Fmoc-(S)-3-amino-4-(6-chloroindol-3-yl)butyric acid | 1147129-73-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: Fmoc-(S)-3-amino-4-(6-chloroindol-3-yl)butyric acid
• CAS: 1147129-73-4
• 化学式: C₂₇H₂₃ClN₂O₄
• 分子量: 474.944
• InChiKey: JFZOUFBXECDWHA-SFHVURJKSA-N

物化性质

• 沸点：
  742.9±60.0 °C(predicted)
• 密度：
  1.379±0.06 g/cm3(Temp: 20 °C; Press: 760 Torr)(predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  5.75
• 重原子数：
  34.0
• 可旋转键数：
  7.0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.19
• 拓扑面积：
  91.42
• 氢给体数：
  3.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  、 Fmoc-(S)-3-amino-4-(6-chloroindol-3-yl)butyric acid 、 芴甲氧羰基-L-β-高亮氨酸 、 Fmoc-L-beta-高苯丙氨酸 、 Fmoc-L-beta-高异亮氨酸 、 Fmoc-L-beta-高谷氨酸 6-叔丁酯 、 (S)-6-Amino-3-(9H-fluoren-9-ylmethoxycarbonylamino)-hexanoic acid 在 哌啶 、 benzotriazol-1-yloxyl-tris-(pyrrolidino)-phosphonium hexafluorophosphate 、 1-羟基苯并三唑 、 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 0.23h， 生成 β53-13
  参考文献：
  名称：

  β-Peptides with improved affinity for hDM2 and hDMX

  摘要：

  We previously described a series of 3(14)-helical beta-peptides that bind the hDM2 protein and inhibit its interaction with a p53-derived peptide in vitro. Here we present a detailed characterization of the interaction of these peptides with hDM2 and report two new beta-peptides in which non-natural side chains have been substituted into the hDM2-recognition epitope. These peptides feature both improved affinity and inhibitory potency in fluorescence polarization and ELISA assays. Additionally, one of the new beta-peptides also binds the hDM2- related protein, hDMX, which has been identified as another key therapeutic target for activation of the p53 pathway in tumors. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2009.01.039
• 作为产物：
  描述：

  重氮甲烷 、 Fmoc-6-氯-L-色氨酸 在 氯化亚砜 作用下， 以22%的产率得到Fmoc-(S)-3-amino-4-(6-chloroindol-3-yl)butyric acid
  参考文献：
  名称：

  β-Peptides with improved affinity for hDM2 and hDMX

  摘要：

  We previously described a series of 3(14)-helical beta-peptides that bind the hDM2 protein and inhibit its interaction with a p53-derived peptide in vitro. Here we present a detailed characterization of the interaction of these peptides with hDM2 and report two new beta-peptides in which non-natural side chains have been substituted into the hDM2-recognition epitope. These peptides feature both improved affinity and inhibitory potency in fluorescence polarization and ELISA assays. Additionally, one of the new beta-peptides also binds the hDM2- related protein, hDMX, which has been identified as another key therapeutic target for activation of the p53 pathway in tumors. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2009.01.039