3,6-Dibromo-8-chloro-7-hydroxy-4-methylchromen-2-one | 1009809-43-1

• 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: 3,6-Dibromo-8-chloro-7-hydroxy-4-methylchromen-2-one
• CAS: 1009809-43-1
• 化学式: C₁₀H₅Br₂ClO₃
• 分子量: 368.409
• InChiKey: ILQHSNZLRHGYEY-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.7
• 重原子数：
  16
• 可旋转键数：
  0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.1
• 拓扑面积：
  46.5
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  3,6-dibromo-7-hydroxy-4-methyl-chromen-2-one 在 三氯化铝 作用下， 反应 1.0h， 以15%的产率得到3,6-Dibromo-8-chloro-7-hydroxy-4-methylchromen-2-one
  参考文献：
  名称：

  Coumarin as Attractive Casein Kinase 2 (CK2) Inhibitor Scaffold: An Integrate Approach To Elucidate the Putative Binding Motif and Explain Structure–Activity Relationships

  摘要：

  Casein kinase 2 (CK2) is an ubiquitous, essential, and highly pleiotropic protein kinase whose abnormally high constitutive activity is suspected to underlie its pathogenic potential in neoplasia and other diseases. Recently, using different virtual screening approaches, we have identified several novel CK2 inhibitors. In particular, we have discovered that coumarin moiety can be considered an attractive CK2 inhibitor scaffold. In the present work, we have synthetized and tested a small library of coumarins (more than 60), rationalizing the observed structure-activity relationship. Moreover, the most promising inhibitor, 3,8-dibromo-7-hydroxy-4-methylchromen-2-one (DBC), has been also crystallized in complex with CK2, and the experimental binding mode has been used to derive a linear interaction energy (LIE) model.

  DOI：

  10.1021/jm070909t

文献信息

• Coumarin as Attractive Casein Kinase 2 (CK2) Inhibitor Scaffold: An Integrate Approach To Elucidate the Putative Binding Motif and Explain Structure–Activity Relationships
  作者：Adriana Chilin、Roberto Battistutta、Andrea Bortolato、Giorgio Cozza、Samuele Zanatta、Giorgia Poletto、Marco Mazzorana、Giuseppe Zagotto、Eugenio Uriarte、Adriano Guiotto、Lorenzo A. Pinna、Flavio Meggio、Stefano Moro

  DOI：10.1021/jm070909t

  日期：2008.2.1

  Casein kinase 2 (CK2) is an ubiquitous, essential, and highly pleiotropic protein kinase whose abnormally high constitutive activity is suspected to underlie its pathogenic potential in neoplasia and other diseases. Recently, using different virtual screening approaches, we have identified several novel CK2 inhibitors. In particular, we have discovered that coumarin moiety can be considered an attractive CK2 inhibitor scaffold. In the present work, we have synthetized and tested a small library of coumarins (more than 60), rationalizing the observed structure-activity relationship. Moreover, the most promising inhibitor, 3,8-dibromo-7-hydroxy-4-methylchromen-2-one (DBC), has been also crystallized in complex with CK2, and the experimental binding mode has been used to derive a linear interaction energy (LIE) model.