(E)-6-Styrylisatin | 132888-01-8

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 二苯乙烯类
• 英文名称: (E)-6-Styrylisatin
• 英文别名: 6-trans-styryl-indoline-2,3-dione；6-trans-Styryl-indolin-2,3-dion；6-[(E)-2-phenylethenyl]-1H-indole-2,3-dione
• CAS: 132888-01-8
• 化学式: C₁₆H₁₁NO₂
• 分子量: 249.269
• InChiKey: ZQOJVXBKHOCLGH-VOTSOKGWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.1
• 重原子数：
  19
• 可旋转键数：
  2
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  46.2
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  (E)-6-Styrylisatin 在 sodium hydroxide 、 双氧水 作用下， 生成 3-amino-trans-stilbene-4-carboxylic acid
  参考文献：
  名称：

  Langenbeck et al., Journal fur praktische Chemie (Leipzig 1954), 1957, vol. <4> 4, p. 136,145

  摘要：

  DOI：
• 作为产物：
  描述：

  在 air 作用下， 生成 (E)-6-Styrylisatin
  参考文献：
  名称：

  Inhibition of monoamine oxidase by (E)-styrylisatin analogues

  摘要：

  Previous studies have shown that (E)-8-(3-chlorostyryl) caffeine (CSC) is a specific reversible inhibitor of human monoamine oxidase B (MAO-B) and does not bind to human MAO-A. Since the small molecule isatin is a natural reversible inhibitor of both MAO-B and MAO-A, (E)-5-styrylisatin and (E)-6-styrylisatin analogues were synthesized in an attempt to identify inhibitors with enhanced potencies and specificities for MAO-B. The (E)-styrylisatin analogues were found to exhibit higher binding affinities than isatin with the MAO preparations tested. The (E)-5-styrylisatin analogues bound more tightly than the (E)-6 analogue although the latter exhibits the highest MAO-B selectivity. Molecular docking studies with MAO-B indicate that the increased binding affinity exhibited by the (E)-styrylisatin analogues, in comparison to isatin, is best explained by the ability of the styrylisatins to bridge both the entrance cavity and the substrate cavity of the enzyme. Experimental support for this model is shown by the weaker binding of the analogues to the Ile199Ala mutant of human MAO-B. The lower selectivity of the (E)-styrylisatin analogues between MAO-A and MAO-B, in contrast to CSC, is best explained by the differing relative geometries of the aromatic rings for these two classes of inhibitors. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2009.03.030

文献信息

• Langenbeck et al., Journal fur praktische Chemie (Leipzig 1954), 1957, vol. <4> 4, p. 136,145
  作者：Langenbeck et al.

  DOI：——

  日期：——
• Inhibition of monoamine oxidase by (E)-styrylisatin analogues
  作者：Elizna M. Van der Walt、Erika M. Milczek、Sarel F. Malan、Dale E. Edmondson、Neal Castagnoli、Jacobus J. Bergh、Jacobus P. Petzer

  DOI：10.1016/j.bmcl.2009.03.030

  日期：2009.5

  Previous studies have shown that (E)-8-(3-chlorostyryl) caffeine (CSC) is a specific reversible inhibitor of human monoamine oxidase B (MAO-B) and does not bind to human MAO-A. Since the small molecule isatin is a natural reversible inhibitor of both MAO-B and MAO-A, (E)-5-styrylisatin and (E)-6-styrylisatin analogues were synthesized in an attempt to identify inhibitors with enhanced potencies and specificities for MAO-B. The (E)-styrylisatin analogues were found to exhibit higher binding affinities than isatin with the MAO preparations tested. The (E)-5-styrylisatin analogues bound more tightly than the (E)-6 analogue although the latter exhibits the highest MAO-B selectivity. Molecular docking studies with MAO-B indicate that the increased binding affinity exhibited by the (E)-styrylisatin analogues, in comparison to isatin, is best explained by the ability of the styrylisatins to bridge both the entrance cavity and the substrate cavity of the enzyme. Experimental support for this model is shown by the weaker binding of the analogues to the Ile199Ala mutant of human MAO-B. The lower selectivity of the (E)-styrylisatin analogues between MAO-A and MAO-B, in contrast to CSC, is best explained by the differing relative geometries of the aromatic rings for these two classes of inhibitors. (C) 2009 Elsevier Ltd. All rights reserved.