1-[(5-hydroxy-4-oxo-4H-pyran-2-yl)methylene]thiosemicarbazide | 1335029-60-1

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡喃
• 英文名称: 1-[(5-hydroxy-4-oxo-4H-pyran-2-yl)methylene]thiosemicarbazide
• 英文别名: [(5-hydroxy-4-oxopyran-2-yl)methylideneamino]thiourea
• CAS: 1335029-60-1
• 化学式: C₇H₇N₃O₃S
• 分子量: 213.217
• InChiKey: SYMCWJAFZPCSKX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.49
• 重原子数：
  14.0
• 可旋转键数：
  2.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  100.85
• 氢给体数：
  3.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  甲醇 、 乙醚 、 1-[(5-hydroxy-4-oxo-4H-pyran-2-yl)methylene]thiosemicarbazide 、 水 、 反应 168.5h， 生成
  参考文献：
  名称：

  Dicopper中心的Ditopic螯合剂可增强酪氨酸酶的抑制作用

  摘要：

  酪氨酸酶（Tys）参与黑色素（保护性色素）生物合成的关键步骤，靶向酪氨酸酶上双核铜活性位点的分子代表了调节酶活性的相关策略。在这项工作中，研究了由已知抑制剂组合产生的可能的协同作用。为此，含有曲酸（KA）和2-羟基吡啶-N的衍生物合成了氧化硫（HOPNO）和硫代半脲（TSC）部分。对来自不同来源（蘑菇，细菌和人）的纯化酪氨酸酶以及人黑素瘤MNT-1细胞系裂解液产生黑色素的抑制活性进行了评估。结果显示，与母体化合物相比，抑制作用显着增强，尤其是对HOPNO-TSC。为了阐明与dicopper（II）活性位点的相互作用方式，对酪氨酸酶生物启发的dicopper（II）中心模型的结合研究进行了研究。一个双位抑制剂（KA-TSC）与模型复合物之间的分离加合物的结构表明，两个螯合位点均可发生与双铜中心的结合。

  DOI：

  10.1002/chem.202004695
• 作为产物：
  描述：

  2-(羟基甲基)-5-甲氧基-4H-吡喃-4-酮 在 manganese(IV) oxide 、 aluminum (III) chloride 、 溶剂黄146 作用下， 以 乙醇 、 甲苯 为溶剂， 反应 27.0h， 生成 1-[(5-hydroxy-4-oxo-4H-pyran-2-yl)methylene]thiosemicarbazide
  参考文献：
  名称：

  Refinement of arylthiosemicarbazone pharmacophore in inhibition of mushroom tyrosinase

  摘要：

  Melanin play a major role in human skin protection and their biosynthesis is vital. Due to their color, they contribute to the skin pigmentation. Tyrosinase is a key enzyme involved in the first stage of melanin biosynthesis, it catalyzes the transformation of tyrosine into L-dopaquinone. The aim of the present study was to study molecules able to inhibit tyrosinase to be used in treating depigmentation-related disorders. In this study, we targeted arylthiosemicarbazone analogs with the aim to contribute to the identification of the optimal aryl ring to be linked to the thiosemicarbazone moiety. The biological activity was evaluated on commercial mushroom tyrosinase which was purified prior use. The results demonstrated that several of our compounds (1a-h, 1j, 1r and 5) had more potent inhibitory activities than kojic acid which was used as the reference inhibitor. (C) 2011 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2011.07.003

文献信息

• Refinement of arylthiosemicarbazone pharmacophore in inhibition of mushroom tyrosinase
  作者：Wei Yi、Carole Dubois、Samir Yahiaoui、Romain Haudecoeur、Catherine Belle、Huacan Song、Renaud Hardré、Marius Réglier、Ahcène Boumendjel

  DOI：10.1016/j.ejmech.2011.07.003

  日期：2011.9

  Melanin play a major role in human skin protection and their biosynthesis is vital. Due to their color, they contribute to the skin pigmentation. Tyrosinase is a key enzyme involved in the first stage of melanin biosynthesis, it catalyzes the transformation of tyrosine into L-dopaquinone. The aim of the present study was to study molecules able to inhibit tyrosinase to be used in treating depigmentation-related disorders. In this study, we targeted arylthiosemicarbazone analogs with the aim to contribute to the identification of the optimal aryl ring to be linked to the thiosemicarbazone moiety. The biological activity was evaluated on commercial mushroom tyrosinase which was purified prior use. The results demonstrated that several of our compounds (1a-h, 1j, 1r and 5) had more potent inhibitory activities than kojic acid which was used as the reference inhibitor. (C) 2011 Elsevier Masson SAS. All rights reserved.
• Ditopic Chelators of Dicopper Centers for Enhanced Tyrosinases Inhibition
  作者：Elina Buitrago、Clarisse Faure、Lylia Challali、Elisabetta Bergantino、Ahcène Boumendjel、Luigi Bubacco、Marcello Carotti、Renaud Hardré、Marc Maresca、Christian Philouze、Hélène Jamet、Marius Réglier、Catherine Belle

  DOI：10.1002/chem.202004695

  日期：2021.3

  particular for HOPNO‐TSC. To elucidate the interaction mode with the dicopper(II) active site, binding studies with a tyrosinase bio‐inspired model of the dicopper(II) center were investigated. The structure of the isolated adduct between one ditopic inhibitor (KA‐TSC) and the model complex reveals that the binding to a dicopper center can occur with both chelating sites. Computational studies on model complexes

  酪氨酸酶（Tys）参与黑色素（保护性色素）生物合成的关键步骤，靶向酪氨酸酶上双核铜活性位点的分子代表了调节酶活性的相关策略。在这项工作中，研究了由已知抑制剂组合产生的可能的协同作用。为此，含有曲酸（KA）和2-羟基吡啶-N的衍生物合成了氧化硫（HOPNO）和硫代半脲（TSC）部分。对来自不同来源（蘑菇，细菌和人）的纯化酪氨酸酶以及人黑素瘤MNT-1细胞系裂解液产生黑色素的抑制活性进行了评估。结果显示，与母体化合物相比，抑制作用显着增强，尤其是对HOPNO-TSC。为了阐明与dicopper（II）活性位点的相互作用方式，对酪氨酸酶生物启发的dicopper（II）中心模型的结合研究进行了研究。一个双位抑制剂（KA-TSC）与模型复合物之间的分离加合物的结构表明，两个螯合位点均可发生与双铜中心的结合。