phenyl 3,4,6-tri-O-benzoyl-1-thio-α-D-mannopyranoside | 1332524-18-1

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: phenyl 3,4,6-tri-O-benzoyl-1-thio-α-D-mannopyranoside
• 英文别名: [(2R,3R,4R,5S,6R)-3,4-dibenzoyloxy-5-hydroxy-6-phenylsulfanyloxan-2-yl]methyl benzoate
• CAS: 1332524-18-1
• 化学式: C₃₃H₂₈O₈S
• 分子量: 584.647
• InChiKey: VALYXMBAPXLERT-DXTPWFDXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.4
• 重原子数：
  42
• 可旋转键数：
  12
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.18
• 拓扑面积：
  134
• 氢给体数：
  1
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  phenyl 3,4,6-tri-O-benzoyl-1-thio-α-D-mannopyranoside 在 N-溴代丁二酰亚胺(NBS) 、 水 作用下， 以 二氯甲烷 、 丙酮 为溶剂， 反应 3.5h， 生成 2-O-acetyl-3,4,6-tri-O-benzoyl-α-D-mannopyranosyl-(1->2)-3,4,6-tri-O-benzoyl-α-D-mannopyranose
  参考文献：
  名称：

  Convergent Synthesis of Homogeneous Glc₁Man₉GlcNAc₂-Protein and Derivatives as Ligands of Molecular Chaperones in Protein Quality Control

  摘要：

  A detailed understanding of the molecular mechanism of chaperone-assisted protein quality control is often hampered by the lack of well-defined homogeneous glycoprotein probes. We describe here a highly convergent chemoenzymatic synthesis of the monoglucosylated glycoforms of bovine ribonuclease (RNase) as specific ligands of lectin-like chaperones calnexin (CNX) and calreticulin (CRT) that are known to recognize the monoglucosylated high-mannose oligosaccharide component of glycoproteins in protein folding. The synthesis of a selectively modified glycoform Gal(1)Glc(1)Man(9)GlcNAc(2)-RNase was accomplished by chemical synthesis of a large N-glycan oxazoline and its subsequent enzymatic ligation to GlcNAc-RNase under the catalysis of a glycosynthase. Selective removal of the terminal galactose by a beta-galactosidase gave the Glc(1)Man(9)GlcNAc(2)-RNase glycoform in excellent yield. CD spectroscopic analysis and RNA-hydrolyzing assay indicated that the synthetic RNase glycoforms maintained essentially the same global conformations and were fully active as the natural bovine ribonudease B. SPR binding studies revealed that the Glc(1)Man(9)GlcNAc(2)-RNase had high affinity to lectin CRT, while the synthetic Man(9)GlcNAc(2)-RNase glycoform and natural RNase B did not show CRT-binding activity. These results confirmed the essential role of the glucose moiety in the chaperone molecular recognition. Interestingly, the galactose-masked glycoform Gal(1)Glc(1)Man(9)GlcNAc(2)-RNase also showed significant affinity to lectin CRT, suggesting that a galactose beta-1,4-linked to the key glucose moiety does not significantly block the lectin binding. These synthetic homogeneous glycoprotein probes should be valuable for a detailed mechanistic study on how molecular chaperones work in concert to distinguish between misfolded and folded glycoproteins in the protein quality control cycle.

  DOI：

  10.1021/ja204831z
• 作为产物：
  描述：

  苯硫酚 在 甲醇 、 三氟化硼乙醚 、 乙酰氯 作用下， 以 二氯甲烷 为溶剂， 反应 27.0h， 生成 phenyl 3,4,6-tri-O-benzoyl-1-thio-α-D-mannopyranoside
  参考文献：
  名称：

  Convergent Synthesis of Homogeneous Glc₁Man₉GlcNAc₂-Protein and Derivatives as Ligands of Molecular Chaperones in Protein Quality Control

  摘要：

  A detailed understanding of the molecular mechanism of chaperone-assisted protein quality control is often hampered by the lack of well-defined homogeneous glycoprotein probes. We describe here a highly convergent chemoenzymatic synthesis of the monoglucosylated glycoforms of bovine ribonuclease (RNase) as specific ligands of lectin-like chaperones calnexin (CNX) and calreticulin (CRT) that are known to recognize the monoglucosylated high-mannose oligosaccharide component of glycoproteins in protein folding. The synthesis of a selectively modified glycoform Gal(1)Glc(1)Man(9)GlcNAc(2)-RNase was accomplished by chemical synthesis of a large N-glycan oxazoline and its subsequent enzymatic ligation to GlcNAc-RNase under the catalysis of a glycosynthase. Selective removal of the terminal galactose by a beta-galactosidase gave the Glc(1)Man(9)GlcNAc(2)-RNase glycoform in excellent yield. CD spectroscopic analysis and RNA-hydrolyzing assay indicated that the synthetic RNase glycoforms maintained essentially the same global conformations and were fully active as the natural bovine ribonudease B. SPR binding studies revealed that the Glc(1)Man(9)GlcNAc(2)-RNase had high affinity to lectin CRT, while the synthetic Man(9)GlcNAc(2)-RNase glycoform and natural RNase B did not show CRT-binding activity. These results confirmed the essential role of the glucose moiety in the chaperone molecular recognition. Interestingly, the galactose-masked glycoform Gal(1)Glc(1)Man(9)GlcNAc(2)-RNase also showed significant affinity to lectin CRT, suggesting that a galactose beta-1,4-linked to the key glucose moiety does not significantly block the lectin binding. These synthetic homogeneous glycoprotein probes should be valuable for a detailed mechanistic study on how molecular chaperones work in concert to distinguish between misfolded and folded glycoproteins in the protein quality control cycle.

  DOI：

  10.1021/ja204831z

文献信息

• Synthesis of an O-sulfo LewisX analog as glycolipid antigen
  作者：Shuhei Ueno、Shigeomi Horito

  DOI：10.1016/j.carres.2011.06.027

  日期：2011.10

  The title compound containing dihydroceramide as a ligand for CD1d was accomplished using the mannosyl, glucosaminyl, and fucosyl donors, and a sphinganine analogue, as suitable building blocks. The 2-O-unprotected mannosyl donor was coupled effectively with the sphinganine analog to afford the mannnosyl sphinganine derivative. The coupling of the glucosaminyl donor with the mannnosyl sphinganine acceptor required triflic acid as a promoter and the promoter change to silver triflate led to the undesired glycal production. The reduction of azide group using Zn powder was the key process, in which the amount of acetic acid was restricted to avoid the benzoyl migration and N-trichloroacetyl deprotection. The trisaccharide glycolipid was sulfonated at the 3-position of fucose moiety. (C) 2011 Elsevier Ltd. All rights reserved.