(Z)-3-amino-5-(2'-hydroxybenzylidene)-2-thioxothiazolidin-4-one | 19745-80-3

• 分子结构分类: 有机化合物 - 苯类化合物 - 酚类
• 英文名称: (Z)-3-amino-5-(2'-hydroxybenzylidene)-2-thioxothiazolidin-4-one
• 英文别名: 3-Amino-5-(2-hydroxybenzyliden)rhodanin；3-Amino-5-(2-hydroxy-benzylidene)-2-thioxo-thiazolidin-4-one；(5Z)-3-amino-5-[(2-hydroxyphenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one
• CAS: 19745-80-3
• 化学式: C₁₀H₈N₂O₂S₂
• 分子量: 252.318
• InChiKey: FHQYHDZJELLOKV-YVMONPNESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.9
• 重原子数：
  16
• 可旋转键数：
  1
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  124
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  N-氨基绕丹宁 、 水杨醛 在 溶剂黄146 、 三乙胺 作用下， 以 乙酸乙酯 为溶剂， 反应 3.0h， 以77%的产率得到(Z)-3-amino-5-(2'-hydroxybenzylidene)-2-thioxothiazolidin-4-one
  参考文献：
  名称：

  Selective small molecule inhibitors of the potential breast cancer marker, human arylamine N-acetyltransferase 1, and its murine homologue, mouse arylamine N-acetyltransferase 2

  摘要：

  The identification, synthesis and evaluation of a series of rhodanine and thiazolidin-2,4-dione derivatives as selective inhibitors of human arylamine N-acetyltransferase 1 and mouse arylamine N-acetyltransferase 2 is described. The most potent inhibitors identified have submicromolar activity and inhibit both the recombinant proteins and human NAT1 in ZR-75 cell lysates in a competitive manner. H-1 NMR studies on purified mouse Nat2 demonstrate that the inhibitors bind within the putative active site of the enzyme. (C) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2008.11.032

文献信息

• Selective small molecule inhibitors of the potential breast cancer marker, human arylamine N-acetyltransferase 1, and its murine homologue, mouse arylamine N-acetyltransferase 2
  作者：Angela J. Russell、Isaac M. Westwood、Matthew H.J. Crawford、James Robinson、Akane Kawamura、Christina Redfield、Nicola Laurieri、Edward D. Lowe、Stephen G. Davies、Edith Sim

  DOI：10.1016/j.bmc.2008.11.032

  日期：2009.1

  The identification, synthesis and evaluation of a series of rhodanine and thiazolidin-2,4-dione derivatives as selective inhibitors of human arylamine N-acetyltransferase 1 and mouse arylamine N-acetyltransferase 2 is described. The most potent inhibitors identified have submicromolar activity and inhibit both the recombinant proteins and human NAT1 in ZR-75 cell lysates in a competitive manner. H-1 NMR studies on purified mouse Nat2 demonstrate that the inhibitors bind within the putative active site of the enzyme. (C) 2008 Elsevier Ltd. All rights reserved.