N-(5-(Boc-amino)pentyl)hept-6-ynamide | 934220-54-9

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: N-(5-(Boc-amino)pentyl)hept-6-ynamide
• 英文别名: 6-heptynoic acid-(5-(Boc)amino-pentyl)-amide；tert-butyl N-[5-(hept-6-ynoylamino)pentyl]carbamate
• CAS: 934220-54-9
• 化学式: C₁₇H₃₀N₂O₃
• 分子量: 310.437
• InChiKey: DOFICTGGGBZCFR-UHFFFAOYSA-N

物化性质

• 沸点：
  494.7±30.0 °C(Predicted)
• 密度：
  0.997±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  22
• 可旋转键数：
  12
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.76
• 拓扑面积：
  67.4
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  N-(5-(Boc-amino)pentyl)hept-6-ynamide 在 盐酸 作用下， 以 1,4-二氧六环 为溶剂， 反应 5.0h， 以75%的产率得到N-(5-aminopentyl)hept-6-ynamide hydrochloride
  参考文献：
  名称：

  Activity-Based Protein Profiling Reagents for Protein Arginine Deiminase 4 (PAD4):  Synthesis and in vitro Evaluation of a Fluorescently Labeled Probe

  摘要：

  Protein arginine deiminase 4 (PAD4), which catalyzes the post-translational conversion of peptidyl arginine to peptidyl citrulline, is widely regarded as one of the best new targets for the development of a novel rheumatoid arthritis therapeutic. In addition to its presumed role in this disease, PAD4 is also a calcium-dependent histone deiminase that acts as a transcriptional co-repressor. Herein we describe the design, synthesis, and in vitro evaluation of two fluorescently labeled activity-based protein profiling (ABPP) reagents that specifically and irreversibly modify the active, that is, calcium-bound, form PAD4 with equal affinity to previously described small molecule chemical probes of PAD4 function. These fluorescently tagged ABPPs will be useful for identifying the conditions under which this enzyme is activated in vivo and may prove to be useful RA diagnostics.

  DOI：

  10.1021/ja0656907
• 作为产物：
  描述：

  6-庚炔酸 在 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 三乙胺 作用下， 以 甲醇 、 二氯甲烷 为溶剂， 反应 21.0h， 生成 N-(5-(Boc-amino)pentyl)hept-6-ynamide
  参考文献：
  名称：

  Activity-Based Protein Profiling Reagents for Protein Arginine Deiminase 4 (PAD4):  Synthesis and in vitro Evaluation of a Fluorescently Labeled Probe

  摘要：

  Protein arginine deiminase 4 (PAD4), which catalyzes the post-translational conversion of peptidyl arginine to peptidyl citrulline, is widely regarded as one of the best new targets for the development of a novel rheumatoid arthritis therapeutic. In addition to its presumed role in this disease, PAD4 is also a calcium-dependent histone deiminase that acts as a transcriptional co-repressor. Herein we describe the design, synthesis, and in vitro evaluation of two fluorescently labeled activity-based protein profiling (ABPP) reagents that specifically and irreversibly modify the active, that is, calcium-bound, form PAD4 with equal affinity to previously described small molecule chemical probes of PAD4 function. These fluorescently tagged ABPPs will be useful for identifying the conditions under which this enzyme is activated in vivo and may prove to be useful RA diagnostics.

  DOI：

  10.1021/ja0656907

文献信息

• WO2007/56389
  申请人：——

  公开号：——

  公开（公告）日：——
• Activity-Based Protein Profiling Reagents for Protein Arginine Deiminase 4 (PAD4):  Synthesis and in vitro Evaluation of a Fluorescently Labeled Probe
  作者：Yuan Luo、Bryan Knuckley、Monica Bhatia、Perry J. Pellechia、Paul R. Thompson

  DOI：10.1021/ja0656907

  日期：2006.11.1

  Protein arginine deiminase 4 (PAD4), which catalyzes the post-translational conversion of peptidyl arginine to peptidyl citrulline, is widely regarded as one of the best new targets for the development of a novel rheumatoid arthritis therapeutic. In addition to its presumed role in this disease, PAD4 is also a calcium-dependent histone deiminase that acts as a transcriptional co-repressor. Herein we describe the design, synthesis, and in vitro evaluation of two fluorescently labeled activity-based protein profiling (ABPP) reagents that specifically and irreversibly modify the active, that is, calcium-bound, form PAD4 with equal affinity to previously described small molecule chemical probes of PAD4 function. These fluorescently tagged ABPPs will be useful for identifying the conditions under which this enzyme is activated in vivo and may prove to be useful RA diagnostics.