8-hydroxyquinoline-5-sulfonamide | 109024-18-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 喹啉及其衍生物
• 英文名称: 8-hydroxyquinoline-5-sulfonamide
• 英文别名: 8-Hydroxyquinoline-5-sulfonamide
• CAS: 109024-18-2
• 化学式: C₉H₈N₂O₃S
• 分子量: 224.24
• InChiKey: QPXVCGVHJVUJSW-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.8
• 重原子数：
  15
• 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：
  102
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  8-羟基喹啉-5-磺酸水合物 在 氯磺酸 、 氨 作用下， 以 乙腈 为溶剂， 反应 1.0h， 生成 8-hydroxyquinoline-5-sulfonamide
  参考文献：
  名称：

  Structural Basis for Inhibition of the Fat Mass and Obesity Associated Protein (FTO)

  摘要：

  The fat mass and obesity associated protein (FTO) is a potential target for anti-obesity medicines. FTO is a 2-oxoglutarate (2OG)-dependent N-methyl nucleic acid demethylase that acts on substrates including 3-methylthymidine, 3-methyluracil, and 6-methyladenine. To identify FTO inhibitors, we screened a set of 2OG analogues and related compounds using differential scanning fluorometry- and liquid chromatography-based assays. The results revealed sets of both cyclic and acyclic 2OG analogues that are FTO inhibitors. Identified inhibitors include small molecules that have been used in clinical studies for the inhibition of other 2OG oxygenases. Crystallo-graphic analyses reveal inhibition by 2OG cosubstrate or primary substrate competitors as well as compounds that bind across both cosubstrate and primary substrate binding sites. The results will aid the development of more potent and selective FTO inhibitors.

  DOI：

  10.1021/jm400193d

文献信息

• Betti reaction enables efficient synthesis of 8-hydroxyquinoline inhibitors of 2-oxoglutarate oxygenases
  作者：C. C. Thinnes、A. Tumber、C. Yapp、G. Scozzafava、T. Yeh、M. C. Chan、T. A. Tran、K. Hsu、H. Tarhonskaya、L. J. Walport、S. E. Wilkins、E. D. Martinez、S. Müller、C. W. Pugh、P. J. Ratcliffe、P. E. Brennan、A. Kawamura、C. J. Schofield

  DOI：10.1039/c5cc06095h

  日期：——

  A Betti reaction was used for efficient generation of 2OG oxygenase inhibitors, including for KDM4 demethylases.

  使用Betti反应高效生成2OG氧化酶抑制剂，包括KDM4去甲基酶。
• 10.1016/j.bioorg.2024.107705
  作者：Joaquim, Angélica Rocha、Lopes, Marcela Silva、Fortes, Isadora Serraglio、de Bem Gentz, Caroline、de Matos Czeczot, Alexia、Perelló, Marcia Alberton、Roth, Candida Deves、Vainstein, Marilene Henning、Basso, Luiz Augusto、Bizarro, Cristiano Valim、Machado, Pablo、de Andrade, Saulo Fernandes

  DOI：10.1016/j.bioorg.2024.107705

  日期：——

  screening against the microorganism of a small antimicrobial library and its new derivatives that possess some structural similarity with InhA inhibitors identified four 7-substituted-8HQ (series , , and ) and four 5-substituted-8HQ active derivatives (series , , and ). In general, the 7-substituted 8-HQs were more potent and, in the enzymatic assay, were able to inhibit InhA at low micromolar range

  耐药菌株的日益流行刺激了新候选药物的发现。其中包括具有抗菌特性的8-羟基喹啉（8HQ）衍生物。不幸的是，缺乏评估此类主要针对烯酰酰基载体蛋白还原酶（InhA）的可能靶标的数据，而InhA是该领域经过验证的靶标。因此，本研究的主要目的是鉴定对 InhA 有活性的 8HQ 衍生物。最初，针对微生物的小型抗菌文库及其与 InhA 抑制剂具有一定结构相似性的新衍生物的筛选确定了四种 7-取代-8HQ（系列 、 和 ）和四种 5-取代-8HQ 活性衍生物（系列 、 、和 ）。一般来说，7-取代的 8-HQ 更有效，并且在酶测定中能够在低微摩尔范围内抑制 InhA。然而，具有抗分枝杆菌活性的 5-取代-8-HQ 不能抑制 InhA。这些发现表明 8-HQ 衍生物的非混杂性质，并强调选择适当取代基以实现酶抑制的重要性。最后，7-取代-8HQ 系列是基于结构的药物设计和进一步开发的有前途的新衍生物。
• Structural Basis for Inhibition of the Fat Mass and Obesity Associated Protein (FTO)
  作者：WeiShen Aik、Marina Demetriades、Muhammad K. K. Hamdan、Eleanor. A. L. Bagg、Kar Kheng Yeoh、Clarisse Lejeune、Zhihong Zhang、Michael A. McDonough、Christopher J. Schofield

  DOI：10.1021/jm400193d

  日期：2013.5.9

  The fat mass and obesity associated protein (FTO) is a potential target for anti-obesity medicines. FTO is a 2-oxoglutarate (2OG)-dependent N-methyl nucleic acid demethylase that acts on substrates including 3-methylthymidine, 3-methyluracil, and 6-methyladenine. To identify FTO inhibitors, we screened a set of 2OG analogues and related compounds using differential scanning fluorometry- and liquid chromatography-based assays. The results revealed sets of both cyclic and acyclic 2OG analogues that are FTO inhibitors. Identified inhibitors include small molecules that have been used in clinical studies for the inhibition of other 2OG oxygenases. Crystallo-graphic analyses reveal inhibition by 2OG cosubstrate or primary substrate competitors as well as compounds that bind across both cosubstrate and primary substrate binding sites. The results will aid the development of more potent and selective FTO inhibitors.