2-(2-benzoyloxy-3-methoxyphenyl)benzothiazole

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 缩酚酸和缩酚酸环醚类
• 英文名称: 2-(2-benzoyloxy-3-methoxyphenyl)benzothiazole
• 英文别名: [2-(1,3-Benzothiazol-2-yl)-6-methoxyphenyl] benzoate；[2-(1,3-benzothiazol-2-yl)-6-methoxyphenyl] benzoate
• 化学式: C₂₁H₁₅NO₃S
• 分子量: 361.421
• InChiKey: JGHIPJWMIOZUBZ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.4
• 重原子数：
  26
• 可旋转键数：
  5
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.05
• 拓扑面积：
  76.7
• 氢给体数：
  0
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  2-(2-benzoyloxy-3-methoxyphenyl)benzothiazole 在 human carboxylesterase 1 作用下， 以 aq. phosphate buffer 为溶剂， 反应 0.33h， 生成 2-(2'-hydroxy-3'-methoxyphenyl)benzothiazole
  参考文献：
  名称：

  Assessment of the inhibitory effects of pyrethroids against human carboxylesterases

  摘要：

  Pyrethroids are broad-spectrum insecticides that widely used in many countries, while humans may be exposed to these toxins by drinking or eating pesticide-contaminated foods. This study aimed to investigate the inhibitory effects of six commonly used pyrethroids against two major human carboxylesterases (CES) including CES1 and CES2. Three optical probe substrates for CES1 (DME, BMBT and DMCB) and a fluorescent probe substrate for CES2 (DDAB) were used to characterize the inhibitory effects of these pyrethroids. The results demonstrated that most of the tested pyrethroids showed moderate to weak inhibitory effects against both CES1 and CES2, but deltamethrin displayed strong inhibition towards CES1. The IC50 values of deltamethrin against CES1-mediated BMBT, DME, and DMCB hydrolysis were determined as 1.58 mu M, 2.39 mu M, and 33 mu M, respectively. Moreover, deltamethrin was cell membrane permeable and capable of inhibition endogenous CES1 in living cells. Further investigation revealed that deltamethrin inhibited CES1-mediated BMBT hydrolysis via competitive manner but noncompetitively inhibited DME or DMCB hydrolysis. The inhibition behaviors of deltamethrin against CES1 were also studied by molecular docking simulation. The results demonstrated that CES1 had at least two different ligand-binding sites, one was the DME site and another was the BMBT site which was identical to the binding site of deltamethrin. In summary, deltamethrin was a strong reversible inhibitor against CES1 and it could tightly bind on CES1 at the same ligand-binding site as BMBT. These findings are helpful for the deep understanding of the interactions between xenobiotics and CES1. (C) 2017 Elsevier Inc. All rights reserved.

  DOI：

  10.1016/j.taap.2017.02.018

文献信息

• Palladium catalyzed ortho-halogenation of 2-arylbenzothiazole and 2,3-diarylquinoxaline
  作者：Sourav Kumar Santra、Arghya Banerjee、Nilufa Khatun、Asim Samanta、Bhisma K. Patel

  DOI：10.1039/c4ra15461d

  日期：——

  A Pd-catalysed mono and di-o-halogenation strategy has been demonstrated selectively using benzothiazoles and quinoxalines as the directing substrates.

  使用苯并噻唑和喹啉作为定向底物，已经演示了一种Pd催化的单一和双卤代策略。
• Assessment of the inhibitory effects of pyrethroids against human carboxylesterases
  作者：Wei Lei、Dan-Dan Wang、Tong-Yi Dou、Jie Hou、Liang Feng、Heng Yin、Qun Luo、Jie Sun、Guang-Bo Ge、Ling Yang

  DOI：10.1016/j.taap.2017.02.018

  日期：2017.4

  Pyrethroids are broad-spectrum insecticides that widely used in many countries, while humans may be exposed to these toxins by drinking or eating pesticide-contaminated foods. This study aimed to investigate the inhibitory effects of six commonly used pyrethroids against two major human carboxylesterases (CES) including CES1 and CES2. Three optical probe substrates for CES1 (DME, BMBT and DMCB) and a fluorescent probe substrate for CES2 (DDAB) were used to characterize the inhibitory effects of these pyrethroids. The results demonstrated that most of the tested pyrethroids showed moderate to weak inhibitory effects against both CES1 and CES2, but deltamethrin displayed strong inhibition towards CES1. The IC50 values of deltamethrin against CES1-mediated BMBT, DME, and DMCB hydrolysis were determined as 1.58 mu M, 2.39 mu M, and 33 mu M, respectively. Moreover, deltamethrin was cell membrane permeable and capable of inhibition endogenous CES1 in living cells. Further investigation revealed that deltamethrin inhibited CES1-mediated BMBT hydrolysis via competitive manner but noncompetitively inhibited DME or DMCB hydrolysis. The inhibition behaviors of deltamethrin against CES1 were also studied by molecular docking simulation. The results demonstrated that CES1 had at least two different ligand-binding sites, one was the DME site and another was the BMBT site which was identical to the binding site of deltamethrin. In summary, deltamethrin was a strong reversible inhibitor against CES1 and it could tightly bind on CES1 at the same ligand-binding site as BMBT. These findings are helpful for the deep understanding of the interactions between xenobiotics and CES1. (C) 2017 Elsevier Inc. All rights reserved.