[1-<13CH3>]-1,3,3-trimethyl-2-hydroxymethylcyclohexene | 233694-19-4

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: [1-<13CH3>]-1,3,3-trimethyl-2-hydroxymethylcyclohexene
• CAS: 233694-19-4
• 化学式: C₁₀H₁₈O
• 分子量: 155.241
• InChiKey: QWNGCDQJLXENDZ-OUBTZVSYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.51
• 重原子数：
  11.0
• 可旋转键数：
  1.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.8
• 拓扑面积：
  20.23
• 氢给体数：
  1.0
• 氢受体数：
  1.0

反应信息

• 作为反应物：
  描述：

  [1-<13CH3>]-1,3,3-trimethyl-2-hydroxymethylcyclohexene 在 pyridinium chlorochromate 作用下， 以 吡啶 、 二氯甲烷 为溶剂， 反应 2.0h， 以71%的产率得到[2-<13>CH3]-β-cyclocitral
  参考文献：
  名称：

  摘要：

  Purpose: Vitamin A (retinol) and its metabolites comprise the natural retinoids. While the biological action of these molecules are thought to be primarily mediated by ca. 55 kDa nuclear retinoic acid receptors, a number of structurally similar 15-20 kDa proteins are involved in the transport, and possibly metabolism, of these compounds. The milk protein beta-lactoglobulin B (beta-LG) is an 18 kDa protein which binds retinol and may be involved in oral delivery of retinol to neonates. beta-LG also binds drugs and other natural products and is of potential interest as a protective delivery vehicle. Methods: To examine the conformation of the model retinoid beta-ionone both in solution and when bound to beta-LG, NMR and computational methods have been employed. Results: Taken together, NMR studies of beta-ionone in solution measuring scalar and dipolar coupling, as well as CHARMm calculations, suggest beta-ionone prefers a slightly twisted 6-s-cis conformation. Isotope-edited NMR studies of 13C-labeled beta-ionones bound to beta-LG, primarily employing the HMQC-NOE experiment, suggest beta-ionone also binds to beta-LG in its 6-s-cis conformation. Conclusions: The methods employed here allow estimates of protein-bound ligand conformation. However, additional sites of ligand labeling will be necessary to aid in binding site localization.

  DOI：

  10.1023/a:1018860221492
• 作为产物：
  描述：

  [1-<13>CH3]-1,3,3-trimethyl-2-carbomethoxycyclohexene 在 lithium aluminium tetrahydride 作用下， 以 乙醚 为溶剂， 反应 4.0h， 以60%的产率得到[1-<13CH3>]-1,3,3-trimethyl-2-hydroxymethylcyclohexene
  参考文献：
  名称：

  摘要：

  Purpose: Vitamin A (retinol) and its metabolites comprise the natural retinoids. While the biological action of these molecules are thought to be primarily mediated by ca. 55 kDa nuclear retinoic acid receptors, a number of structurally similar 15-20 kDa proteins are involved in the transport, and possibly metabolism, of these compounds. The milk protein beta-lactoglobulin B (beta-LG) is an 18 kDa protein which binds retinol and may be involved in oral delivery of retinol to neonates. beta-LG also binds drugs and other natural products and is of potential interest as a protective delivery vehicle. Methods: To examine the conformation of the model retinoid beta-ionone both in solution and when bound to beta-LG, NMR and computational methods have been employed. Results: Taken together, NMR studies of beta-ionone in solution measuring scalar and dipolar coupling, as well as CHARMm calculations, suggest beta-ionone prefers a slightly twisted 6-s-cis conformation. Isotope-edited NMR studies of 13C-labeled beta-ionones bound to beta-LG, primarily employing the HMQC-NOE experiment, suggest beta-ionone also binds to beta-LG in its 6-s-cis conformation. Conclusions: The methods employed here allow estimates of protein-bound ligand conformation. However, additional sites of ligand labeling will be necessary to aid in binding site localization.

  DOI：

  10.1023/a:1018860221492