(Z)-4-(2-(5-(N-(2-chlorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid | 1051387-87-1

• 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: (Z)-4-(2-(5-(N-(2-chlorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
• 英文别名: 4-[2-[5-[(2-chlorophenyl)methylsulfamoyl]-2-oxoindol-3-yl]hydrazinyl]benzoic acid
• CAS: 1051387-87-1
• 化学式: C₂₂H₁₇ClN₄O₅S
• 分子量: 484.92
• InChiKey: NNCLDJYKDAGUFL-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.3
• 重原子数：
  33
• 可旋转键数：
  8
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.05
• 拓扑面积：
  145
• 氢给体数：
  4
• 氢受体数：
  8

反应信息

• 作为产物：
  描述：

  N-(2-chlorobenzyl)-2,3-dioxoindoline-5-sulfonamide 、 4-肼基苯甲酸 在 盐酸 作用下， 以 乙醇 、 水 为溶剂， 反应 0.25h， 以28%的产率得到(Z)-4-(2-(5-(N-(2-chlorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
  参考文献：
  名称：

  Inhibitors of Src Homology-2 Domain Containing Protein Tyrosine Phosphatase-2 (Shp2) Based on Oxindole Scaffolds

  摘要：

  Screening of the NCl diversity set of compounds has led to the identification of 5 (NSC-117199), which inhibits the protein tyrosine phosphatase (PTP) Shp2 with an IC(50) of 47 mu M. A focused library incorporating an isatin scaffold was designed and evaluated for inhibition of Shp2 and Shp1 PTP activities. Several compounds were identified that selectively inhibit Shp2 over ShpI and PTP1B with low to submicromolar activity. A model for the binding of the active compounds is proposed.

  DOI：

  10.1021/jm8002526

文献信息

• Inhibitors of Src Homology-2 Domain Containing Protein Tyrosine Phosphatase-2 (Shp2) Based on Oxindole Scaffolds
  作者：Harshani R. Lawrence、Roberta Pireddu、Liwei Chen、Yunting Luo、Shen-Shu Sung、Ann Marie Szymanski、M. L. Richard Yip、Wayne C. Guida、Saïd M. Sebti、Jie Wu、Nicholas J. Lawrence

  DOI：10.1021/jm8002526

  日期：2008.8.1

  Screening of the NCl diversity set of compounds has led to the identification of 5 (NSC-117199), which inhibits the protein tyrosine phosphatase (PTP) Shp2 with an IC(50) of 47 mu M. A focused library incorporating an isatin scaffold was designed and evaluated for inhibition of Shp2 and Shp1 PTP activities. Several compounds were identified that selectively inhibit Shp2 over ShpI and PTP1B with low to submicromolar activity. A model for the binding of the active compounds is proposed.