3-(sulfurmethyl)-N-(4-methyl-3(4-(pyridine-3-yl)pyrimidin-2-ylamino)phenyl)benzamide | 1258531-74-6

• 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: 3-(sulfurmethyl)-N-(4-methyl-3(4-(pyridine-3-yl)pyrimidin-2-ylamino)phenyl)benzamide
• 英文别名: N-[4-methyl-3-[(4-pyridin-3-ylpyrimidin-2-yl)amino]phenyl]-3-methylsulfanylbenzamide
• CAS: 1258531-74-6
• 化学式: C₂₄H₂₁N₅OS
• 分子量: 427.53
• InChiKey: NZNWQGUJOLVDKY-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.4
• 重原子数：
  31
• 可旋转键数：
  6
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.08
• 拓扑面积：
  105
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  3-(甲硫基)苯甲酸 在 吡啶 、 氯化亚砜 、 三乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 4.0h， 生成 3-(sulfurmethyl)-N-(4-methyl-3(4-(pyridine-3-yl)pyrimidin-2-ylamino)phenyl)benzamide
  参考文献：
  名称：

  Synthesis and docking study of 2-phenylaminopyrimidine Abl tyrosine kinase inhibitors

  摘要：

  Six analogs of imatinib, an Abl kinase inhibitor clinically used as a first-line therapeutic agent for chronic myeloid leukaemia (CML), have been synthesized and characterized. And their potency as Abl kinase inhibitors have been screened by a robust virtual screening method developed based on the crystal structure (PDB code 2hyy) of Abl-imatinib complex using Surflex-Docking. The docking results are consistent with the inhibitory potency of the compounds characterized by MS method. And the H-bonds between imatinib analogs and Thr315 and Met318 residues in Abl kinase are shown to be crucial for achieving accurate poses and high binding affinities for the ATP-competitive kinase inhibitors. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.09.127

文献信息

• Synthesis and docking study of 2-phenylaminopyrimidine Abl tyrosine kinase inhibitors
  作者：Shuang Lü、Qun Luo、Xiang Hao、Xianchan Li、Liyun Ji、Wei Zheng、Fuyi Wang

  DOI：10.1016/j.bmcl.2011.09.127

  日期：2011.12

  Six analogs of imatinib, an Abl kinase inhibitor clinically used as a first-line therapeutic agent for chronic myeloid leukaemia (CML), have been synthesized and characterized. And their potency as Abl kinase inhibitors have been screened by a robust virtual screening method developed based on the crystal structure (PDB code 2hyy) of Abl-imatinib complex using Surflex-Docking. The docking results are consistent with the inhibitory potency of the compounds characterized by MS method. And the H-bonds between imatinib analogs and Thr315 and Met318 residues in Abl kinase are shown to be crucial for achieving accurate poses and high binding affinities for the ATP-competitive kinase inhibitors. (C) 2011 Elsevier Ltd. All rights reserved.