(E)-3-(3-Hydroxyphenyl)-1-(2-nitro-phenyl)prop-2-en-1-one

• 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)-3-(3-Hydroxyphenyl)-1-(2-nitro-phenyl)prop-2-en-1-one
• 英文别名: (E)-3-(3-hydroxyphenyl)-1-(2-nitrophenyl)prop-2-en-1-one
• 化学式: C₁₅H₁₁NO₄
• 分子量: 269.257
• InChiKey: CGQOGBILLVJQTG-CMDGGOBGSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.2
• 重原子数：
  20
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  83.1
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  (E)-3-(3-Hydroxyphenyl)-1-(2-nitro-phenyl)prop-2-en-1-one 在 碘 、 sodium acetate 、 potassium ethyl xanthogenate 作用下， 以 二甲基亚砜 为溶剂， 反应 6.0h， 以81%的产率得到2-(3-hydroxyphenyl)thiochroman-4-one
  参考文献：
  名称：

  无过渡金属碘催化的脱硝 C-S 交叉偶联：获得硫铬烷衍生物的非典型途径

  摘要：

  已经开发了一种碘催化的脱硝 C-S 交叉偶联反应，以从 2'-硝基查耳酮和黄原酸盐中获得硫色酮。该策略被扩展为通过分子间 C-S 交叉偶联和醛醇反应合成三组分硫色素。该反应通过与碘/脱硝的 C-S 键形成的卤素键络合物活化查尔酮的酮基而进行，黄原酸盐/磺胺-迈克尔加成到查尔酮上。该方法也被证明可用于化学选择性还原查尔酮。该协议还用于合成生物学上重要的 3'-羟基硫黄酮和硫色素酮。

  DOI：

  10.1021/acs.joc.2c00425
• 作为产物：
  描述：

  邻硝基苯乙酮 、 间羟基苯甲醛 在 sodium hydroxide 作用下， 以 乙醇 为溶剂， 以45 %的产率得到(E)-3-(3-Hydroxyphenyl)-1-(2-nitro-phenyl)prop-2-en-1-one
  参考文献：
  名称：

  Synthesis, Antimicrobial Activities, and Molecular Modeling Studies of Agents for the Sortase A Enzyme

  摘要：

  Sortase A (SrtA) is an attractive target for developing new anti‐infective drugs that aim to interfere with essential virulence mechanisms, such as adhesion to host cells and biofilm formation. Herein, twenty hydroxy, nitro, bromo, fluoro, and methoxy substituted chalcone compounds were synthesized, antimicrobial activities and molecular modeling strategies against the SrtA enzyme were investigated. The most active compounds were found to be T2, T4, and T19 against Streptococcus mutans (S. mutans) with MIC values of 1.93, 3.8, 3.94 μg/mL, and docking scores of −6.46, −6.63, −6.73 kcal/mol, respectively. Also, these three active compounds showed better activity than the chlorohexidine (CHX) (MIC value: 4.88 μg/mL, docking score: −6.29 kcal/mol) in both in vitro and in silico. Structural stability and binding free energy analysis of S.mutans SrtA with active compounds were measured by molecular dynamic (MD) simulations throughout 100 nanoseconds (ns) time. It was observed that the stability of the critical interactions between these compounds and the target enzyme was preserved. To prove further, in vivo biological evaluation studies could be conducted for the most promising precursor compounds T2, T4, and T19, and it might open new avenues to the discovery of more potent SrtA inhibitors.

  DOI：

  10.1002/cbdv.202301659

文献信息

• Transition Metal-Free Iodine-Catalyzed Denitrative C–S Cross-Coupling: An Atypical Route to Access Thiochromane Derivatives
  作者：Anuradha Nandy、Govindasamy Sekar

  DOI：10.1021/acs.joc.2c00425

  日期：2022.6.3

  extended for a three-component synthesis of thiochromenes via intermolecular C–S cross-coupling followed by aldol reaction. The reaction proceeds via activation of the keto group of chalcone through a halogen bond complex with iodine/denitrative C–S bond formation with xanthate/sulfa-Michael addition to chalcones. The methodology was also demonstrated for chemoselective reduction of chalcones. The protocol

  已经开发了一种碘催化的脱硝 C-S 交叉偶联反应，以从 2'-硝基查耳酮和黄原酸盐中获得硫色酮。该策略被扩展为通过分子间 C-S 交叉偶联和醛醇反应合成三组分硫色素。该反应通过与碘/脱硝的 C-S 键形成的卤素键络合物活化查尔酮的酮基而进行，黄原酸盐/磺胺-迈克尔加成到查尔酮上。该方法也被证明可用于化学选择性还原查尔酮。该协议还用于合成生物学上重要的 3'-羟基硫黄酮和硫色素酮。
• Synthesis, Antimicrobial Activities, and Molecular Modeling Studies of Agents for the Sortase A Enzyme
  作者：Gizem Tatar Yilmaz、Nurettin Yayli、Tamer Tüzüner、Gözde Bozdal、Merve Salmanli、Gülin Renda、Büşra Korkmaz、Arif Bozdeveci、Şengül Alpay Karaoğlu

  DOI：10.1002/cbdv.202301659

  日期：——

  Sortase A (SrtA) is an attractive target for developing new anti‐infective drugs that aim to interfere with essential virulence mechanisms, such as adhesion to host cells and biofilm formation. Herein, twenty hydroxy, nitro, bromo, fluoro, and methoxy substituted chalcone compounds were synthesized, antimicrobial activities and molecular modeling strategies against the SrtA enzyme were investigated. The most active compounds were found to be T2, T4, and T19 against Streptococcus mutans (S. mutans) with MIC values of 1.93, 3.8, 3.94 μg/mL, and docking scores of −6.46, −6.63, −6.73 kcal/mol, respectively. Also, these three active compounds showed better activity than the chlorohexidine (CHX) (MIC value: 4.88 μg/mL, docking score: −6.29 kcal/mol) in both in vitro and in silico. Structural stability and binding free energy analysis of S.mutans SrtA with active compounds were measured by molecular dynamic (MD) simulations throughout 100 nanoseconds (ns) time. It was observed that the stability of the critical interactions between these compounds and the target enzyme was preserved. To prove further, in vivo biological evaluation studies could be conducted for the most promising precursor compounds T2, T4, and T19, and it might open new avenues to the discovery of more potent SrtA inhibitors.