Boc-Val-p-NO2Phe-Pro-OH | 1268722-95-7

• 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: Boc-Val-p-NO2Phe-Pro-OH
• 英文别名: Boc-Val-Phe(4-NO2)-Pro-OH；(2S)-1-[(2S)-2-[[(2S)-3-methyl-2-[(2-methylpropan-2-yl)oxycarbonylamino]butanoyl]amino]-3-(4-nitrophenyl)propanoyl]pyrrolidine-2-carboxylic acid
• CAS: 1268722-95-7
• 化学式: C₂₄H₃₄N₄O₈
• 分子量: 506.556
• InChiKey: ZNONLGQUSMYPNJ-FHWLQOOXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.8
• 重原子数：
  36
• 可旋转键数：
  10
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.58
• 拓扑面积：
  171
• 氢给体数：
  3
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  Boc-Val-p-NO2Phe-Pro-OH 、 N-乙酰基-N'-FMOC-L-赖氨酸 在 1-羟基苯并三唑 、 N,N'-二异丙基碳二亚胺 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 生成
  参考文献：
  名称：

  Biotin Ergopeptide Probes for Dopamine Receptors

  摘要：

  The incorporation of chemical modifications into the structure of bioactive compounds is often difficult because the biological properties of the new molecules must be retained with respect to the native ligand. Ergopeptides, with their high affinities at D-1 and D-2 dopamine receptors, are particularly complex examples. Here, we report the systematic derivatization of two ergopeptides with different peptide-based spacers and their evaluation by radioligand binding assays. Selected spacer-containing ergopeptides with minimal biological alteration and a proper anchoring point were further derivatized with a biotin reporter. Detailed characterization studies identified 13 as a biotin ergopeptide maintaining high affinity and agonist behavior at dopamine receptors, being a useful tool for the study of heteromers involving D1R, D2R, or D3R.

  DOI：

  10.1021/jm101566d
• 作为产物：
  描述：

  BOC-L-4-硝基苯丙氨酸 、 (±)-N-Fmoc-3-哌啶甲酸 Fmoc-DL-哌啶甲酸 、 FMOC-L-4-氟苯丙氨酸 在 2-chlorotrityl chloride polystyrene resin 、 1-羟基苯并三唑 、 N,N'-二异丙基碳二亚胺 、 哌啶 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 以3.58 g的产率得到Boc-Val-p-NO2Phe-Pro-OH
  参考文献：
  名称：

  Biotin Ergopeptide Probes for Dopamine Receptors

  摘要：

  The incorporation of chemical modifications into the structure of bioactive compounds is often difficult because the biological properties of the new molecules must be retained with respect to the native ligand. Ergopeptides, with their high affinities at D-1 and D-2 dopamine receptors, are particularly complex examples. Here, we report the systematic derivatization of two ergopeptides with different peptide-based spacers and their evaluation by radioligand binding assays. Selected spacer-containing ergopeptides with minimal biological alteration and a proper anchoring point were further derivatized with a biotin reporter. Detailed characterization studies identified 13 as a biotin ergopeptide maintaining high affinity and agonist behavior at dopamine receptors, being a useful tool for the study of heteromers involving D1R, D2R, or D3R.

  DOI：

  10.1021/jm101566d