(E)-3-Hydroxybenzaldehyde Semicarbazone | 120445-49-0

• 分子结构分类: 有机化合物 - 苯类化合物 - 酚类
• 英文名称: (E)-3-Hydroxybenzaldehyde Semicarbazone
• 英文别名: [(E)-(3-hydroxyphenyl)methylideneamino]urea
• CAS: 120445-49-0
• 化学式: C₈H₉N₃O₂
• 分子量: 179.178
• InChiKey: KXDJYMXFPSDOBE-BJMVGYQFSA-N

物化性质

• 密度：
  1.34±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1
• 重原子数：
  13
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  87.7
• 氢给体数：
  3
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  S-(4-叔-丁基苯甲基)[2-(1-甲基丁基)吡啶-3-基]硫代氨基甲酸酯 、 间羟基苯甲醛 在 盐酸 作用下， 以 乙醇 、 水 为溶剂， 反应 10.0h， 生成 (E)-3-Hydroxybenzaldehyde Semicarbazone
  参考文献：
  名称：

  Structure-Based Discovery of Thiosemicarbazone Metalloproteinase Inhibitors for Hemorrhage Treatment in Snakebites

  摘要：

  The venoms of snakes are composed by many toxins, which are responsible for various toxic effects including intense pain, bleeding disorders, and local tissue damage caused by hemorrhage and necrosis. The snake venom metalloproteinases (SVMPs) are proteolytic zinc-dependent enzymes acting in different hemostatic mechanisms. In this work, a structure-based molecular modeling strategy was used for the rational design, by means of a homology 3D model of an SVMP isolated from Bothrops pauloensis venom (BpMP-I), followed by synthesis and in vitro evaluation of new thiosemicarbazones as the first inhibitors of the B. pauloensis SVMP. Besides being effective for the SVMP inhibition, two molecules were shown to be effective also in vivo, inhibiting hemorrhage caused by the B. pauloensis whole venom. Docking studies on metalloproteinases from other snake species suggest that the thiosemicarbazones activity is not confined to BpMP-I, but seems to be a common feature of metzincins.

  DOI：

  10.1021/acsmedchemlett.7b00186

文献信息

• Structure-Based Discovery of Thiosemicarbazone Metalloproteinase Inhibitors for Hemorrhage Treatment in Snakebites
  作者：Francis B. Ferreira、Thiago M. Pereira、Dayane L. N. Souza、Daiana S. Lopes、Vitor Freitas、Veridiana M. R. Ávila、Arthur E. Kümmerle、Carlos Mauricio R. Sant’Anna

  DOI：10.1021/acsmedchemlett.7b00186

  日期：2017.11.9

  The venoms of snakes are composed by many toxins, which are responsible for various toxic effects including intense pain, bleeding disorders, and local tissue damage caused by hemorrhage and necrosis. The snake venom metalloproteinases (SVMPs) are proteolytic zinc-dependent enzymes acting in different hemostatic mechanisms. In this work, a structure-based molecular modeling strategy was used for the rational design, by means of a homology 3D model of an SVMP isolated from Bothrops pauloensis venom (BpMP-I), followed by synthesis and in vitro evaluation of new thiosemicarbazones as the first inhibitors of the B. pauloensis SVMP. Besides being effective for the SVMP inhibition, two molecules were shown to be effective also in vivo, inhibiting hemorrhage caused by the B. pauloensis whole venom. Docking studies on metalloproteinases from other snake species suggest that the thiosemicarbazones activity is not confined to BpMP-I, but seems to be a common feature of metzincins.