4-[2-(Hydroxymethyl)naphthalen-1-Yl]-N-[2-(Morpholin-4-Yl)ethyl]benzamide | 1380213-44-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: 4-[2-(Hydroxymethyl)naphthalen-1-Yl]-N-[2-(Morpholin-4-Yl)ethyl]benzamide
• 英文别名: 4-[2-(hydroxymethyl)naphthalen-1-yl]-N-(2-morpholin-4-ylethyl)benzamide
• CAS: 1380213-44-4
• 化学式: C₂₄H₂₆N₂O₃
• 分子量: 390.482
• InChiKey: QFHPEAOPPKNNMS-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.9
• 重原子数：
  29
• 可旋转键数：
  6
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  61.8
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  4-羧基苯硼酸频那醇酯 在 (1,1'-bis(diphenylphosphino)ferrocene)palladium(II) dichloride 、 potassium phosphate 、 O-(benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium tetrafluoroborate 、 N,N-二异丙基乙胺 作用下， 以 1,4-二氧六环 、 二氯甲烷 、 水 为溶剂， 反应 18.0h， 生成 4-[2-(Hydroxymethyl)naphthalen-1-Yl]-N-[2-(Morpholin-4-Yl)ethyl]benzamide
  参考文献：
  名称：

  Investigation of the binding pocket of human hematopoietic prostaglandin (PG) D2 synthase (hH-PGDS): A tale of two waters

  摘要：

  The inhibition of hH-PGDS has been proposed as a potential target for the development of anti-allergic and anti-inflammatory drugs. Herein we describe our investigation of the binding pocket of this important enzyme and our observation that two water molecules bind to our inhibitors and the enzyme. A series of compounds were prepared to the probe the importance of the water molecules in determining the binding affinity of the inhibitors to the enzyme. The study provides insight into the binding requirements for the design of potent hH-PGDS inhibitors. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2012.04.004

文献信息

• Investigation of the binding pocket of human hematopoietic prostaglandin (PG) D2 synthase (hH-PGDS): A tale of two waters
  作者：John I. Trujillo、James R. Kiefer、Wei Huang、Jacqueline E. Day、Joseph Moon、Gina M. Jerome、Christine P. Bono、Christine M. Kornmeier、Melanie L. Williams、Cyrille Kuhn、Glen R. Rennie、Thomas A. Wynn、Christopher P. Carron、Atli Thorarensen

  DOI：10.1016/j.bmcl.2012.04.004

  日期：2012.6

  The inhibition of hH-PGDS has been proposed as a potential target for the development of anti-allergic and anti-inflammatory drugs. Herein we describe our investigation of the binding pocket of this important enzyme and our observation that two water molecules bind to our inhibitors and the enzyme. A series of compounds were prepared to the probe the importance of the water molecules in determining the binding affinity of the inhibitors to the enzyme. The study provides insight into the binding requirements for the design of potent hH-PGDS inhibitors. (C) 2012 Elsevier Ltd. All rights reserved.