(2E)-1-(2-naphthyl)-3-(3-methoxy-4-benzyloxyphenyl)-2-propen-1-one | 1258008-16-0

• 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: (2E)-1-(2-naphthyl)-3-(3-methoxy-4-benzyloxyphenyl)-2-propen-1-one
• 英文别名: (E)-3-(3-methoxy-4-phenylmethoxyphenyl)-1-naphthalen-2-ylprop-2-en-1-one
• CAS: 1258008-16-0
• 化学式: C₂₇H₂₂O₃
• 分子量: 394.47
• InChiKey: HTVOJACZNBGXGN-RVDMUPIBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.4
• 重原子数：
  30
• 可旋转键数：
  7
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.07
• 拓扑面积：
  35.5
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  4-苄氧基-3-甲氧基苯甲醛 、 2-萘乙酮 在 potassium hydroxide 作用下， 以 甲醇 、 水 为溶剂， 反应 24.0h， 以63%的产率得到(2E)-1-(2-naphthyl)-3-(3-methoxy-4-benzyloxyphenyl)-2-propen-1-one
  参考文献：
  名称：

  Synthesis, Biological Evaluation, And Molecular Modeling of Chalcone Derivatives As Potent Inhibitors of Mycobacterium tuberculosis Protein Tyrosine Phosphatases (PtpA and PtpB)

  摘要：

  Tuberculosis (TB) is a major infectious disease caused by Mycobacterium tuberculosis (Mtb). According to the World Health Organization (WHO), about 1.8 million people die from TB and 10 million new cases are recorded each year. Recently, a new series of naphthylchalcones has been identified as inhibitors of Mtb protein tyrosine phosphatases (PTPs). In this work, 100 chalcones were designed, synthesized, and investigated for their inhibitory properties against MtbPtps. Structure-activity relationships (SAR) were developed, leading to the discovery of new potent inhibitors with IC50 values in the low-micromolar range. Kinetic studies revealed competitive inhibition and high selectivity toward the Mtb enzymes. Molecular modeling investigations were carried out with the aim of revealing the most relevant structural requirements underlying the binding affinity and selectivity of this series of inhibitors as potential anti-TB drugs.

  DOI：

  10.1021/jm2012062

文献信息

• Naphthylchalcones induce apoptosis and caspase activation in a leukemia cell line: The relationship between mitochondrial damage, oxidative stress, and cell death
  作者：Evelyn Winter、Louise Domeneghini Chiaradia、Clarissa A.S. de Cordova、Ricardo José Nunes、Rosendo Augusto Yunes、Tânia Beatriz Creczynski-Pasa

  DOI：10.1016/j.bmc.2010.09.025

  日期：2010.11

  In this study, we investigated the effects of 24 chalcone derivatives from 2-naphthylacetophenone toward a lymphoblastic leukemia cell line (L1210). Three compounds, called R7, R13, and R15, presented concentration- and time-dependent cytotoxicity and induced cellular death by apoptosis via mitochondrial injury and oxidative stress. The effects of these compounds appear to occur through different mechanisms because R13 and R7 induced a greater disturbance of mitochondrial potential, and all compounds induced disturbances of cellular ATP content and increased caspase-3 activity before cellular death. These compounds also interfered with antioxidant enzymes activities and GSH content through different mechanisms. (C) 2010 Elsevier Ltd. All rights reserved.
• Synthesis, Biological Evaluation, And Molecular Modeling of Chalcone Derivatives As Potent Inhibitors of Mycobacterium tuberculosis Protein Tyrosine Phosphatases (PtpA and PtpB)
  作者：Louise Domeneghini Chiaradia、Priscila Graziela Alves Martins、Marlon Norberto Sechini Cordeiro、Rafael Victorio Carvalho Guido、Gabriela Ecco、Adriano Defini Andricopulo、Rosendo Augusto Yunes、Javier Vernal、Ricardo José Nunes、Hernán Terenzi

  DOI：10.1021/jm2012062

  日期：2012.1.12

  Tuberculosis (TB) is a major infectious disease caused by Mycobacterium tuberculosis (Mtb). According to the World Health Organization (WHO), about 1.8 million people die from TB and 10 million new cases are recorded each year. Recently, a new series of naphthylchalcones has been identified as inhibitors of Mtb protein tyrosine phosphatases (PTPs). In this work, 100 chalcones were designed, synthesized, and investigated for their inhibitory properties against MtbPtps. Structure-activity relationships (SAR) were developed, leading to the discovery of new potent inhibitors with IC50 values in the low-micromolar range. Kinetic studies revealed competitive inhibition and high selectivity toward the Mtb enzymes. Molecular modeling investigations were carried out with the aim of revealing the most relevant structural requirements underlying the binding affinity and selectivity of this series of inhibitors as potential anti-TB drugs.