Allyl 2-O-acetyl-6-O-benzyl-3-O-methyl-α-D-glucopyranoside | 332083-23-5

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: Allyl 2-O-acetyl-6-O-benzyl-3-O-methyl-α-D-glucopyranoside
• CAS: 332083-23-5
• 化学式: C₁₉H₂₆O₇
• 分子量: 366.411
• InChiKey: WXMVIYCBZFDSJY-FQBWVUSXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.44
• 重原子数：
  26.0
• 可旋转键数：
  9.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  83.45
• 氢给体数：
  1.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  Allyl 2-O-acetyl-6-O-benzyl-3-O-methyl-α-D-glucopyranoside 在 (1,5-cyclooctadiene)[bis(methyldiphenylphosphine)]iridium(I) hexafluorophosphate N-溴代丁二酰亚胺(NBS) 、 4 A molecular sieve 、 叔丁基二甲硅基三氟甲磺酸酯 、 氢气 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 反应 0.84h， 生成
  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：

  Allyl 4,6-O-benzylidene-3-O-methyl-α-D-glucopyranoside 在 三乙基硅烷 、 4-二甲氨基吡啶 、 三乙胺 、 三氟乙酸 、 三氟乙酸酐 作用下， 以 二氯甲烷 、 1,2-二氯乙烷 为溶剂， 反应 6.0h， 生成 Allyl 2-O-acetyl-6-O-benzyl-3-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