(E)-4-(3-(4-hydroxy-3-methoxyphenyl)-3-oxoprop-1-en-1-yl)benzoic acid

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 直链 1,3-二芳基丙烷
• 英文名称: (E)-4-(3-(4-hydroxy-3-methoxyphenyl)-3-oxoprop-1-en-1-yl)benzoic acid
• 英文别名: 4-[(E)-3-(4-hydroxy-3-methoxyphenyl)-3-oxoprop-1-enyl]benzoic acid
• 化学式: C₁₇H₁₄O₅
• 分子量: 298.295
• InChiKey: GADBODJYJJFTRG-XBXARRHUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.2
• 重原子数：
  22
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.06
• 拓扑面积：
  83.8
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  对醛基苯甲酸 、 香草乙酮 在 potassium hydroxide 作用下， 反应 24.0h， 以49%的产率得到(E)-4-(3-(4-hydroxy-3-methoxyphenyl)-3-oxoprop-1-en-1-yl)benzoic acid
  参考文献：
  名称：

  A chalcone derivative binds a putative allosteric site of YopH: Inhibition of a virulence factor of Yersinia

  摘要：

  Identification of allosteric inhibitors of PTPs has attracted great interest as a new strategy to overcome the challenge of discover potent and selective molecules for therapeutic intervention. YopH is a virulence factor of the genus Yersinia , validated as an antimicrobial target. The finding of a second substrate binding site in YopH has revealed a putative allosteric site that could be further exploited. Novel chalcone compounds that inhibit PTPs activity were designed and synthesized. Compound 3j was the most potent inhibitor, interestingly, with different mechanisms of inhibition for the panel of enzymes evaluated. Further, our results showed that com- pound 3j is an irreversible non-competitive inhibitor of YopH that binds to a site different than the catalytic site, but close to the well-known second binding site of YopH.

  DOI：

  10.1016/j.bmcl.2020.127350

文献信息

• A chalcone derivative binds a putative allosteric site of YopH: Inhibition of a virulence factor of Yersinia
  作者：Ana C.A. de Souza、Mattia Mori、Larissa Sens、Ruth F. Rocha、Tiago Tizziani、Luiz F.S. de Souza、Louise Domeneghini Chiaradia-Delatorre、Maurizio Botta、Ricardo J. Nunes、Hernán Terenzi、Angela C.O. Menegatti

  DOI：10.1016/j.bmcl.2020.127350

  日期：2020.8

  Identification of allosteric inhibitors of PTPs has attracted great interest as a new strategy to overcome the challenge of discover potent and selective molecules for therapeutic intervention. YopH is a virulence factor of the genus Yersinia , validated as an antimicrobial target. The finding of a second substrate binding site in YopH has revealed a putative allosteric site that could be further exploited. Novel chalcone compounds that inhibit PTPs activity were designed and synthesized. Compound 3j was the most potent inhibitor, interestingly, with different mechanisms of inhibition for the panel of enzymes evaluated. Further, our results showed that com- pound 3j is an irreversible non-competitive inhibitor of YopH that binds to a site different than the catalytic site, but close to the well-known second binding site of YopH.