1-[(2-Methylpropan-2-yl)oxycarbonylamino]-3-[2-(phenylmethoxycarbonylamino)ethyl]cyclobutane-1-carboxylic acid | 184103-67-1

• 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: 1-[(2-Methylpropan-2-yl)oxycarbonylamino]-3-[2-(phenylmethoxycarbonylamino)ethyl]cyclobutane-1-carboxylic acid
• CAS: 184103-67-1
• 化学式: C₂₀H₂₈N₂O₆
• 分子量: 392.452
• InChiKey: ORNNOOFKADADRR-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  28
• 可旋转键数：
  10
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.55
• 拓扑面积：
  114
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  BOC-L-脯氨酸 、 N-Boc-O-苄基-L-苏氨酸 、 N-叔丁氧羰基-N'-甲苯磺酰基-L-精氨酸 、 1-[(2-Methylpropan-2-yl)oxycarbonylamino]-3-[2-(phenylmethoxycarbonylamino)ethyl]cyclobutane-1-carboxylic acid 生成 (2S)-2-[[(2S)-1-[3-(2-aminoethyl)-1-[[(2S,3R)-2-amino-3-hydroxybutanoyl]amino]cyclobutanecarbonyl]pyrrolidine-2-carbonyl]amino]-5-(diaminomethylideneamino)pentanoic 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：

  N-[3-Benzenesulfonyl-3-(2-hydroxy-ethyl)-1-(piperidine-1-carbonyl)-cyclobutyl]-benzamide 在 palladium on activated charcoal 盐酸 、 甲醇 、 sodium sulfide 、 copper (II) carbonate hydroxide 、 sodium hydroxide 、 sodium amalgam 、 N,N,N',N'-tetramethylguanidinium azide 、 氢气 、 4-甲基苯磺酸吡啶 、 magnesium oxide 、 三乙胺 作用下， 以 四氢呋喃 、 乙醇 、 二氯甲烷 、 叔丁醇 为溶剂， 25.0~130.0 ℃ 、101.33 kPa 条件下， 反应 226.0h， 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