N-benzyloxycarbonyl-L-phenylalanyl-1-amino-3-(benzyloxy)-methoxypropan-2-ol

• 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: N-benzyloxycarbonyl-L-phenylalanyl-1-amino-3-(benzyloxy)-methoxypropan-2-ol
• 英文别名: benzyl N-[(2S)-1-[[2-hydroxy-3-(phenylmethoxymethoxy)propyl]amino]-1-oxo-3-phenylpropan-2-yl]carbamate
• 化学式: C₂₈H₃₂N₂O₆
• 分子量: 492.572
• InChiKey: NCXUEZNPYUKDRT-AMVUTOCUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.5
• 重原子数：
  36
• 可旋转键数：
  15
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  106
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  N-benzyloxycarbonyl-L-phenylalanyl-1-amino-3-(benzyloxy)-methoxypropan-2-ol 在 戴斯-马丁氧化剂 作用下， 以 二氯甲烷 为溶剂， 反应 2.0h， 以52%的产率得到N-benzyloxycarbonyl-L-phenylalanyl-1-amino-3-(benzyloxy)-methoxypropan-2-one
  参考文献：
  名称：

  Peptidyl and azapeptidyl methylketones as substrate analog inhibitors of papain and cathepsin B

  摘要：

  Peptidyl methylketones containing Phe, Tyr, Tyr(I) Tyr(I-2), Leu and Ile in P-2 were synthesized and tested as substrate analog reversible inhibitors of papain and bovine spleen cathepsin B. The most effective cathepsin B inhibitor contained Tyr(I-2) and displayed an inhibition constant of 4.7 mu M at pH 6.8 and 25 degrees C, while Leu or lie gave practically inert analogs. Replacement of the amino acids in P-2 with the analogous alpha-azaamino acids, as well as the glycine in P-1 with alpha-azaglycine, led to complete loss of inhibiting activity. Introducing alkoxy substituents at the methyl adjacent to the ketone group generally resulted in more effective inhibitors, with inhibition constants in the micromolar range for both papain and cathepsin B.

  DOI：

  10.1016/0223-5234(96)88312-7
• 作为产物：
  描述：

  <<(phenylmethoxy)methoxy>methyl>oxirane 在 氨 作用下， 以 四氢呋喃 、 乙醇 为溶剂， 反应 74.0h， 生成 N-benzyloxycarbonyl-L-phenylalanyl-1-amino-3-(benzyloxy)-methoxypropan-2-ol
  参考文献：
  名称：

  Peptidyl and azapeptidyl methylketones as substrate analog inhibitors of papain and cathepsin B

  摘要：

  Peptidyl methylketones containing Phe, Tyr, Tyr(I) Tyr(I-2), Leu and Ile in P-2 were synthesized and tested as substrate analog reversible inhibitors of papain and bovine spleen cathepsin B. The most effective cathepsin B inhibitor contained Tyr(I-2) and displayed an inhibition constant of 4.7 mu M at pH 6.8 and 25 degrees C, while Leu or lie gave practically inert analogs. Replacement of the amino acids in P-2 with the analogous alpha-azaamino acids, as well as the glycine in P-1 with alpha-azaglycine, led to complete loss of inhibiting activity. Introducing alkoxy substituents at the methyl adjacent to the ketone group generally resulted in more effective inhibitors, with inhibition constants in the micromolar range for both papain and cathepsin B.

  DOI：

  10.1016/0223-5234(96)88312-7