3-bromo-N-[2-(2-hydroxyethoxy)ethyl]benzenesulfonamide | 1286282-19-6

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 3-bromo-N-[2-(2-hydroxyethoxy)ethyl]benzenesulfonamide
• CAS: 1286282-19-6
• 化学式: C₁₀H₁₄BrNO₄S
• mdl: MFCD13319020
• 分子量: 324.195
• InChiKey: DITWPDQTAAIZQI-UHFFFAOYSA-N

物化性质

• 沸点：
  473.0±55.0 °C(Predicted)
• 密度：
  1.546±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.7
• 重原子数：
  17
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.4
• 拓扑面积：
  84
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  3-bromo-N-[2-(2-hydroxyethoxy)ethyl]benzenesulfonamide 在 三乙胺 作用下， 以 二氯甲烷 、 乙腈 为溶剂， 反应 16.0h， 生成 3-bromo-N-(2-(2-(pyrrolidin-1-yl)ethoxy))ethylbenzenesulfonamide trifluroacetic acid
  参考文献：
  名称：

  Small-Molecule Ligands of Methyl-Lysine Binding Proteins

  摘要：

  Proteins which bind methylated lysines ("readers" of the histone code) are important components in the epigenetic regulation of gene expression and can also modulate other proteins that contain methyl-lysine such as p53 and Rb. Recognition of methyl-lysine marks by MBT domains leads to compaction of chromatin and a repressed transcriptional state. Antagonists of MBT domains would serve as probes to interrogate the functional role of these proteins and initiate the chemical biology of methyl-lysine readers as a target class. Small-molecule MBT antagonists were designed based on the structure of histone peptide - MBT complexes and their interaction with MBT domains determined using a chemiluminescent assay and ITC. The ligands discovered antagonize native histone peptide binding, exhibiting 5-fold stronger binding affinity to L3MBTL1 than its preferred histone peptide. The first cocrystal structure of a small molecule bound to L3MBTL1 was determined and provides new insights into binding requirements for further ligand design.

  DOI：

  10.1021/jm200045v
• 作为产物：
  描述：

  3-溴苯磺酰氯 、 二甘醇胺 在 三乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 14.0h， 生成 3-bromo-N-[2-(2-hydroxyethoxy)ethyl]benzenesulfonamide
  参考文献：
  名称：

  Small-Molecule Ligands of Methyl-Lysine Binding Proteins

  摘要：

  Proteins which bind methylated lysines ("readers" of the histone code) are important components in the epigenetic regulation of gene expression and can also modulate other proteins that contain methyl-lysine such as p53 and Rb. Recognition of methyl-lysine marks by MBT domains leads to compaction of chromatin and a repressed transcriptional state. Antagonists of MBT domains would serve as probes to interrogate the functional role of these proteins and initiate the chemical biology of methyl-lysine readers as a target class. Small-molecule MBT antagonists were designed based on the structure of histone peptide - MBT complexes and their interaction with MBT domains determined using a chemiluminescent assay and ITC. The ligands discovered antagonize native histone peptide binding, exhibiting 5-fold stronger binding affinity to L3MBTL1 than its preferred histone peptide. The first cocrystal structure of a small molecule bound to L3MBTL1 was determined and provides new insights into binding requirements for further ligand design.

  DOI：

  10.1021/jm200045v

文献信息

• [EN] BENZAZEPINE SULFONAMIDE COMPOUNDS<br/>[FR] COMPOSÉS SULFONAMIDE DE BENZAZÉPINE
  申请人：HOFFMANN LA ROCHE

  公开号：WO2016096778A1

  公开（公告）日：2016-06-23

  This invention relates to novel benzazepine sulfonamide compounds of the formula (I), wherein R4 or R5 is -SO2-NR7R8 and R1 to R8 and Y are as defined in the description and in the claims, as well as pharmaceutically acceptable salts thereof. These compounds are TLR agonists and may therefore be useful as medicaments for the treatment of diseases such as cancer, autoimmune diseases, inflammation, sepsis, allergy, asthma, graft rejection, graft-versus-host disease, immunodeficiencies, and infectious diseases.

  这项发明涉及公式（I）中的新型苯并哌啶磺酰胺化合物，其中R4或R5为-SO2-NR7R8，R1至R8和Y如描述和权利要求中所定义，并且其药学上可接受的盐。这些化合物是TLR激动剂，因此可能用作治疗癌症、自身免疫疾病、炎症、败血症、过敏、哮喘、移植排斥、移植物抗宿主病、免疫缺陷和传染病等疾病的药物。
• BENZAZEPINE SULFONAMIDE COMPOUNDS
  申请人：F. Hoffmann-La Roche AG

  公开号：EP3233835A1

  公开（公告）日：2017-10-25
• US9890124B2
  申请人：——

  公开号：US9890124B2

  公开（公告）日：2018-02-13
• Small-Molecule Ligands of Methyl-Lysine Binding Proteins
  作者：J. Martin Herold、Tim J. Wigle、Jacqueline L. Norris、Robert Lam、Victoria K. Korboukh、Cen Gao、Lindsey A. Ingerman、Dmitri B. Kireev、Guillermo Senisterra、Masoud Vedadi、Ashutosh Tripathy、Peter J. Brown、Cheryl H. Arrowsmith、Jian Jin、William P. Janzen、Stephen V. Frye

  DOI：10.1021/jm200045v

  日期：2011.4.14

  Proteins which bind methylated lysines ("readers" of the histone code) are important components in the epigenetic regulation of gene expression and can also modulate other proteins that contain methyl-lysine such as p53 and Rb. Recognition of methyl-lysine marks by MBT domains leads to compaction of chromatin and a repressed transcriptional state. Antagonists of MBT domains would serve as probes to interrogate the functional role of these proteins and initiate the chemical biology of methyl-lysine readers as a target class. Small-molecule MBT antagonists were designed based on the structure of histone peptide - MBT complexes and their interaction with MBT domains determined using a chemiluminescent assay and ITC. The ligands discovered antagonize native histone peptide binding, exhibiting 5-fold stronger binding affinity to L3MBTL1 than its preferred histone peptide. The first cocrystal structure of a small molecule bound to L3MBTL1 was determined and provides new insights into binding requirements for further ligand design.