(4-formylphenyl) 2-methoxybenzoate | 671756-68-6

• 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: (4-formylphenyl) 2-methoxybenzoate
• CAS: 671756-68-6
• 化学式: C₁₅H₁₂O₄
• 分子量: 256.258
• InChiKey: WKYPPLQSEGRYMD-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.6
• 重原子数：
  19
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.07
• 拓扑面积：
  52.6
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  哌啶 、 (4-formylphenyl) 2-methoxybenzoate 以 乙腈 为溶剂， 生成 (2-methoxyphenyl)(piperidin-1-yl)methanone
  参考文献：
  名称：

  Aminolysis of Y-Substituted-phenyl 2-Methoxybenzoates in Acetonitrile: Effect of the o-Methoxy Group on Reactivity and Reaction Mechanism

  摘要：

  Second-order rate constants (k(N)) were measured for aminolyses of Y-substituted-phenyl 2-methoxybenzoates 2a-i and 4-nitrophenyl X-substituted-benzoates 3a-j in MeCN at 25.0 degrees C. The Bronsted-type plot for the reactions of 2a-i with piperidine curves downward, indicating that a change in rate-determining step (RDS) occurs. The Hammett plot for the reactions of 3a-j with piperidine consists of two intersecting straight lines, which might be taken as evidence for a change in RDS. However, the nonlinear Hammett plot has been suggested not to be due to a change in RDS but rather to the stabilization of the ground state of substrates possessing an electron-donating group (EDG) (e.g., 3a-c) through a resonance interaction, since the corresponding Yukawa-Tsuno plot exhibits an excellent linear correlation with rho = 0.54 and r = 1.54. The rho value found for the reactions of 3a-j in MeCN is much smaller than that reported previously for the corresponding reactions in H2O (i.e., rho = 0.75). It is proposed that the reactions of 3a-j in MeCN proceed through a forced concerted mechanism due to instability of T-+/- in the aprotic solvent, while the reactions of 2a-i proceed through a stepwise pathway with a stabilized T-+/- through an intramolecular H-bonding interaction.

  DOI：

  10.1021/jo201387h
• 作为产物：
  描述：

  邻甲氧基苯甲酸 在 氯化亚砜 、 三乙胺 作用下， 生成 (4-formylphenyl) 2-methoxybenzoate
  参考文献：
  名称：

  Design, Synthesis and Evaluation of Rhodanine Derivatives as Aldose Reductase Inhibitors

  摘要：

  Aldose reductase (ALR) enzyme plays a significant role in conversion of excess amount of glucose into sorbitol in diabetic condition, inhibitors of which decrease the secondary complication of diabetes mellitus. To understand the structural interaction of inhibitors with ALR enzyme and develop more effective ALR inhibitors, a series of substituted 5‐phenylbenzoate containing N‐substituted rhodanine derivatives were synthesized and evaluated for their in vitro ALR inhibitory activity. Docking studies of these compounds were carried out, which revealed that the 5‐phenylbenzoate moiety deeply influenced the key π‐π stacking while 4‐oxo‐2‐thioxothiazolidines contributed in hydrogen bond interactions. The phenyl ring of benzylidene system occupied in specific pocket constituted from Phe115, Phe122, Leu300 and Cys303 while the rhodanine ring forms a tight net of hydrogen bond with Val47 at anionic binding site of the enzyme. The structural insights obtained from the docking study gave better understanding of rhodanine and macromolecular interaction and will help us in further designing and improving of ALR inhibitory activity of rhodanine analogs.

  DOI：

  10.1111/cbdd.12369

文献信息

• Aminolysis of Y-Substituted-phenyl 2-Methoxybenzoates in Acetonitrile: Effect of the <i>o</i>-Methoxy Group on Reactivity and Reaction Mechanism
  作者：Ik-Hwan Um、Ae Ri Bae

  DOI：10.1021/jo201387h

  日期：2011.9.16

  Second-order rate constants (k(N)) were measured for aminolyses of Y-substituted-phenyl 2-methoxybenzoates 2a-i and 4-nitrophenyl X-substituted-benzoates 3a-j in MeCN at 25.0 degrees C. The Bronsted-type plot for the reactions of 2a-i with piperidine curves downward, indicating that a change in rate-determining step (RDS) occurs. The Hammett plot for the reactions of 3a-j with piperidine consists of two intersecting straight lines, which might be taken as evidence for a change in RDS. However, the nonlinear Hammett plot has been suggested not to be due to a change in RDS but rather to the stabilization of the ground state of substrates possessing an electron-donating group (EDG) (e.g., 3a-c) through a resonance interaction, since the corresponding Yukawa-Tsuno plot exhibits an excellent linear correlation with rho = 0.54 and r = 1.54. The rho value found for the reactions of 3a-j in MeCN is much smaller than that reported previously for the corresponding reactions in H2O (i.e., rho = 0.75). It is proposed that the reactions of 3a-j in MeCN proceed through a forced concerted mechanism due to instability of T-+/- in the aprotic solvent, while the reactions of 2a-i proceed through a stepwise pathway with a stabilized T-+/- through an intramolecular H-bonding interaction.
• Design, Synthesis and Evaluation of Rhodanine Derivatives as Aldose Reductase Inhibitors
  作者：Yogesh P. Agrawal、Mona Y. Agrawal、Arun K. Gupta

  DOI：10.1111/cbdd.12369

  日期：2015.2

  Aldose reductase (ALR) enzyme plays a significant role in conversion of excess amount of glucose into sorbitol in diabetic condition, inhibitors of which decrease the secondary complication of diabetes mellitus. To understand the structural interaction of inhibitors with ALR enzyme and develop more effective ALR inhibitors, a series of substituted 5‐phenylbenzoate containing N‐substituted rhodanine derivatives were synthesized and evaluated for their in vitro ALR inhibitory activity. Docking studies of these compounds were carried out, which revealed that the 5‐phenylbenzoate moiety deeply influenced the key π‐π stacking while 4‐oxo‐2‐thioxothiazolidines contributed in hydrogen bond interactions. The phenyl ring of benzylidene system occupied in specific pocket constituted from Phe115, Phe122, Leu300 and Cys303 while the rhodanine ring forms a tight net of hydrogen bond with Val47 at anionic binding site of the enzyme. The structural insights obtained from the docking study gave better understanding of rhodanine and macromolecular interaction and will help us in further designing and improving of ALR inhibitory activity of rhodanine analogs.