4-fluoro-2-hydrazinylbenzonitrile | 1261105-29-6

• 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: 4-fluoro-2-hydrazinylbenzonitrile
• CAS: 1261105-29-6
• 化学式: C₇H₆FN₃
• 分子量: 151.143
• InChiKey: WEKQGTQNMFFZOP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  11
• 可旋转键数：
  1
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.0
• 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：

  2,4-二氟苯腈 在 一水合肼 作用下， 以 甲醇 为溶剂， 反应 16.0h， 生成 4-fluoro-2-hydrazinylbenzonitrile 、 2-氟-4-肼基-苯甲腈
  参考文献：
  名称：

  A highly selective Hsp90 affinity chromatography resin with a cleavable linker

  摘要：

  Over 200 proteins have been identified that interact with the protein chaperone Hsp90, a recognized therapeutic target thought to participate in non-oncogene addiction in a variety of human cancers. However, defining Hsp90 clients is challenging because interactions between Hsp90 and its physiologically relevant targets involve low affinity binding and are thought to be transient. Using a chemo-proteomic strategy, we have developed a novel orthogonally cleavable Hsp90 affinity resin that allows purification of the native protein and is quite selective for Hsp90 over its immediate family members, GRP94 and TRAP 1. We show that the resin can be used under low stringency conditions for the rapid, unambiguous capture of native Hsp90 in complex with a native client. We also show that the choice of linker used to tether the ligand to the insoluble support can have a dramatic effect on the selectivity of the affinity media. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2012.03.043

文献信息

• A highly selective Hsp90 affinity chromatography resin with a cleavable linker
  作者：Philip F. Hughes、Jared J. Barrott、David A. Carlson、David R. Loiselle、Brittany L. Speer、Khaldon Bodoor、Lauretta A. Rund、Timothy A.J. Haystead

  DOI：10.1016/j.bmc.2012.03.043

  日期：2012.5

  Over 200 proteins have been identified that interact with the protein chaperone Hsp90, a recognized therapeutic target thought to participate in non-oncogene addiction in a variety of human cancers. However, defining Hsp90 clients is challenging because interactions between Hsp90 and its physiologically relevant targets involve low affinity binding and are thought to be transient. Using a chemo-proteomic strategy, we have developed a novel orthogonally cleavable Hsp90 affinity resin that allows purification of the native protein and is quite selective for Hsp90 over its immediate family members, GRP94 and TRAP 1. We show that the resin can be used under low stringency conditions for the rapid, unambiguous capture of native Hsp90 in complex with a native client. We also show that the choice of linker used to tether the ligand to the insoluble support can have a dramatic effect on the selectivity of the affinity media. (C) 2012 Elsevier Ltd. All rights reserved.