4,6-dimethyl-N,N-dioctylpyridin-2-amine | 1421004-89-8

• 分子结构分类: 有机化合物 - 有机氮化合物
• 英文名称: 4,6-dimethyl-N,N-dioctylpyridin-2-amine
• CAS: 1421004-89-8
• 化学式: C₂₃H₄₂N₂
• 分子量: 346.6
• InChiKey: SPKOZUNQJSKZPW-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  7.23
• 重原子数：
  25.0
• 可旋转键数：
  15.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.78
• 拓扑面积：
  16.13
• 氢给体数：
  0.0
• 氢受体数：
  2.0

反应信息

• 作为反应物：
  描述：

  4,6-dimethyl-N,N-dioctylpyridin-2-amine 在 2-氨基吡啶 、 N-溴代丁二酰亚胺(NBS) 、 copper(I) bromide 作用下， 以 甲醇 、 二氯甲烷 、 N,N-二甲基乙酰胺 为溶剂， 反应 22.0h， 生成 5-methoxy-4,6-dimethyl-N,N-dioctylpyridin-2-amine
  参考文献：
  名称：

  Besting Vitamin E: Sidechain Substitution is Key to the Reactivity of Naphthyridinol Antioxidants in Lipid Bilayers

  摘要：

  A series of naphthyridinol analogs of alpha-tocopherol (alpha-TOH, right) with varying sidechain substitution was synthesized to determine how systematic changes in the lipophilicity of these potent antioxidants impact their radical-trapping activities in lipid bilayers, regenerability by water-soluble reductants, and binding to human tocopherol transport protein (TTP). The activities of the naphthyridinols were assayed in phosphatidylcholine unilamellar liposomes using a recently developed high-throughput assay that employs a boron dipyrromethene conjugate of alpha-TOH (H2B-PMHC) that undergoes fluorescence enhancement upon oxidation. The naphthyridinols afforded a dose-dependent protection of H2B-PMHC consistent with unprecedented peroxyl radical-trapping activity in lipid bilayers. While sidechain length and/or branching had no effect on their apparent reactivity, it dramatically impacted reaction stoichiometry, with more lipophilic compounds trapping two peroxyl radicals and more hydrophilic compounds trapping significantly less than one. It is suggested that the less lipophilic compounds autoxidize rapidly in the aqueous phase and that preferential partitioning of the more lipophilic compounds to the bilayer protects them from autoxidation. The cooperativity of a lipophilic naphthyridinol with water-soluble reducing agents was also studied in liposomes using H2B-PMHC and revealed superior regenerability by each of ascorbate, N-acetylcysteine, and urate when compared to alpha-TOH. Binding assays with human TTP, a key determinant of the bioavailability of the tocopherols, reveal that the naphthyiridinols can be very good ligands for the protein. In fact, naphthyridinols with sidechains of eight or more carbons had affinities for TTP which were similar to, and in one case alpha-fold better than, alpha-TOH.

  DOI：

  10.1021/ja309153x
• 作为产物：
  描述：

  1-溴辛烷 、 2-氨基-4,6-二甲基吡啶 在 sodium hydride 作用下， 以 四氢呋喃 为溶剂， 反应 4.5h， 以83%的产率得到4,6-dimethyl-N,N-dioctylpyridin-2-amine
  参考文献：
  名称：

  Besting Vitamin E: Sidechain Substitution is Key to the Reactivity of Naphthyridinol Antioxidants in Lipid Bilayers

  摘要：

  A series of naphthyridinol analogs of alpha-tocopherol (alpha-TOH, right) with varying sidechain substitution was synthesized to determine how systematic changes in the lipophilicity of these potent antioxidants impact their radical-trapping activities in lipid bilayers, regenerability by water-soluble reductants, and binding to human tocopherol transport protein (TTP). The activities of the naphthyridinols were assayed in phosphatidylcholine unilamellar liposomes using a recently developed high-throughput assay that employs a boron dipyrromethene conjugate of alpha-TOH (H2B-PMHC) that undergoes fluorescence enhancement upon oxidation. The naphthyridinols afforded a dose-dependent protection of H2B-PMHC consistent with unprecedented peroxyl radical-trapping activity in lipid bilayers. While sidechain length and/or branching had no effect on their apparent reactivity, it dramatically impacted reaction stoichiometry, with more lipophilic compounds trapping two peroxyl radicals and more hydrophilic compounds trapping significantly less than one. It is suggested that the less lipophilic compounds autoxidize rapidly in the aqueous phase and that preferential partitioning of the more lipophilic compounds to the bilayer protects them from autoxidation. The cooperativity of a lipophilic naphthyridinol with water-soluble reducing agents was also studied in liposomes using H2B-PMHC and revealed superior regenerability by each of ascorbate, N-acetylcysteine, and urate when compared to alpha-TOH. Binding assays with human TTP, a key determinant of the bioavailability of the tocopherols, reveal that the naphthyiridinols can be very good ligands for the protein. In fact, naphthyridinols with sidechains of eight or more carbons had affinities for TTP which were similar to, and in one case alpha-fold better than, alpha-TOH.

  DOI：

  10.1021/ja309153x