(2S)-2-amino-1-[(2R)-2-methylpyrrolidin-1-yl]-3-phenylpropan-1-one

• 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: (2S)-2-amino-1-[(2R)-2-methylpyrrolidin-1-yl]-3-phenylpropan-1-one
• 化学式: C₁₄H₂₀N₂O
• 分子量: 232.326
• InChiKey: PGARGXWKPXQVRY-YPMHNXCESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.57
• 重原子数：
  17.0
• 可旋转键数：
  3.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  46.33
• 氢给体数：
  1.0
• 氢受体数：
  2.0

反应信息

• 作为反应物：
  描述：

  (2S)-2-amino-1-[(2R)-2-methylpyrrolidin-1-yl]-3-phenylpropan-1-one 在 哌啶 、 N-羟基-7-氮杂苯并三氮唑 、 trimethylpyridine 、 N-[(dimethylamino)-3-oxo-1H-1,2,3-triazolo[4,5-b]pyridin-1-yl-methylene]-N-methylmethanaminium hexafluorophosphate 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 4.0h， 生成 L-methionyl-L-threonyl-L-methionyl-L-valyl-L-leucyl-L-seryl-L-phenylalanine (2R)-methylpyrrolidinyl amide
  参考文献：
  名称：

  Binding of peptides in solution by the Escherichia coli chaperone PapD as revealed using an inhibition ELISA and NMR spectroscopy

  摘要：

  PapD is the prototype member of a family of periplasmic chaperones which are required for assembly of virulence associated pili in pathogenic, gram-negative bacteria. In the present investigation, an ELISA has been developed for evaluation of compounds as inhibitors of PapD. Synthetic peptides, including an octamer, derived from the C-terminus of the pilus adhesin PapG were able to inhibit PapD in the ELISA. Evaluation of a panel of octapeptides in the ELISA, in combination with NMR studies, showed that the peptides were bound as extended beta-strands by PapD in aqueous solution. The PapD-peptide complex was stabilized by backbone to backbone hydrogen bonds and interactions involving three hydrophobic peptide side chains. This structural information, together with previous crystal structure data, provides a starting point in efforts to design and synthesize compounds which bind to chaperones and interfere with pilus assembly in pathogenic bacteria.

  DOI：

  10.1016/s0968-0896(98)00162-x
• 作为产物：
  描述：

  L-脯氨醇 在 palladium on activated charcoal 咪唑 、 盐酸 、 氢气 、 碘 、 O-(benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium tetrafluoroborate 、 三乙胺 、 三苯基膦 作用下， 以 乙醇 、 溶剂黄146 、 乙酸乙酯 、 N,N-二甲基甲酰胺 、 甲苯 为溶剂， 25.0 ℃ 、101.33 kPa 条件下， 反应 8.67h， 生成 (2S)-2-amino-1-[(2R)-2-methylpyrrolidin-1-yl]-3-phenylpropan-1-one
  参考文献：
  名称：

  Binding of peptides in solution by the Escherichia coli chaperone PapD as revealed using an inhibition ELISA and NMR spectroscopy

  摘要：

  PapD is the prototype member of a family of periplasmic chaperones which are required for assembly of virulence associated pili in pathogenic, gram-negative bacteria. In the present investigation, an ELISA has been developed for evaluation of compounds as inhibitors of PapD. Synthetic peptides, including an octamer, derived from the C-terminus of the pilus adhesin PapG were able to inhibit PapD in the ELISA. Evaluation of a panel of octapeptides in the ELISA, in combination with NMR studies, showed that the peptides were bound as extended beta-strands by PapD in aqueous solution. The PapD-peptide complex was stabilized by backbone to backbone hydrogen bonds and interactions involving three hydrophobic peptide side chains. This structural information, together with previous crystal structure data, provides a starting point in efforts to design and synthesize compounds which bind to chaperones and interfere with pilus assembly in pathogenic bacteria.

  DOI：

  10.1016/s0968-0896(98)00162-x

文献信息

• Binding of peptides in solution by the Escherichia coli chaperone PapD as revealed using an inhibition ELISA and NMR spectroscopy
  作者：Katarina Flemmer Karlsson、Björn Walse、Torbjörn Drakenberg、Sarbari Roy、Karl-Erik Bergquist、Jerome S. Pinkner、Scott J. Hultgren、Jan Kihlberg

  DOI：10.1016/s0968-0896(98)00162-x

  日期：1998.11

  PapD is the prototype member of a family of periplasmic chaperones which are required for assembly of virulence associated pili in pathogenic, gram-negative bacteria. In the present investigation, an ELISA has been developed for evaluation of compounds as inhibitors of PapD. Synthetic peptides, including an octamer, derived from the C-terminus of the pilus adhesin PapG were able to inhibit PapD in the ELISA. Evaluation of a panel of octapeptides in the ELISA, in combination with NMR studies, showed that the peptides were bound as extended beta-strands by PapD in aqueous solution. The PapD-peptide complex was stabilized by backbone to backbone hydrogen bonds and interactions involving three hydrophobic peptide side chains. This structural information, together with previous crystal structure data, provides a starting point in efforts to design and synthesize compounds which bind to chaperones and interfere with pilus assembly in pathogenic bacteria.