N-(2-chloro-phenyl)-3-(4-([3-(2-chloro-phenylcarbamoyl)-propionyl]-hydrazonomethyl)-benzylidene-hydrazinocarbonyl)-propionamide | 356561-76-7

• 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: N-(2-chloro-phenyl)-3-(4-([3-(2-chloro-phenylcarbamoyl)-propionyl]-hydrazonomethyl)-benzylidene-hydrazinocarbonyl)-propionamide
• 英文别名: N-(2-chloro-phenyl)-3-(4-{[3-(2-chloro-phenylcarbamoyl)-propionyl]-hydrazonomethyl}-benzylidene-hydrazinocarbonyl)-propionamide；N'-[[4-[[[4-(2-chloroanilino)-4-oxobutanoyl]hydrazinylidene]methyl]phenyl]methylideneamino]-N-(2-chlorophenyl)butanediamide
• CAS: 356561-76-7
• 化学式: C₂₈H₂₆Cl₂N₆O₄
• 分子量: 581.458
• InChiKey: OWCZBPBKTGGJTG-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.2
• 重原子数：
  40
• 可旋转键数：
  12
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.14
• 拓扑面积：
  141
• 氢给体数：
  4
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  N-(2-chloro-phenyl)-3-hydrazinocarbonyl-propionamide 、 对苯二甲醛 以 乙醇 为溶剂， 反应 2.0h， 以69%的产率得到N-(2-chloro-phenyl)-3-(4-([3-(2-chloro-phenylcarbamoyl)-propionyl]-hydrazonomethyl)-benzylidene-hydrazinocarbonyl)-propionamide
  参考文献：
  名称：

  Complexes of Bacterial Nicotinate Mononucleotide Adenylyltransferase with Inhibitors: Implication for Structure-Based Drug Design and Improvement

  摘要：

  Bacterial nicotinate mononucleotide adenylyltransferase encoded by the essential gene nadD plays a central role in the synthesis of the redox cofactor NAD(+). The NadD enzyme is conserved in the majority of bacterial species and has been recognized as a novel target for developing new and potentially broad-spectrum antibacterial therapeutics. Here we report the crystal structures of Bacillus anthracis NadD in complex with three NadD inhibitors, including two analogues synthesized in the present study. These structures revealed a common binding site shared by different classes of NadD inhibitors and explored the chemical environment surrounding this site. The structural data obtained here also showed that the subtle changes in ligand structure can lead to significant changes in the binding mode, information that will be useful for future structure-based optimization and design of high affinity inhibitors.

  DOI：

  10.1021/jm100377f

文献信息

• [EN] TARGETING NAD BIOSYNTHESIS IN BACTERIAL PATHOGENS<br/>[FR] CIBLAGE DE LA BIOSYNTHÈSE DE LA NAD DANS DES BACTÉRIES PATHOGÈNES
  申请人：UNIV MARYLAND

  公开号：WO2011006158A3

  公开（公告）日：2011-05-19
• Complexes of Bacterial Nicotinate Mononucleotide Adenylyltransferase with Inhibitors: Implication for Structure-Based Drug Design and Improvement
  作者：Nian Huang、Rohit Kolhatkar、Yvonne Eyobo、Leonardo Sorci、Irina Rodionova、Andrei L. Osterman、Alexander D. MacKerell、Hong Zhang

  DOI：10.1021/jm100377f

  日期：2010.7.22

  Bacterial nicotinate mononucleotide adenylyltransferase encoded by the essential gene nadD plays a central role in the synthesis of the redox cofactor NAD(+). The NadD enzyme is conserved in the majority of bacterial species and has been recognized as a novel target for developing new and potentially broad-spectrum antibacterial therapeutics. Here we report the crystal structures of Bacillus anthracis NadD in complex with three NadD inhibitors, including two analogues synthesized in the present study. These structures revealed a common binding site shared by different classes of NadD inhibitors and explored the chemical environment surrounding this site. The structural data obtained here also showed that the subtle changes in ligand structure can lead to significant changes in the binding mode, information that will be useful for future structure-based optimization and design of high affinity inhibitors.