6-(2-Chlorophenyl)-2,4-dioxo-hexanoic acid

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 酮酸及其衍生物
• 英文名称: 6-(2-Chlorophenyl)-2,4-dioxo-hexanoic acid
• 英文别名: 6-(2-chlorophenyl)-2,4-dioxohexanoic acid
• 化学式: C₁₂H₁₁ClO₄
• 分子量: 254.67
• InChiKey: NSGKCQNNKXAXKH-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2
• 重原子数：
  17
• 可旋转键数：
  6
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  71.4
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  2-氯苄溴 在 potassium carbonate 、 二甲基亚砜 、 sodium chloride 、 lithium diisopropyl amide 作用下， 以 四氢呋喃 、 甲苯 为溶剂， 生成 6-(2-Chlorophenyl)-2,4-dioxo-hexanoic acid
  参考文献：
  名称：

  Triketoacid inhibitors of HIV-integrase: A new chemotype useful for probing the integrase pharmacophore

  摘要：

  Integrase is one of three enzymes expressed by HIV and represents a validated target for therapy. This study reports on the discovery of a new triketoacid-based chemotype that selectively inhibits the strand transfer reaction of HIV-integrase. SAR studies showed that the template binds to integrase in a manner similar to the diketoacid-based inhibitors. Moreover, comparison of the new chemotype to two different diketoacid templates led us to propose two aryl-binding domains in the inhibitor binding site. This information was used to design a new diketoacid template with improved activity against the enzyme. (c) 2006 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2006.03.010

文献信息

• Triketoacid inhibitors of HIV-integrase: A new chemotype useful for probing the integrase pharmacophore
  作者：Michael A. Walker、Timothy Johnson、Zhuping Ma、Jacques Banville、Roger Remillard、Oak Kim、Yunhui Zhang、Andrew Staab、Henry Wong、Albert Torri、Himadri Samanta、Zeyu Lin、Carol Deminie、Brian Terry、Mark Krystal、Nicholas Meanwell

  DOI：10.1016/j.bmcl.2006.03.010

  日期：2006.6

  Integrase is one of three enzymes expressed by HIV and represents a validated target for therapy. This study reports on the discovery of a new triketoacid-based chemotype that selectively inhibits the strand transfer reaction of HIV-integrase. SAR studies showed that the template binds to integrase in a manner similar to the diketoacid-based inhibitors. Moreover, comparison of the new chemotype to two different diketoacid templates led us to propose two aryl-binding domains in the inhibitor binding site. This information was used to design a new diketoacid template with improved activity against the enzyme. (c) 2006 Elsevier Ltd. All rights reserved.