(4R)-N-(3-((2-dodecanamidoethyl)amino)-3-oxopropyl)-2-(4-methoxyphenyl)-5,5-dimethyl-1,3-dioxane-4-carboxamide | 1357265-80-5

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: (4R)-N-(3-((2-dodecanamidoethyl)amino)-3-oxopropyl)-2-(4-methoxyphenyl)-5,5-dimethyl-1,3-dioxane-4-carboxamide
• CAS: 1357265-80-5
• 化学式: C₃₁H₅₁N₃O₆
• 分子量: 561.762
• InChiKey: FSADAISJANAQFI-MBCWZBCWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.8
• 重原子数：
  40.0
• 可旋转键数：
  19.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  114.99
• 氢给体数：
  3.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  (4R)-N-(3-((2-dodecanamidoethyl)amino)-3-oxopropyl)-2-(4-methoxyphenyl)-5,5-dimethyl-1,3-dioxane-4-carboxamide 在 盐酸 作用下， 以 四氢呋喃 、 水 为溶剂， 反应 1.0h， 以78%的产率得到
  参考文献：
  名称：

  Resin-based investigation of acyl carrier protein interaction networks in Escherichia coli

  摘要：

  Protein-protein interactions play an integral role in metabolic regulation. Elucidation of these networks is complicated by the changing identity of the proteins themselves. Here we demonstrate a resin-based technique that leverages the unique tools for acyl carrier protein (ACP) modification with non-hydrolyzable linkages. ACPs from Escherichia coli and Shewanella oneidensis MR-1 are bound to Affigel-15 with varying acyl groups attached and introduced to proteomic samples. Isolation of these binding partners is followed by MudPIT analysis to identify each interactome with the variable of ACP-tethered substrates. These techniques allow for investigation of protein interaction networks with the changing identity of a given protein target. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2011.10.053
• 作为产物：
  描述：

  (4R)-N-(3-((2-aminoethyl)amino)-3-oxopropyl)-2-(4-methoxyphenyl)-5,5-dimethyl-1,3-dioxane-4-carboxamide 、 月桂酰氯 在 吡啶 作用下， 以 二氯甲烷 为溶剂， 反应 2.0h， 以43%的产率得到(4R)-N-(3-((2-dodecanamidoethyl)amino)-3-oxopropyl)-2-(4-methoxyphenyl)-5,5-dimethyl-1,3-dioxane-4-carboxamide
  参考文献：
  名称：

  Resin-based investigation of acyl carrier protein interaction networks in Escherichia coli

  摘要：

  Protein-protein interactions play an integral role in metabolic regulation. Elucidation of these networks is complicated by the changing identity of the proteins themselves. Here we demonstrate a resin-based technique that leverages the unique tools for acyl carrier protein (ACP) modification with non-hydrolyzable linkages. ACPs from Escherichia coli and Shewanella oneidensis MR-1 are bound to Affigel-15 with varying acyl groups attached and introduced to proteomic samples. Isolation of these binding partners is followed by MudPIT analysis to identify each interactome with the variable of ACP-tethered substrates. These techniques allow for investigation of protein interaction networks with the changing identity of a given protein target. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2011.10.053