N-[3-(2-Azido-ethyl)-1-(piperidine-1-carbonyl)-cyclobutyl]-benzamide | 184103-59-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: N-[3-(2-Azido-ethyl)-1-(piperidine-1-carbonyl)-cyclobutyl]-benzamide
• 英文别名: N-[3-(2-azidoethyl)-1-(piperidine-1-carbonyl)cyclobutyl]benzamide
• CAS: 184103-59-1
• 化学式: C₁₉H₂₅N₅O₂
• 分子量: 355.44
• InChiKey: LVGIPRPHEKSFTP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.4
• 重原子数：
  26
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.58
• 拓扑面积：
  63.8
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  N-[3-(2-Azido-ethyl)-1-(piperidine-1-carbonyl)-cyclobutyl]-benzamide 在 palladium on activated charcoal 盐酸 、 sodium sulfide 、 copper (II) carbonate hydroxide 、 sodium hydroxide 、 氢气 、 magnesium oxide 作用下， 以 乙醇 、 叔丁醇 为溶剂， 25.0~130.0 ℃ 、101.33 kPa 条件下， 反应 64.0h， 生成 1-[(2-Methylpropan-2-yl)oxycarbonylamino]-3-[2-(phenylmethoxycarbonylamino)ethyl]cyclobutane-1-carboxylic acid
  参考文献：
  名称：

  1-Aminocyclobutanecarboxylic Acid Derivatives as Novel Structural Elements in Bioactive Peptides:  Application to Tuftsin Analogs

  摘要：

  Four novel 2,4-methano amino acids (MAAs, 1-aminocyclobutane-1-carboxylic acids) were synthesized. These include the basic MAA analogs of lysine (16), ornithine (5), and arginine (6) and the neutral methanovaline (22), related to proline. The above MAAs, as well as the MAA analog of homothreonine (7), were incorporated into the peptide chain of the immuno-modulatory peptide tuftsin, Thr-Lys-Pro-Arg, known to enhance several biological activities mediated by phagocytic cells. The synthetic methano tuftsin analogs were assayed for their ability to stimulate interleukin-6 (IL-6) secretion by mouse peritoneal macrophages and for their stability in human serum toward enzymatic degradation. It was found that, at 2 x 10(-7) M, [MThr(1)]tuftsin (24) and an isomer of [MVal(3)]tuftsin (27a) were considerably more active than the parent peptide in augmentation of cytokine release. [MOrn(2)]Tuftsin (25) was equally potent. The analogs [MThr(1)]tuftsin (24) and [MOrn(2)]tuftsin (25), both pertaining to the proteolytically sensitive Thr-Lys bond of tuftsin, exhibited high resistance to enzymatic hydrolysis as compared to tuftsin. Using specific rabbit anti-tuftsin antibodies in a competitive enzyme-linked immunosorbent assay (ELISA) revealed that none of the MAA analogs can crossreact with tuftsin. It may indicate that the peptides assume global structures different than that of tuftsin.

  DOI：

  10.1021/jm960390t
• 作为产物：
  描述：

  Methanesulfonic acid 2-[3-benzoylamino-3-(piperidine-1-carbonyl)-cyclobutyl]-ethyl ester 在 N,N,N',N'-tetramethylguanidinium azide 作用下， 以 various solvent(s) 为溶剂， 反应 2.0h， 以34%的产率得到N-[3-(2-Azido-ethyl)-1-(piperidine-1-carbonyl)-cyclobutyl]-benzamide
  参考文献：
  名称：

  1-Aminocyclobutanecarboxylic Acid Derivatives as Novel Structural Elements in Bioactive Peptides:  Application to Tuftsin Analogs

  摘要：

  Four novel 2,4-methano amino acids (MAAs, 1-aminocyclobutane-1-carboxylic acids) were synthesized. These include the basic MAA analogs of lysine (16), ornithine (5), and arginine (6) and the neutral methanovaline (22), related to proline. The above MAAs, as well as the MAA analog of homothreonine (7), were incorporated into the peptide chain of the immuno-modulatory peptide tuftsin, Thr-Lys-Pro-Arg, known to enhance several biological activities mediated by phagocytic cells. The synthetic methano tuftsin analogs were assayed for their ability to stimulate interleukin-6 (IL-6) secretion by mouse peritoneal macrophages and for their stability in human serum toward enzymatic degradation. It was found that, at 2 x 10(-7) M, [MThr(1)]tuftsin (24) and an isomer of [MVal(3)]tuftsin (27a) were considerably more active than the parent peptide in augmentation of cytokine release. [MOrn(2)]Tuftsin (25) was equally potent. The analogs [MThr(1)]tuftsin (24) and [MOrn(2)]tuftsin (25), both pertaining to the proteolytically sensitive Thr-Lys bond of tuftsin, exhibited high resistance to enzymatic hydrolysis as compared to tuftsin. Using specific rabbit anti-tuftsin antibodies in a competitive enzyme-linked immunosorbent assay (ELISA) revealed that none of the MAA analogs can crossreact with tuftsin. It may indicate that the peptides assume global structures different than that of tuftsin.

  DOI：

  10.1021/jm960390t