N-(2-amino-4-methylphenyl)-4-chlorobenzene-1-sulfonamide | 196394-27-1

• 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: N-(2-amino-4-methylphenyl)-4-chlorobenzene-1-sulfonamide
• 英文别名: N-(2-amino-4-methylphenyl)-4-chlorobenzenesulfonamide
• CAS: 196394-27-1
• 化学式: C₁₃H₁₃ClN₂O₂S
• 分子量: 296.777
• InChiKey: BQQUAUHNMYIQBE-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.4
• 重原子数：
  19
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.08
• 拓扑面积：
  80.6
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  4-chloro-N-[2-[(E)-(3,5-dichloro-2-hydroxyphenyl)methylideneamino]-4-methylphenyl]benzenesulfonamide 在 水 作用下， 生成 N-(2-amino-4-methylphenyl)-4-chlorobenzene-1-sulfonamide
  参考文献：
  名称：

  Design of β-Amyloid Aggregation Inhibitors from a Predicted Structural Motif

  摘要：

  Drug design studies targeting one of the primary toxic agents in Alzheimer's disease, soluble oligomers of amyloid beta-protein (A beta), have been complicated by the rapid, heterogeneous aggregation of A beta and the resulting difficulty to structurally characterize the peptide. To address this, we have developed [Nle(35), D-Pro(37)]A beta(42), a substituted peptide inspired from molecular dynamics simulations which forms structures stable enough to be analyzed by NMR. We report herein that [Nle(35), D-Pro(37)]A beta(42) stabilizes the trimer and prevents mature fibril and beta-sheet formation. Further, [Nle(35), D-Pro(37)]A beta(42) interacts with WT A beta(42) and reduces aggregation levels and fibril formation in mixtures. Using ligand-based drug design based on [Nle(35), D-Pro(37)]A beta(42), a lead compound was identified with effects on inhibition similar to the peptide. The ability of [Nle(35), D-Pro(37)]A beta(42) and the compound to inhibit the aggregation of A beta(42) provides a novel tool to study the structure of A beta oligomers. More broadly, our data demonstrate how molecular dynamics simulation can guide experiment for further research into AD.

  DOI：

  10.1021/jm201332p

文献信息

• Design of β-Amyloid Aggregation Inhibitors from a Predicted Structural Motif
  作者：Paul A. Novick、Dahabada H. Lopes、Kim M. Branson、Alexandra Esteras-Chopo、Isabella A. Graef、Gal Bitan、Vijay S. Pande

  DOI：10.1021/jm201332p

  日期：2012.4.12

  Drug design studies targeting one of the primary toxic agents in Alzheimer's disease, soluble oligomers of amyloid beta-protein (A beta), have been complicated by the rapid, heterogeneous aggregation of A beta and the resulting difficulty to structurally characterize the peptide. To address this, we have developed [Nle(35), D-Pro(37)]A beta(42), a substituted peptide inspired from molecular dynamics simulations which forms structures stable enough to be analyzed by NMR. We report herein that [Nle(35), D-Pro(37)]A beta(42) stabilizes the trimer and prevents mature fibril and beta-sheet formation. Further, [Nle(35), D-Pro(37)]A beta(42) interacts with WT A beta(42) and reduces aggregation levels and fibril formation in mixtures. Using ligand-based drug design based on [Nle(35), D-Pro(37)]A beta(42), a lead compound was identified with effects on inhibition similar to the peptide. The ability of [Nle(35), D-Pro(37)]A beta(42) and the compound to inhibit the aggregation of A beta(42) provides a novel tool to study the structure of A beta oligomers. More broadly, our data demonstrate how molecular dynamics simulation can guide experiment for further research into AD.