(2S,3S)-1-Benzyloxycarbonylmethyl-aziridine-2,3-dicarboxylic acid diethyl ester | 288855-23-2

• 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,3S)-1-Benzyloxycarbonylmethyl-aziridine-2,3-dicarboxylic acid diethyl ester
• 英文别名: diethyl (2S,3S)-1-(2-oxo-2-phenylmethoxyethyl)aziridine-2,3-dicarboxylate
• CAS: 288855-23-2
• 化学式: C₁₇H₂₁NO₆
• 分子量: 335.357
• InChiKey: QUPPNIGRKWDSJB-GJZGRUSLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.1
• 重原子数：
  24
• 可旋转键数：
  11
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  81.9
• 氢给体数：
  0
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  (2S,3S)-1-Benzyloxycarbonylmethyl-aziridine-2,3-dicarboxylic acid diethyl ester 在 palladium on activated charcoal 氢气 作用下， 以 乙醇 为溶剂， 反应 1.0h， 以89%的产率得到(2S,3S)-1-Carboxymethyl-aziridine-2,3-dicarboxylic acid diethyl ester
  参考文献：
  名称：

  aziridinyl peptides as inhibitors of cysteine proteases: Effect of a free carboxylic acid function on inhibition

  摘要：

  Peptides containing aziridine-2,3-dicarboxylate (Azi) as electrophilic building block are evaluated as inhibitors of the cysteine proteases papain, cathepsin B, cathepsin L and clostripain. The influence of a free carboxylic acid as functional group at different positions of the inhibitor molecule on inhibition is analyzed. Structure-activity relationships and binding mode hypotheses are discussed. In contrast to the bacterial enzyme clostripain, the papain like mammalian proteases (cathepsins) are irreversibly inactivated by aziridinyl peptides. N-Unsubstituted aziridines are much more potent inhibitors of papain and cathepsins if they contain the free carboxylic acid attached to the aziridine ring (HOAzi-Leu-ProOBzl). Two free carboxylic acid functions at the aziridine ring are necessary for good inhibition of these enzymes by N'-acylated aziridinyl peptides (BOC-Phe-Azi(OH)(2)). Chimeric bispeptidyl derivatives are selective CB inhibitors if the free acid is located at the C-terminus of the peptide (BOC-Phe-(EtO)Azi-Leu-ProOH). Clostripain is only inhibited by aziridinyl peptide esters. (C) 2000 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(00)00058-4
• 作为产物：
  描述：

  diethyl (2S,3S)-(+)-aziridine-2,3-dicarboxylate 、 2-溴乙酸苄酯 在 sodium carbonate 、 potassium iodide 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 48.0h， 以52.6%的产率得到(2S,3S)-1-Benzyloxycarbonylmethyl-aziridine-2,3-dicarboxylic acid diethyl ester
  参考文献：
  名称：

  aziridinyl peptides as inhibitors of cysteine proteases: Effect of a free carboxylic acid function on inhibition

  摘要：

  Peptides containing aziridine-2,3-dicarboxylate (Azi) as electrophilic building block are evaluated as inhibitors of the cysteine proteases papain, cathepsin B, cathepsin L and clostripain. The influence of a free carboxylic acid as functional group at different positions of the inhibitor molecule on inhibition is analyzed. Structure-activity relationships and binding mode hypotheses are discussed. In contrast to the bacterial enzyme clostripain, the papain like mammalian proteases (cathepsins) are irreversibly inactivated by aziridinyl peptides. N-Unsubstituted aziridines are much more potent inhibitors of papain and cathepsins if they contain the free carboxylic acid attached to the aziridine ring (HOAzi-Leu-ProOBzl). Two free carboxylic acid functions at the aziridine ring are necessary for good inhibition of these enzymes by N'-acylated aziridinyl peptides (BOC-Phe-Azi(OH)(2)). Chimeric bispeptidyl derivatives are selective CB inhibitors if the free acid is located at the C-terminus of the peptide (BOC-Phe-(EtO)Azi-Leu-ProOH). Clostripain is only inhibited by aziridinyl peptide esters. (C) 2000 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(00)00058-4

文献信息

• aziridinyl peptides as inhibitors of cysteine proteases: Effect of a free carboxylic acid function on inhibition
  作者：T. Schirmeister、M. Peric

  DOI：10.1016/s0968-0896(00)00058-4

  日期：2000.6

  Peptides containing aziridine-2,3-dicarboxylate (Azi) as electrophilic building block are evaluated as inhibitors of the cysteine proteases papain, cathepsin B, cathepsin L and clostripain. The influence of a free carboxylic acid as functional group at different positions of the inhibitor molecule on inhibition is analyzed. Structure-activity relationships and binding mode hypotheses are discussed. In contrast to the bacterial enzyme clostripain, the papain like mammalian proteases (cathepsins) are irreversibly inactivated by aziridinyl peptides. N-Unsubstituted aziridines are much more potent inhibitors of papain and cathepsins if they contain the free carboxylic acid attached to the aziridine ring (HOAzi-Leu-ProOBzl). Two free carboxylic acid functions at the aziridine ring are necessary for good inhibition of these enzymes by N'-acylated aziridinyl peptides (BOC-Phe-Azi(OH)(2)). Chimeric bispeptidyl derivatives are selective CB inhibitors if the free acid is located at the C-terminus of the peptide (BOC-Phe-(EtO)Azi-Leu-ProOH). Clostripain is only inhibited by aziridinyl peptide esters. (C) 2000 Elsevier Science Ltd. All rights reserved.