(S)-2-[N'-((S)-2-Benzyloxycarbonylamino-3-phenyl-propionyl)-hydrazino]-3-phenyl-propionic acid methyl ester | 205748-86-3

• 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: (S)-2-[N'-((S)-2-Benzyloxycarbonylamino-3-phenyl-propionyl)-hydrazino]-3-phenyl-propionic acid methyl ester
• CAS: 205748-86-3
• 化学式: C₂₇H₂₉N₃O₅
• 分子量: 475.544
• InChiKey: FWQVWQXTEKIGMC-ZEQRLZLVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.93
• 重原子数：
  35.0
• 可旋转键数：
  11.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.22
• 拓扑面积：
  105.76
• 氢给体数：
  3.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  (S)-2-[N'-((S)-2-Benzyloxycarbonylamino-3-phenyl-propionyl)-hydrazino]-3-phenyl-propionic acid methyl ester 在 palladium on activated charcoal 氢气 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 2.5h， 以83%的产率得到(S)-2-[N'-((S)-2-Amino-3-phenyl-propionyl)-hydrazino]-3-phenyl-propionic acid methyl ester
  参考文献：
  名称：

  Ribosome-Mediated Incorporation of Hydrazinophenylalanine into Modified Peptide and Protein Analogues

  摘要：

  (S)-alpha-Hydrazinophenylalanyl-tRNA(Phe), an amino acyl-tRNA derivative containing the unnatural amino acid (S)-alpha-hydrazinophenylalanine, was prepared in an effort to examine the stereochemical requirements of the A-site of the ribosome during in vitro protein synthesis. The (S)-alpha-hydrazinophenylalanine moiety was of interest because it contains two nucleophilic centers, the secondary nitrogen attached to Ca, which is normally acylated during the course of peptide bond formation, and the sterically less hindered primary nitrogen. To determine the position of acylation, (S)-alpha-hydrazinophenylalanyl-tRNA(Phe) was tested in an Escherichia coli in vitro protein biosynthesizing system lacking elongation factor G, such that only dipeptide products were formed. The dipeptide product mixture was analyzed by HPLC in direct comparison with authentic synthetic standards. The dipeptide assay utilizing (S)-alpha-hydrazinophenylalanyl-tRNA(Phe) as the A-site tRNA established that the analogue functioned well as an acceptor tRNA; HPLC analysis of the products showed that both dipeptides were formed in approximately equal amounts. When attached to a suppressor tRNA transcript, (S)-alpha-hydrazinophenylalanine was also incorporated into position 27 of dihydrofolate reductase in an E. coli protein synthesizing system by readthrough of a nonsense codon. This finding expands the currently accepted model of peptide bond formation at the ribosome and adds to the repertoire of peptide-like products shown to form at the peptidyltransferase center of the ribosome.

  DOI：

  10.1021/ja974066e
• 作为产物：
  描述：

  N-苄氧羰基-L-苯丙氨酸 、 在 1-羟基苯并三唑 、 三乙胺 、 N,N'-二环己基碳二亚胺 作用下， 生成 (S)-2-[N'-((S)-2-Benzyloxycarbonylamino-3-phenyl-propionyl)-hydrazino]-3-phenyl-propionic acid methyl ester
  参考文献：
  名称：

  Ribosome-Mediated Incorporation of Hydrazinophenylalanine into Modified Peptide and Protein Analogues

  摘要：

  (S)-alpha-Hydrazinophenylalanyl-tRNA(Phe), an amino acyl-tRNA derivative containing the unnatural amino acid (S)-alpha-hydrazinophenylalanine, was prepared in an effort to examine the stereochemical requirements of the A-site of the ribosome during in vitro protein synthesis. The (S)-alpha-hydrazinophenylalanine moiety was of interest because it contains two nucleophilic centers, the secondary nitrogen attached to Ca, which is normally acylated during the course of peptide bond formation, and the sterically less hindered primary nitrogen. To determine the position of acylation, (S)-alpha-hydrazinophenylalanyl-tRNA(Phe) was tested in an Escherichia coli in vitro protein biosynthesizing system lacking elongation factor G, such that only dipeptide products were formed. The dipeptide product mixture was analyzed by HPLC in direct comparison with authentic synthetic standards. The dipeptide assay utilizing (S)-alpha-hydrazinophenylalanyl-tRNA(Phe) as the A-site tRNA established that the analogue functioned well as an acceptor tRNA; HPLC analysis of the products showed that both dipeptides were formed in approximately equal amounts. When attached to a suppressor tRNA transcript, (S)-alpha-hydrazinophenylalanine was also incorporated into position 27 of dihydrofolate reductase in an E. coli protein synthesizing system by readthrough of a nonsense codon. This finding expands the currently accepted model of peptide bond formation at the ribosome and adds to the repertoire of peptide-like products shown to form at the peptidyltransferase center of the ribosome.

  DOI：

  10.1021/ja974066e