1-Amino-3-guanidinomethyl-cyclobutanecarboxylic acid | 184103-39-7

• 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: 1-Amino-3-guanidinomethyl-cyclobutanecarboxylic acid
• CAS: 184103-39-7
• 化学式: C₇H₁₄N₄O₂
• 分子量: 186.214
• InChiKey: ZMPRCSAHGQJZNT-VOVMAIODSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.34
• 重原子数：
  13.0
• 可旋转键数：
  3.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  125.22
• 氢给体数：
  5.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  1-Amino-3-guanidinomethyl-cyclobutanecarboxylic acid 在 potassium hydrogencarbonate 、 三氟乙酸 作用下， 以 1,4-二氧六环 为溶剂， 反应 4.25h， 生成 1-({(S)-1-[(S)-6-Amino-2-((2S,3R)-2-amino-3-hydroxy-butyrylamino)-hexanoyl]-pyrrolidine-2-carbonyl}-amino)-3-guanidinomethyl-cyclobutanecarboxylic 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：

  trans-1-(benzoylamino)-3-(hydroxymethyl)cyclobutane-1-N,N-pentamethylenecarboxamide 在 palladium on activated charcoal 盐酸 、 N,N,N',N'-tetramethylguanidinium azide 、 氢气 、 三乙胺 作用下， 以 乙醇 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 25.0~130.0 ℃ 、101.33 kPa 条件下， 反应 67.0h， 生成 1-Amino-3-guanidinomethyl-cyclobutanecarboxylic 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