H2N-Trp(Boc)-Tyr-OBn | 918902-96-2

• 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: H2N-Trp(Boc)-Tyr-OBn
• CAS: 918902-96-2
• 化学式: C₃₂H₃₅N₃O₆
• 分子量: 557.646
• InChiKey: BTOIZWGYNNREIG-SVBPBHIXSA-N

物化性质

• 密度：
  1.23±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.47
• 重原子数：
  41.0
• 可旋转键数：
  9.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.28
• 拓扑面积：
  132.88
• 氢给体数：
  3.0
• 氢受体数：
  8.0

反应信息

• 作为反应物：
  描述：

  H2N-Trp(Boc)-Tyr-OBn 在 potassium carbonate 、 sodium iodide 作用下， 以 四氢呋喃 、 N,N-二甲基甲酰胺 、 丙酮 为溶剂， 反应 12.13h， 生成 benzyl (12S,15S)-12-((1-(tert-butoxycarbonyl)-1H-indol-3-yl)methyl)-10,13-dioxo-2-oxa-11,14-diaza-1(1,4)-benzenacyclohexadecaphane-15-carboxylate
  参考文献：
  名称：

  Structure–activity studies of cyclic ketone inhibitors of the serine protease plasmin: Design, synthesis, and biological activity

  摘要：

  Three series of cyclic ketone inhibitors were synthesized and evaluated against the serine protease plasmin. Peptide inhibitors that incorporated 3-oxotetrahydrofuran and 3-oxotetrahydrothiophene 1,1-dioxide groups had the highest activities. Alkylamino substituents, which were designed to bind in the S1 subsite of plasmin, were attached to the inhibitors. Compounds 5c and 5g, which incorporated 6-aminohexyl substituents, were found to be optimal and demonstrated IC50 values in the low micromolar range. Incorporating conformationally constrained peptide segments into the inhibitors did not improve their activities. (c) 2006 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2006.08.040
• 作为产物：
  描述：

  Fmoc-L-色氨酸(Boc)-OH 在 哌啶 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 N,N-二异丙基乙胺 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 37.0h， 生成 H2N-Trp(Boc)-Tyr-OBn
  参考文献：
  名称：

  Structure–activity studies of cyclic ketone inhibitors of the serine protease plasmin: Design, synthesis, and biological activity

  摘要：

  Three series of cyclic ketone inhibitors were synthesized and evaluated against the serine protease plasmin. Peptide inhibitors that incorporated 3-oxotetrahydrofuran and 3-oxotetrahydrothiophene 1,1-dioxide groups had the highest activities. Alkylamino substituents, which were designed to bind in the S1 subsite of plasmin, were attached to the inhibitors. Compounds 5c and 5g, which incorporated 6-aminohexyl substituents, were found to be optimal and demonstrated IC50 values in the low micromolar range. Incorporating conformationally constrained peptide segments into the inhibitors did not improve their activities. (c) 2006 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2006.08.040