4-(2H-1,3-benzodioxol-5-yl)benzohydrazide | 1421511-66-1

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并间二氧杂环戊烯类
• 英文名称: 4-(2H-1,3-benzodioxol-5-yl)benzohydrazide
• CAS: 1421511-66-1
• 化学式: C₁₄H₁₂N₂O₃
• 分子量: 256.261
• InChiKey: ZLJRIHUEENIEAC-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.69
• 重原子数：
  19.0
• 可旋转键数：
  2.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.07
• 拓扑面积：
  73.58
• 氢给体数：
  2.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  4-(2H-1,3-benzodioxol-5-yl)benzohydrazide 、 3,5-二溴-2,4-二羟基苯甲醛 以 乙醇 、 溶剂黄146 为溶剂， 反应 3.0h， 以73%的产率得到4-(benzo[d][1,3]dioxol-5-yl)-N'-(3,5-dibromo-2,4-dihydroxybenzylidene)benzohydrazide
  参考文献：
  名称：

  Discovery and Mechanism Study of SIRT1 Activators that Promote the Deacetylation of Fluorophore-Labeled Substrate

  摘要：

  SIRT1 is an NAD(+)-dependent deacetylase, whose activators have potential therapeutic applications in age-related diseases. Here we report a new class of SIRT1 activators. The activation is dependent on the fluorophore labeled to the substrate. To elucidate the activation mechanism, we solved the crystal structure of SIRT3/ac-RHKKac-AMC complex. The structure revealed that the fluorophore blocked the H-bond formation and created a cavity between the substrate and the Rossmann fold. We built the SIRT1/ac-RHKKac-AMC complex model based on the crystal structure. K-m and K-d determinations demonstrated that the fluorophore decreased the peptide binding affinity. The binding modes of SIRT1 activators indicated that a portion of the activators interacts with the fluorophore through pi-stacking, while the portion inserts into the cavity or interacts with the Rossmann fold, thus increasing the substrate affinity. Our study provides new insights into the mechanism of SIRT1 activation and may aid the design of novel SIRT1 activators.

  DOI：

  10.1021/jm301032j
• 作为产物：
  描述：

  4-溴-1,2-亚甲二氧基苯 在 四(三苯基膦)钯 、 hydrazine hydrate 、 potassium fluoride dihydrate 作用下， 以 乙二醇二甲醚 、 乙醇 、 水 为溶剂， 反应 3.83h， 生成 4-(2H-1,3-benzodioxol-5-yl)benzohydrazide
  参考文献：
  名称：

  Discovery and Mechanism Study of SIRT1 Activators that Promote the Deacetylation of Fluorophore-Labeled Substrate

  摘要：

  SIRT1 is an NAD(+)-dependent deacetylase, whose activators have potential therapeutic applications in age-related diseases. Here we report a new class of SIRT1 activators. The activation is dependent on the fluorophore labeled to the substrate. To elucidate the activation mechanism, we solved the crystal structure of SIRT3/ac-RHKKac-AMC complex. The structure revealed that the fluorophore blocked the H-bond formation and created a cavity between the substrate and the Rossmann fold. We built the SIRT1/ac-RHKKac-AMC complex model based on the crystal structure. K-m and K-d determinations demonstrated that the fluorophore decreased the peptide binding affinity. The binding modes of SIRT1 activators indicated that a portion of the activators interacts with the fluorophore through pi-stacking, while the portion inserts into the cavity or interacts with the Rossmann fold, thus increasing the substrate affinity. Our study provides new insights into the mechanism of SIRT1 activation and may aid the design of novel SIRT1 activators.

  DOI：

  10.1021/jm301032j