[(4S)-5-benzyl-4-(2-methylpropyl)-1,1,3-trioxo-1,2,5-thiadiazolidin-2-yl]methyl 2-(4-benzoylphenyl)propanoate | 1253393-91-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: [(4S)-5-benzyl-4-(2-methylpropyl)-1,1,3-trioxo-1,2,5-thiadiazolidin-2-yl]methyl 2-(4-benzoylphenyl)propanoate
• CAS: 1253393-91-7
• 化学式: C₃₀H₃₂N₂O₆S
• 分子量: 548.66
• InChiKey: IAXZWYPEHHZCGO-ZUILJJEPSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.7
• 重原子数：
  39
• 可旋转键数：
  11
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  109
• 氢给体数：
  0
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  2-(4-苯甲酰基苯基)丙酸 、 在 1,8-二氮杂双环[5.4.0]十一碳-7-烯 作用下， 以 二氯甲烷 为溶剂， 以82%的产率得到[(4S)-5-benzyl-4-(2-methylpropyl)-1,1,3-trioxo-1,2,5-thiadiazolidin-2-yl]methyl 2-(4-benzoylphenyl)propanoate
  参考文献：
  名称：

  Effects of structure on inhibitory activity in a series of mechanism-based inhibitors of human neutrophil elastase

  摘要：

  A structurally-diverse series of carboxylate derivatives based on the 1,2,5-thiadiazolidin-one 1,1 dioxide scaffold were synthesized and used to probe the S' subsites of human neutrophil elastase (HNE) and neutrophil proteinase 3 (Pr 3). Several compounds are potent inhibitors of HNE but devoid of inhibitory activity toward Pr 3, suggesting that the S' subsites of HNE exhibit significant plasticity and can, unlike Pr 3, tolerate various large hydrophobic groups. The results provide a promising framework for the design of highly selective inhibitors of the two enzymes. (c) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2010.07.071

文献信息

• Effects of structure on inhibitory activity in a series of mechanism-based inhibitors of human neutrophil elastase
  作者：Dengfeng Dou、Guijia He、Rongze Kuang、Qingfong Fu、Radhika Venkataraman、William C. Groutas

  DOI：10.1016/j.bmc.2010.07.071

  日期：2010.9

  A structurally-diverse series of carboxylate derivatives based on the 1,2,5-thiadiazolidin-one 1,1 dioxide scaffold were synthesized and used to probe the S' subsites of human neutrophil elastase (HNE) and neutrophil proteinase 3 (Pr 3). Several compounds are potent inhibitors of HNE but devoid of inhibitory activity toward Pr 3, suggesting that the S' subsites of HNE exhibit significant plasticity and can, unlike Pr 3, tolerate various large hydrophobic groups. The results provide a promising framework for the design of highly selective inhibitors of the two enzymes. (c) 2010 Elsevier Ltd. All rights reserved.