2-trimethylsilylethyl 4-(2,3,4,6-tetra-O-acetyl-α-D-mannopyranosyl)-2-ene-2-(N-tert-butyloxycarbonyl)butenoate | 540754-35-6

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: 2-trimethylsilylethyl 4-(2,3,4,6-tetra-O-acetyl-α-D-mannopyranosyl)-2-ene-2-(N-tert-butyloxycarbonyl)butenoate
• CAS: 540754-35-6
• 化学式: C₂₈H₄₅NO₁₃Si
• 分子量: 631.75
• InChiKey: YNAVIBDVNLQOEX-FXEFVXDJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.79
• 重原子数：
  43.0
• 可旋转键数：
  12.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  179.06
• 氢给体数：
  1.0
• 氢受体数：
  13.0

反应信息

• 作为反应物：
  描述：

  2-trimethylsilylethyl 4-(2,3,4,6-tetra-O-acetyl-α-D-mannopyranosyl)-2-ene-2-(N-tert-butyloxycarbonyl)butenoate 在 {(1,5-cyclooctadiene)Rh(1,2-bis((2R,5R)-2,5-diethylphospholano)benzene)}triflate 氢气 作用下， 以 四氢呋喃 为溶剂， 25.0 ℃ 、620.52 kPa 条件下， 反应 48.0h， 以99%的产率得到2-trimethylsilylethyl 4-(2,3,4,6-tetra-O-acetyl-α-D-mannopyranosyl)-2-(N-tert-butyloxycarbonyl)butanoate
  参考文献：
  名称：

  Solid-Phase Synthesis for the Identification of High-Affinity Bivalent Lectin Ligands

  摘要：

  The development of carbohydrate-based therapeutics has been frustrated by the low affinities that characterize protein-carbohydrate complexation. Because of the oligomeric nature of most lectins, the use of multivalency may offer a successful strategy for the creation of high-affinity ligands. The solid-phase evaluation of libraries of peptide-linked multivalent ligands facilitates rapid examination of a large fraction of linker structure space. If such solid-phase assays are to replicate solution binding behavior, the potential for intermolecular bivalent binding on bead surfaces must be eliminated. Here we report the solid-phase synthesis and analysis of peptide-linked, spatially segregated mono- and bivalent ligands for the legume lectin concanavalin A. Bead shaving protocols were used for the creation of beads displaying spatially segregated binding sequences on the surface of Tentagel resins. The same ligands were also synthesized on PEGA resin to determine the effect of ligand presentation on solid-phase binding. While we set out to determine the lower limit of assay sensitivity, the unexpected observation that intermolecular bivalent ligand binding is enhanced for bivalent ligands relative to monovalent ligands allowed direct observation of the level of surface blocking required to prevent intermolecular bivalent ligand binding. For a protein with binding sites separated by 65 A, approximately 99.9% of Tentagel(1) surface sites and 99.99% of the total sites on a PEGA bead must be blocked to prevent intermolecular bivalent binding. We also report agglutination and calorimetric solution-phase binding studies of mono- and bivalent peptide-linked ligands.

  DOI：

  10.1021/jo0207271
• 作为产物：
  描述：

  2-(trimethylsilyl)ethyl 2-((tert-butoxycarbonyl)amino)-2-(dimethoxyphosphoryl)acetate 、 [(2R,3R,4R,5R,6R)-3,4,5-triacetyloxy-6-(2-oxoethyl)oxan-2-yl]methyl acetate 在 1,1,2,3-四甲基胍 作用下， 以 四氢呋喃 为溶剂， 反应 0.75h， 以68%的产率得到2-trimethylsilylethyl 4-(2,3,4,6-tetra-O-acetyl-α-D-mannopyranosyl)-2-ene-2-(N-tert-butyloxycarbonyl)butenoate
  参考文献：
  名称：

  Solid-Phase Synthesis for the Identification of High-Affinity Bivalent Lectin Ligands

  摘要：

  The development of carbohydrate-based therapeutics has been frustrated by the low affinities that characterize protein-carbohydrate complexation. Because of the oligomeric nature of most lectins, the use of multivalency may offer a successful strategy for the creation of high-affinity ligands. The solid-phase evaluation of libraries of peptide-linked multivalent ligands facilitates rapid examination of a large fraction of linker structure space. If such solid-phase assays are to replicate solution binding behavior, the potential for intermolecular bivalent binding on bead surfaces must be eliminated. Here we report the solid-phase synthesis and analysis of peptide-linked, spatially segregated mono- and bivalent ligands for the legume lectin concanavalin A. Bead shaving protocols were used for the creation of beads displaying spatially segregated binding sequences on the surface of Tentagel resins. The same ligands were also synthesized on PEGA resin to determine the effect of ligand presentation on solid-phase binding. While we set out to determine the lower limit of assay sensitivity, the unexpected observation that intermolecular bivalent ligand binding is enhanced for bivalent ligands relative to monovalent ligands allowed direct observation of the level of surface blocking required to prevent intermolecular bivalent ligand binding. For a protein with binding sites separated by 65 A, approximately 99.9% of Tentagel(1) surface sites and 99.99% of the total sites on a PEGA bead must be blocked to prevent intermolecular bivalent binding. We also report agglutination and calorimetric solution-phase binding studies of mono- and bivalent peptide-linked ligands.

  DOI：

  10.1021/jo0207271