4-(N-boc-L-prolinamido)phenol | 102284-28-6

• 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: 4-(N-boc-L-prolinamido)phenol
• CAS: 102284-28-6
• 化学式: C₁₆H₂₂N₂O₄
• 分子量: 306.362
• InChiKey: GMZVXUPDDNCMJS-ZDUSSCGKSA-N

物化性质

• 沸点：
  516.0±45.0 °C(Predicted)
• 密度：
  1?+-.0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.3
• 重原子数：
  22.0
• 可旋转键数：
  3.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  78.87
• 氢给体数：
  2.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  4-(N-boc-L-prolinamido)phenol 在 吡啶 、 盐酸 、 甲酸 作用下， 以 四氢呋喃 、 N,N-二甲基甲酰胺 为溶剂， 反应 9.0h， 生成 4-(L-prolinamido)phenyl N-isopropylcarbamate hydrochloride
  参考文献：
  名称：

  Peptidyl carbamates incorporating amino acid isosteres as novel elastase inhibitors

  摘要：

  The design and synthesis of 13 novel peptidyl carbamates are described. When tested for inhibitory activity toward porcine pancreatic elastase, trypsin, and chymotrypsin, six compounds were found to specifically inhibit elastase without affecting the other two serine proteases. All the active inhibitors had an amino acid isostere at the P1 position. Kinetic studies indicated that the inhibition was competitive with Ki values ranging from 4.23 X 10(-5) to 2.4 X 10(-6) M. The degree of inhibition was found to be dependent on the specificity of the peptide chain for the extended subsites on the enzyme as well as on the nature of P1'. Preliminary work on one inhibitor indicates that the inhibition is reversible and proceeds via the rapid formation of a strong enzyme-inhibitor complex, followed by slow acylation of the serine residue on the active site of the enzyme. Peptidyl carbamates represent a novel class of elastase inhibitors.

  DOI：

  10.1021/jm00158a025
• 作为产物：
  描述：

  对氨基苯酚 、 Boc-Pro-OH 在 N,N'-二环己基碳二亚胺 作用下， 以 四氢呋喃 为溶剂， 以40%的产率得到4-(N-boc-L-prolinamido)phenol
  参考文献：
  名称：

  Peptidyl carbamates incorporating amino acid isosteres as novel elastase inhibitors

  摘要：

  The design and synthesis of 13 novel peptidyl carbamates are described. When tested for inhibitory activity toward porcine pancreatic elastase, trypsin, and chymotrypsin, six compounds were found to specifically inhibit elastase without affecting the other two serine proteases. All the active inhibitors had an amino acid isostere at the P1 position. Kinetic studies indicated that the inhibition was competitive with Ki values ranging from 4.23 X 10(-5) to 2.4 X 10(-6) M. The degree of inhibition was found to be dependent on the specificity of the peptide chain for the extended subsites on the enzyme as well as on the nature of P1'. Preliminary work on one inhibitor indicates that the inhibition is reversible and proceeds via the rapid formation of a strong enzyme-inhibitor complex, followed by slow acylation of the serine residue on the active site of the enzyme. Peptidyl carbamates represent a novel class of elastase inhibitors.

  DOI：

  10.1021/jm00158a025