2-(Aminomethyl)-4-methylpentanamide | 1249706-29-3

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: 2-(Aminomethyl)-4-methylpentanamide
• CAS: 1249706-29-3
• 化学式: C₇H₁₆N₂O
• 分子量: 144.217
• InChiKey: ZBUPIZBVXGJHSP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.1
• 重原子数：
  10
• 可旋转键数：
  4
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.86
• 拓扑面积：
  69.1
• 氢给体数：
  2
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  3-(3-t-butyl-5-(3-(naphthalen-1-yl)ureido)-1H-pyrazol-1-yl)benzoic acid 、 2-(Aminomethyl)-4-methylpentanamide 在 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 作用下， 生成 3-(3-(tert-butyl)-5-(3-(naphthalen-1-yl)ureido)-1H-pyrazol-1-yl)-N-(2-carbamoyl-4-methylpentyl)benzamide
  参考文献：
  名称：

  Biochemical and biophysical characterization of unique switch pocket inhibitors of p38α

  摘要：

  Herein we describe the identification and characterization of a class of molecules that are believed to extend into a region of p38 known as the 'switch pocket'. Although these molecules lack a canonical hinge binding motif, they show K(i) values as low as 100 nM against p38. We show that molecules that interact with this region of the protein demonstrate different binding kinetics than a canonical ATP mimetic, as well as a wide range of kinome profiles. Thus, the switch pocket presents new opportunities for kinome selectivity which could result in unique biochemical responses and offer new opportunities in the field of kinase drug discovery. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2010.04.097

文献信息

• Biochemical and biophysical characterization of unique switch pocket inhibitors of p38α
  作者：Steven L. Swann、Philip J. Merta、Lemma Kifle、Duncan Groebe、Kathy Sarris、Philip J. Hajduk、Chaohong Sun

  DOI：10.1016/j.bmcl.2010.04.097

  日期：2010.10

  Herein we describe the identification and characterization of a class of molecules that are believed to extend into a region of p38 known as the 'switch pocket'. Although these molecules lack a canonical hinge binding motif, they show K(i) values as low as 100 nM against p38. We show that molecules that interact with this region of the protein demonstrate different binding kinetics than a canonical ATP mimetic, as well as a wide range of kinome profiles. Thus, the switch pocket presents new opportunities for kinome selectivity which could result in unique biochemical responses and offer new opportunities in the field of kinase drug discovery. (C) 2010 Elsevier Ltd. All rights reserved.