6-imino-2-thioxo-5-{[3,4,5-tris(methyloxy)phenyl]methyl}-2,5-dihydro-4(3H)-pyrimidinone | 108097-23-0

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚醚
• 英文名称: 6-imino-2-thioxo-5-{[3,4,5-tris(methyloxy)phenyl]methyl}-2,5-dihydro-4(3H)-pyrimidinone
• 英文别名: 6-amino-2-sulfanylidene-5-[(3,4,5-trimethoxyphenyl)methyl]-5H-pyrimidin-4-one
• CAS: 108097-23-0
• 化学式: C₁₄H₁₇N₃O₄S
• 分子量: 323.373
• InChiKey: FUUFCISRXRORLQ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1
• 重原子数：
  22
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.36
• 拓扑面积：
  127
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  ethyl 2-cyano-3-(3,4,5-trimethoxyphenyl)propanoate 、 硫脲 在 sodium ethanolate 作用下， 以 乙醇 为溶剂， 反应 6.0h， 生成 6-imino-2-thioxo-5-{[3,4,5-tris(methyloxy)phenyl]methyl}-2,5-dihydro-4(3H)-pyrimidinone
  参考文献：
  名称：

  6-Imino-2-thioxo-pyrimidinones as a new class of dipeptidyl peptidase IV inhibitors

  摘要：

  Dipeptidyl peptidase IV is a glycoprotein which removes N-terminal dipeptides from physiologically relevant polypeptides. An homologous series of 6-imino-2-thioxo-5-{[3,4,5-tris(methyloxy)phenyl]methyl}-2,5-dihydro-4(3H)-pyrimidinones has been tested for inhibition of DPP IV activity. The inhibitory effects at 0.1 mM were observed. Enzyme kinetic studies revealed that compounds inhibit DPP IV activity competitively. According to the molecular docking analysis, the inhibitors are anchored into the DPP IV hydrolytic site by interactions of the pyrimidinone core with Glu206, Tyr662, and Tyr547, with the alkyl chain entering the S1 pocket. We conclude that pyrimidinone-like compounds are a promising new scaffold for reversible inhibition of DPP IV.

  DOI：

  10.1007/s00044-010-9314-5

文献信息

• GLUNCIC, B.;KOVACEVIC, K.
  作者：GLUNCIC, B.、KOVACEVIC, K.

  DOI：——

  日期：——
• GLUNCIC B.; JAKOVINA M.; KOVACEVIC K.; KUJUNDZIC N., ACTA PHARM. JUGOSL., 36,(1986) N 4, 393-404
  作者：GLUNCIC B.、 JAKOVINA M.、 KOVACEVIC K.、 KUJUNDZIC N.

  DOI：——

  日期：——
• 6-Imino-2-thioxo-pyrimidinones as a new class of dipeptidyl peptidase IV inhibitors
  作者：Dubravko Jelić、Krunoslav Nujić、Višnja Stepanić、Krunoslav Kovačević、Donatella Verbanac

  DOI：10.1007/s00044-010-9314-5

  日期：2011.4

  Dipeptidyl peptidase IV is a glycoprotein which removes N-terminal dipeptides from physiologically relevant polypeptides. An homologous series of 6-imino-2-thioxo-5-[3,4,5-tris(methyloxy)phenyl]methyl}-2,5-dihydro-4(3H)-pyrimidinones has been tested for inhibition of DPP IV activity. The inhibitory effects at 0.1 mM were observed. Enzyme kinetic studies revealed that compounds inhibit DPP IV activity competitively. According to the molecular docking analysis, the inhibitors are anchored into the DPP IV hydrolytic site by interactions of the pyrimidinone core with Glu206, Tyr662, and Tyr547, with the alkyl chain entering the S1 pocket. We conclude that pyrimidinone-like compounds are a promising new scaffold for reversible inhibition of DPP IV.