N2-(3-(3-(3-(3-aminopropanamido)propanamido)propanamido)propanoyl)-N5-((R)-1-((carboxymethyl)amino)-3-(((4-chlorophenyl)(hydroxy)carbamoyl)thio)-1-oxopropan-2-yl)-L-glutamine | 642097-54-9

• 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: N2-(3-(3-(3-(3-aminopropanamido)propanamido)propanamido)propanoyl)-N5-((R)-1-((carboxymethyl)amino)-3-(((4-chlorophenyl)(hydroxy)carbamoyl)thio)-1-oxopropan-2-yl)-L-glutamine
• CAS: 642097-54-9
• 化学式: C₂₉H₄₁ClN₈O₁₂S
• 分子量: 761.21
• InChiKey: XXSLWIPZUZUZFK-PMACEKPBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.71
• 重原子数：
  51.0
• 可旋转键数：
  23.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.48
• 拓扑面积：
  315.76
• 氢给体数：
  10.0
• 氢受体数：
  12.0

反应信息

• 作为反应物：
  描述：

  N2-(3-(3-(3-(3-aminopropanamido)propanamido)propanamido)propanoyl)-N5-((R)-1-((carboxymethyl)amino)-3-(((4-chlorophenyl)(hydroxy)carbamoyl)thio)-1-oxopropan-2-yl)-L-glutamine 在 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 5.0h， 生成
  参考文献：
  名称：

  Bivalent Transition-State Analogue Inhibitors of Human Glyoxalase I

  摘要：

  [GRAPHICS]A new class of competitive inhibitors of homodimeric human glyoxalase 1 has been created by cross-linking two molecules of the transition-state analogue S-(N-4-chlorophenyl-N-hydroxycarbamoyl)glutathione (CHG) through their gamma-glutamyl-NH2 groups with poly-beta-alanyl tethers of differing length: [CHG(beta-ala)(n)](2) suberate diamide (n = 1-7). The strongest inhibitors of this antitumor target enzyme likely bind simultaneously to the active site on each subunit to give K-i values as small as 0.96 nM (n = 6).

  DOI：

  10.1021/ol035917s
• 作为产物：
  描述：

  N2-(3-aminopropanoyl)-N5-((R)-1-((carboxymethyl)amino)-3-(((4-chlorophenyl)(hydroxy)carbamoyl)thio)-1-oxopropan-2-yl)-L-glutamine 在 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 7.5h， 生成 N2-(3-(3-(3-(3-aminopropanamido)propanamido)propanamido)propanoyl)-N5-((R)-1-((carboxymethyl)amino)-3-(((4-chlorophenyl)(hydroxy)carbamoyl)thio)-1-oxopropan-2-yl)-L-glutamine
  参考文献：
  名称：

  Bivalent Transition-State Analogue Inhibitors of Human Glyoxalase I

  摘要：

  [GRAPHICS]A new class of competitive inhibitors of homodimeric human glyoxalase 1 has been created by cross-linking two molecules of the transition-state analogue S-(N-4-chlorophenyl-N-hydroxycarbamoyl)glutathione (CHG) through their gamma-glutamyl-NH2 groups with poly-beta-alanyl tethers of differing length: [CHG(beta-ala)(n)](2) suberate diamide (n = 1-7). The strongest inhibitors of this antitumor target enzyme likely bind simultaneously to the active site on each subunit to give K-i values as small as 0.96 nM (n = 6).

  DOI：

  10.1021/ol035917s