tert-butyl 4-[3-[[2-(5-methoxy-3-oxo-1H-isoindol-2-yl)-1,3-thiazole-4-carbonyl]amino]pyridin-4-yl]piperazine-1-carboxylate | 1026668-82-5

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪烷类
• 英文名称: tert-butyl 4-[3-[[2-(5-methoxy-3-oxo-1H-isoindol-2-yl)-1,3-thiazole-4-carbonyl]amino]pyridin-4-yl]piperazine-1-carboxylate
• CAS: 1026668-82-5
• 化学式: C₂₇H₃₀N₆O₅S
• 分子量: 550.638
• InChiKey: AAPRDEWVCINDRL-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  39
• 可旋转键数：
  7
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.37
• 拓扑面积：
  145
• 氢给体数：
  1
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  tert-butyl 4-[3-[[2-(5-methoxy-3-oxo-1H-isoindol-2-yl)-1,3-thiazole-4-carbonyl]amino]pyridin-4-yl]piperazine-1-carboxylate 在 三氟乙酸 作用下， 以 neat (no solvent) 为溶剂， 反应 0.25h， 生成 2-amino-N-(4-(piperazin-1-yl)pyridin-3-yl)thiazole-4-carboxamide
  参考文献：
  名称：

  Structure-based design and optimization of 2-aminothiazole-4-carboxamide as a new class of CHK1 inhibitors

  摘要：

  Drug design efforts in the emerging 2-aminothiazole-4-carboxamide class of CHK1 inhibitors have uncovered specific combinations of key substructures within the molecule; resulting in significant improvements in cell-based activity while retaining a greater than one hundred-fold selectivity against CDK2. The X-ray crystal structure of a complex between compound 39 and the CHK1 protein detailing a 'U-shaped' topology and key interactions with the protein surface at the ATP site is also reported. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.02.108
• 作为产物：
  描述：

  1-Boc-4-(2-氨基苯基)哌嗪 在 tris-(dibenzylideneacetone)dipalladium(0) 、 caesium carbonate 、 N,N-二异丙基乙胺 、 Methanaminium,N-[(dimethylamino)(3H-1,2,3-triazolo[4,5-b]pyridin-3-yloxy)methylene]-N-methyl-, hexafluorophosphate(1-) 作用下， 以 1,4-二氧六环 、 N,N-二甲基甲酰胺 为溶剂， 反应 30.0h， 生成 tert-butyl 4-[3-[[2-(5-methoxy-3-oxo-1H-isoindol-2-yl)-1,3-thiazole-4-carbonyl]amino]pyridin-4-yl]piperazine-1-carboxylate
  参考文献：
  名称：

  Structure-based design and optimization of 2-aminothiazole-4-carboxamide as a new class of CHK1 inhibitors

  摘要：

  Drug design efforts in the emerging 2-aminothiazole-4-carboxamide class of CHK1 inhibitors have uncovered specific combinations of key substructures within the molecule; resulting in significant improvements in cell-based activity while retaining a greater than one hundred-fold selectivity against CDK2. The X-ray crystal structure of a complex between compound 39 and the CHK1 protein detailing a 'U-shaped' topology and key interactions with the protein surface at the ATP site is also reported. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.02.108

文献信息

• 2-AMINOTHIAZOLE-4-CARBOXYLIC AMIDES AS PROTEIN KINASE INHIBITORS
  申请人：Shipps, JR. Gerald W.

  公开号：US20100130465A1

  公开（公告）日：2010-05-27

  The present invention relates to novel Anilinopiperazine Derivatives of formula (I), compositions comprising the Anilinopiperazine Derivatives, and methods for using the Anilinopiperazine Derivatives for treating or preventing a proliferative disorder, an anti-proliferative disorder, inflammation, arthritis, a central nervous system disorder, a cardiovascular disease, alopecia, a neuronal disease, an ischemic injury, a viral disease, a fungal infection, or a disorder related to the activity of a protein kinase.

  本发明涉及一种新型的Anilinopiperazine衍生物的公式(I)，包括该Anilinopiperazine衍生物的组合物，并且使用该Anilinopiperazine衍生物治疗或预防增生性疾病、抗增生性疾病、炎症、关节炎、中枢神经系统疾病、心血管疾病、脱发、神经疾病、缺血性损伤、病毒性疾病、真菌感染或与蛋白激酶活性相关的疾病的方法。
• US8318735B2
  申请人：——

  公开号：US8318735B2

  公开（公告）日：2012-11-27
• Structure-based design and optimization of 2-aminothiazole-4-carboxamide as a new class of CHK1 inhibitors
  作者：Xiaohua Huang、Cliff C. Cheng、Thierry O. Fischmann、José S. Duca、Matthew Richards、Praveen K. Tadikonda、Panduranga Adulla Reddy、Lianyun Zhao、M. Arshad Siddiqui、David Parry、Nicole Davis、Wolfgang Seghezzi、Derek Wiswell、Gerald W. Shipps

  DOI：10.1016/j.bmcl.2013.02.108

  日期：2013.5

  Drug design efforts in the emerging 2-aminothiazole-4-carboxamide class of CHK1 inhibitors have uncovered specific combinations of key substructures within the molecule; resulting in significant improvements in cell-based activity while retaining a greater than one hundred-fold selectivity against CDK2. The X-ray crystal structure of a complex between compound 39 and the CHK1 protein detailing a 'U-shaped' topology and key interactions with the protein surface at the ATP site is also reported. (C) 2013 Elsevier Ltd. All rights reserved.