3,6,9,12,15,18,21,24,27,30-decaoxadotriacontane-1,32-diyl dimethanesulfonate | 928211-39-6

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机磺酸及其衍生物
• 英文名称: 3,6,9,12,15,18,21,24,27,30-decaoxadotriacontane-1,32-diyl dimethanesulfonate
• CAS: 928211-39-6
• 化学式: C₂₄H₅₀O₁₆S₂
• 分子量: 658.783
• InChiKey: HSWQTLWJRCOFMD-UHFFFAOYSA-N

物化性质

• 沸点：
  719.4±60.0 °C(Predicted)
• 密度：
  1.212±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -0.9
• 重原子数：
  42.0
• 可旋转键数：
  35.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  179.04
• 氢给体数：
  0.0
• 氢受体数：
  16.0

反应信息

• 作为反应物：
  描述：

  3,6,9,12,15,18,21,24,27,30-decaoxadotriacontane-1,32-diyl dimethanesulfonate 在 palladium on activated charcoal 氢气 、 sodium hydride 作用下， 以 四氢呋喃 、 乙醇 为溶剂， 反应 14.0h， 生成 二十一甘醇
  参考文献：
  名称：

  Dependence of Effective Molarity on Linker Length for an Intramolecular Protein−Ligand System

  摘要：

  This paper reports dissociation constants and "effective molarities" (M-eff) for the intramolecular binding of a ligand covalently attached to the surface of a protein by oligo(ethylene glycol) (EG(n)) linkers of different lengths (n = 0, 2, 5, 10, and 20) and compares these experimental values with theoretical estimates from polymer theory. As expected, the value of M-eff is lowest when the linker is too short (n = 0) to allow the ligand to bind noncovalently at the active site of the protein without strain, is highest when the linker is the optimal length (n = 2) to allow such binding to occur, and decreases monotonically as the length increases past this optimal value (but only by a factor of similar to 8 from n = 2 to n = 20). These experimental results are not compatible with a model in which the single bonds of the linker are completely restricted when the ligand has bound noncovalently to the active site of the protein, but they are quantitatively compatible with a model that treats the linker as a random-coil polymer. Calorimetry revealed that enthalpic interactions between the linker and the protein are not important in determining the thermodynamics of the system. Taken together, these results suggest that the manifestation of the linker in the thermodynamics of binding is exclusively entropic. The values of M-eff are, theoretically, intrinsic properties of the EG(n) linkers and can be used to predict the avidities of multivalent ligands with these linkers for multivalent proteins. The weak dependence of M-eff on linker length suggests that multivalent ligands containing flexible linkers that are longer than the spacing between the binding sites of a multivalent protein will be effective in binding, and that the use of flexible linkers with lengths somewhat greater than the optimal distance between binding sites is a justifiable strategy for the design of multivalent ligands.

  DOI：

  10.1021/ja066780e
• 作为产物：
  描述：

  五乙二醇单苄醚 在 palladium on activated charcoal 氢气 、 sodium hydride 、 三乙胺 作用下， 以 四氢呋喃 、 乙醇 、 二氯甲烷 为溶剂， 反应 16.0h， 生成 3,6,9,12,15,18,21,24,27,30-decaoxadotriacontane-1,32-diyl dimethanesulfonate
  参考文献：
  名称：

  Dependence of Effective Molarity on Linker Length for an Intramolecular Protein−Ligand System

  摘要：

  This paper reports dissociation constants and "effective molarities" (M-eff) for the intramolecular binding of a ligand covalently attached to the surface of a protein by oligo(ethylene glycol) (EG(n)) linkers of different lengths (n = 0, 2, 5, 10, and 20) and compares these experimental values with theoretical estimates from polymer theory. As expected, the value of M-eff is lowest when the linker is too short (n = 0) to allow the ligand to bind noncovalently at the active site of the protein without strain, is highest when the linker is the optimal length (n = 2) to allow such binding to occur, and decreases monotonically as the length increases past this optimal value (but only by a factor of similar to 8 from n = 2 to n = 20). These experimental results are not compatible with a model in which the single bonds of the linker are completely restricted when the ligand has bound noncovalently to the active site of the protein, but they are quantitatively compatible with a model that treats the linker as a random-coil polymer. Calorimetry revealed that enthalpic interactions between the linker and the protein are not important in determining the thermodynamics of the system. Taken together, these results suggest that the manifestation of the linker in the thermodynamics of binding is exclusively entropic. The values of M-eff are, theoretically, intrinsic properties of the EG(n) linkers and can be used to predict the avidities of multivalent ligands with these linkers for multivalent proteins. The weak dependence of M-eff on linker length suggests that multivalent ligands containing flexible linkers that are longer than the spacing between the binding sites of a multivalent protein will be effective in binding, and that the use of flexible linkers with lengths somewhat greater than the optimal distance between binding sites is a justifiable strategy for the design of multivalent ligands.

  DOI：

  10.1021/ja066780e