued efforts to solve this problem led to the development of new molecular tools with an oligosaccharide structure that contains a phenyldiazirine group for the elucidation of carbohydrate-protein interactions. We investigated whether carbohydrate-lectin interactions are affected by differences in the glycosidic formation and synthesized three types of molecular tools containing Galp-GlcpNAc disaccharide ligands and a photoreactive group (1, 2, 3). Photoaffinity labeling validated the recognition of the new ligand by different glycosidic bonds. Photoaffinity labeling also demonstrated that both the reducing end sugar and non-reducing end sugar recognized the Erythrina cristagalli agglutinin.

  DOI：

  10.1016/j.bmc.2014.06.049

文献信息

• One-Step Synthesis of Biotinyl Photoprobes from Unprotected Carbohydrates
  作者：Yasumaru Hatanaka、Uwe Kempin、Park Jong-Jip

  DOI：10.1021/jo000414a

  日期：2000.9.1

  A simple and versatile approach for the preparation of carbohydrate photoprobes has been developed. By a single-step reaction at 37 degrees C, a biotinylated carbene-generating unit was introduced to the reducing end of unprotected carbohydrates. Micromole quantities of N-acetyllactosamine, Lewis X trisaccharide, and sialyl Lewis X tetrasaccharide were easily converted to their biotinylated photoreactive analogues, which enabled the nonradioisotopic chemiluminescent detection of the photolabeled products. Thus, a sequence of lectin photoaffinity labeling, from the probe synthesis to the detection of labeled protein, was readily accomplished within one week. Our strategy may be applicable to any aldehyde-bearing ligand.
• The development of new molecular tools containing a chemically synthesized carbohydrate ligand for the elucidation of carbohydrate roles via photoaffinity labeling: Carbohydrate–protein interactions are affected by the structures of the glycosidic bonds and the reducing-end sugar
  作者：Isao Ohtsuka、Yutaka Sadakane、Noriyasu Hada、Mari Higuchi、Toshiyuki Atsumi、Nobuko Kakiuchi

  DOI：10.1016/j.bmc.2014.06.049

  日期：2014.8

  Photoaffinity labeling technology is a highly efficient method for cloning carbohydrate-binding proteins. When the carbohydrate probes are synthesized according to conventional methods, however, the reducing terminus of the sugar is opened to provide an acyclic structure. Our continued efforts to solve this problem led to the development of new molecular tools with an oligosaccharide structure that contains a phenyldiazirine group for the elucidation of carbohydrate-protein interactions. We investigated whether carbohydrate-lectin interactions are affected by differences in the glycosidic formation and synthesized three types of molecular tools containing Galp-GlcpNAc disaccharide ligands and a photoreactive group (1, 2, 3). Photoaffinity labeling validated the recognition of the new ligand by different glycosidic bonds. Photoaffinity labeling also demonstrated that both the reducing end sugar and non-reducing end sugar recognized the Erythrina cristagalli agglutinin.