DL-2-N-carbobenzoxamino-4-phosphonobutyric acid triethyl ester | 155179-93-4

• 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: DL-2-N-carbobenzoxamino-4-phosphonobutyric acid triethyl ester
• CAS: 155179-93-4
• 化学式: C₁₈H₂₈NO₇P
• 分子量: 401.397
• InChiKey: STQHWYWSIHHNJB-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.5
• 重原子数：
  27.0
• 可旋转键数：
  12.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  100.16
• 氢给体数：
  1.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  DL-2-N-carbobenzoxamino-4-phosphonobutyric acid triethyl ester 在 sodium hydroxide 作用下， 以 乙醇 、 水 为溶剂， 以320 mg的产率得到Z-Abu(PO3Et2)-OH
  参考文献：
  名称：

  Synthesis and separation of a diastereomeric pair of phosphonopeptide inhibitors of the cyclic AMP-dependent protein kinase catalytic subunit

  摘要：

  In this paper we report the establishment of a novel procedure to synthesize a nonhydrolyzable phosphonopeptide dead-end inhibitor of the catalytic subunit of cAMP-dependent protein kinase. This procedure has been optimized to maximize the peptide yield and gives a diastereomeric pair of heptapeptides that can be separated on a C-18 reverse phase HPLC column. The two peptides have been characterized by NMR and the ability of these peptides to inhibit the reaction of the catalytic subunit of cAMP-dependent protein kinase. Peptide A has a dissociation constant of 9 micromolar, and is a 10-fold better inhibitor as compared to peptide B. On the basis of this 10-fold greater inhibition afforded by peptide A, this peptide is assigned the all L-form configuration. It is expected that this procedure can easily be adapted to synthesize a variety of different peptide inhibitors which involve a nonhydrolyzable phosphate on an amino acid.

  DOI：

  10.1016/s0040-4020(01)85056-0
• 作为产物：
  描述：

  原甲酸三乙酯 、 2-(N-benzyloxycarbonylamino)-4-phosphonobutanoic acid 以80%的产率得到DL-2-N-carbobenzoxamino-4-phosphonobutyric acid triethyl ester
  参考文献：
  名称：

  Synthesis and separation of a diastereomeric pair of phosphonopeptide inhibitors of the cyclic AMP-dependent protein kinase catalytic subunit

  摘要：

  In this paper we report the establishment of a novel procedure to synthesize a nonhydrolyzable phosphonopeptide dead-end inhibitor of the catalytic subunit of cAMP-dependent protein kinase. This procedure has been optimized to maximize the peptide yield and gives a diastereomeric pair of heptapeptides that can be separated on a C-18 reverse phase HPLC column. The two peptides have been characterized by NMR and the ability of these peptides to inhibit the reaction of the catalytic subunit of cAMP-dependent protein kinase. Peptide A has a dissociation constant of 9 micromolar, and is a 10-fold better inhibitor as compared to peptide B. On the basis of this 10-fold greater inhibition afforded by peptide A, this peptide is assigned the all L-form configuration. It is expected that this procedure can easily be adapted to synthesize a variety of different peptide inhibitors which involve a nonhydrolyzable phosphate on an amino acid.

  DOI：

  10.1016/s0040-4020(01)85056-0