Methyl 6-O-acetyl-4-O-levulinyl-2,3-di-O-methyl-α-D-glucopyranoside | 332083-28-0

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 糖脂
• 英文名称: Methyl 6-O-acetyl-4-O-levulinyl-2,3-di-O-methyl-α-D-glucopyranoside
• CAS: 332083-28-0
• 化学式: C₁₆H₂₆O₉
• 分子量: 362.377
• InChiKey: ZPUNAMZLCMUCIX-JZYAIQKZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.23
• 重原子数：
  25.0
• 可旋转键数：
  9.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.81
• 拓扑面积：
  106.59
• 氢给体数：
  0.0
• 氢受体数：
  9.0

反应信息

• 作为反应物：
  描述：

  Methyl 6-O-acetyl-4-O-levulinyl-2,3-di-O-methyl-α-D-glucopyranoside 在 硫酸 、 三氟化硼乙醚 作用下， 以 溶剂黄146 、 甲苯 为溶剂， 反应 4.5h， 生成 Ethyl 6-O-acetyl-4-O-levulinyl-2,3-di-O-methyl-1-thio-β-D-glucopyranoside
  参考文献：
  名称：

  Experimental Proof for the Structure of a Thrombin-Inhibiting Heparin Molecule

  摘要：

  Kinetic studies of thrombin inhibition by antithrombin in the presence of heparin have shown that thrombin binds to heparin in a preformed heparin - antithrombin complex. To study the relative position of the thrombin binding domain and the antithrombin binding domain on a heparin molecule we have designed and synthesized heparin mimetics which structurally are very similar to the genuine polysaccharide. Their inhibitory properties with respect to factor Xa and thrombin provide experimental evidence that in heparin the thrombin binding domain must be located at the nonreducing end of the antithrombin binding domain to observe thrombin inhibition. As expected, factor Xa inhibition is not affected by elongation of the antithrombin binding pentasaccharide sequence, regardless of the position in which this elongation takes place.

  DOI：

  10.1002/1521-3765(20010216)7:4<858::aid-chem858>3.0.co;2-n
• 作为产物：
  描述：

  甲基 2,3-二-O-甲基-alpha-D-吡喃葡萄糖苷 在 吡啶 、 4-二甲氨基吡啶 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 作用下， 以 1,4-二氧六环 为溶剂， 反应 5.5h， 生成 Methyl 6-O-acetyl-4-O-levulinyl-2,3-di-O-methyl-α-D-glucopyranoside
  参考文献：
  名称：

  Experimental Proof for the Structure of a Thrombin-Inhibiting Heparin Molecule

  摘要：

  Kinetic studies of thrombin inhibition by antithrombin in the presence of heparin have shown that thrombin binds to heparin in a preformed heparin - antithrombin complex. To study the relative position of the thrombin binding domain and the antithrombin binding domain on a heparin molecule we have designed and synthesized heparin mimetics which structurally are very similar to the genuine polysaccharide. Their inhibitory properties with respect to factor Xa and thrombin provide experimental evidence that in heparin the thrombin binding domain must be located at the nonreducing end of the antithrombin binding domain to observe thrombin inhibition. As expected, factor Xa inhibition is not affected by elongation of the antithrombin binding pentasaccharide sequence, regardless of the position in which this elongation takes place.

  DOI：

  10.1002/1521-3765(20010216)7:4<858::aid-chem858>3.0.co;2-n