1-(4-(3-nitrobenzoyl)benzoyl)-3-thiosemicarbazide | 1353654-34-8

• 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: 1-(4-(3-nitrobenzoyl)benzoyl)-3-thiosemicarbazide
• 英文别名: [[4-(3-Nitrobenzoyl)benzoyl]amino]thiourea
• CAS: 1353654-34-8
• 化学式: C₁₅H₁₂N₄O₄S
• 分子量: 344.351
• InChiKey: RWMPSNURTGYLPE-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.9
• 重原子数：
  24
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  162
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  间硝基苯甲酸 在 吡啶 、 Jones reagent 、 氯化亚砜 、 溶剂黄146 作用下， 反应 6.0h， 生成 1-(4-(3-nitrobenzoyl)benzoyl)-3-thiosemicarbazide
  参考文献：
  名称：

  3-Mercapto-1,2,4-triazoles and N-acylated thiosemicarbazides as metallo-β-lactamase inhibitors

  摘要：

  The production of beta-lactamases is an effective strategy by which pathogenic bacteria can develop resistance against beta-lactam antibiotics. While inhibitors of serine-beta-lactamases are widely used in combination therapy with b-lactam antibiotics, there are no clinically available inhibitors of metallo-beta-lactamases (MBLs), and so there is a need for the development of such inhibitors. This work describes the optimisation of a lead inhibitor previously identified by fragment screening of a compound library. We also report that thiosemicarbazide intermediates in the syntheses of these compounds are also moderately potent inhibitors of the IMP-1 MBL from Pseudomonas aeruginosa. The interactions of these inhibitors with the active site of IMP-1 were examined using in silico methods. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.10.116

文献信息

• 3-Mercapto-1,2,4-triazoles and N-acylated thiosemicarbazides as metallo-β-lactamase inhibitors
  作者：Faridoon、Waleed M. Hussein、Peter Vella、Nazar Ul Islam、David L. Ollis、Gerhard Schenk、Ross P. McGeary

  DOI：10.1016/j.bmcl.2011.10.116

  日期：2012.1

  The production of beta-lactamases is an effective strategy by which pathogenic bacteria can develop resistance against beta-lactam antibiotics. While inhibitors of serine-beta-lactamases are widely used in combination therapy with b-lactam antibiotics, there are no clinically available inhibitors of metallo-beta-lactamases (MBLs), and so there is a need for the development of such inhibitors. This work describes the optimisation of a lead inhibitor previously identified by fragment screening of a compound library. We also report that thiosemicarbazide intermediates in the syntheses of these compounds are also moderately potent inhibitors of the IMP-1 MBL from Pseudomonas aeruginosa. The interactions of these inhibitors with the active site of IMP-1 were examined using in silico methods. (C) 2011 Elsevier Ltd. All rights reserved.