S-butyl 2-oxo-2H-chromene-3-carbothioate | 1614257-60-1

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 香豆素及其衍生物
• 英文名称: S-butyl 2-oxo-2H-chromene-3-carbothioate
• 英文别名: S-butyl 2-oxochromene-3-carbothioate
• CAS: 1614257-60-1
• 化学式: C₁₄H₁₄O₃S
• 分子量: 262.329
• InChiKey: YZAQDIUEJFLWHX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.8
• 重原子数：
  18
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  68.7
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  香豆素-3-羧酸乙酯 在 4-二甲氨基吡啶 、 氯化亚砜 、 sodium hydroxide 作用下， 以 氯仿 为溶剂， 反应 4.0h， 生成 S-butyl 2-oxo-2H-chromene-3-carbothioate
  参考文献：
  名称：

  New coumarin derivatives: Design, synthesis and use as inhibitors of hMAO

  摘要：

  A series new 2H-chromene-3-carboxamides (4a-4i) and S-2H-chromene-3-carbothioates (5j-5t) were synthesized and evaluated as monoamine oxidase A and B inhibitors. Among them, compound 5k (IC50=0.21μM, IC50 iproniazid=7.65μM) showed the most activity and higher MAO-B selectivity (189.2-fold vs 1-fold) with respect to the MAO-A isoform. The need to clarify at a 3D level some important molecular aspects of discussed SAR, we undertaked a number of docking simulations to better assess. The steric effect was analyzed interms of both posing and scoring by investigating the nature of the binding interactions. The docking results of active compound 5k with hMAO-B complex indicated that conserved residue ILE 199 was important for ligand binding via Sigma-Pi interaction.

  DOI：

  10.1016/j.bmc.2014.05.002

文献信息

• New coumarin derivatives: Design, synthesis and use as inhibitors of hMAO
  作者：Xu He、Yan-Yan Chen、Jing-Bo Shi、Wen-Jiang Tang、Zhi-Xiang Pan、Zhi-Qiang Dong、Bao-An Song、Jun Li、Xin-Hua Liu

  DOI：10.1016/j.bmc.2014.05.002

  日期：2014.7

  A series new 2H-chromene-3-carboxamides (4a-4i) and S-2H-chromene-3-carbothioates (5j-5t) were synthesized and evaluated as monoamine oxidase A and B inhibitors. Among them, compound 5k (IC50=0.21μM, IC50 iproniazid=7.65μM) showed the most activity and higher MAO-B selectivity (189.2-fold vs 1-fold) with respect to the MAO-A isoform. The need to clarify at a 3D level some important molecular aspects of discussed SAR, we undertaked a number of docking simulations to better assess. The steric effect was analyzed interms of both posing and scoring by investigating the nature of the binding interactions. The docking results of active compound 5k with hMAO-B complex indicated that conserved residue ILE 199 was important for ligand binding via Sigma-Pi interaction.