4-(2-Phenylethyl)morpholine-2,6-dione | 1341105-35-8

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: 4-(2-Phenylethyl)morpholine-2,6-dione
• CAS: 1341105-35-8
• 化学式: C₁₂H₁₃NO₃
• 分子量: 219.24
• InChiKey: HEFUIIRRAJUSRE-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  16
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  46.6
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  (carboxymethyl(phenethyl)amino)acetic acid 在 乙酸酐 、 三氟乙酸酐 作用下， 反应 5.0h， 以100%的产率得到4-(2-Phenylethyl)morpholine-2,6-dione
  参考文献：
  名称：

  Imidazole-derived 2-[N-carbamoylmethyl-alkylamino]acetic acids, substrate-dependent modulators of insulin-degrading enzyme in amyloid-β hydrolysis

  摘要：

  Insulin degrading enzyme (IDE) is a highly conserved zinc metalloprotease that is involved in the clearance of various physiologically peptides like amyloid-beta and insulin. This enzyme has been involved in the physiopathology of diabetes and Alzheimer's disease. We describe here a series of small molecules discovered by screening. Co-crystallization of the compounds with IDE revealed a binding both at the permanent exosite and at the discontinuous, conformational catalytic site. Preliminary structure activity relationships are described. Selective inhibition of amyloid-beta degradation over insulin hydrolysis was possible. Neuroblastoma cells treated with the optimized compound display a dose-dependent increase in amyloid-beta levels. (c) 2014 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2014.04.009

文献信息

• Imidazole-derived 2-[N-carbamoylmethyl-alkylamino]acetic acids, substrate-dependent modulators of insulin-degrading enzyme in amyloid-β hydrolysis
  作者：Julie Charton、Marion Gauriot、Qing Guo、Nathalie Hennuyer、Xavier Marechal、Julie Dumont、Malika Hamdane、Virginie Pottiez、Valerie Landry、Olivier Sperandio、Marion Flipo、Luc Buee、Bart Staels、Florence Leroux、Wei-Jen Tang、Benoit Deprez、Rebecca Deprez-Poulain

  DOI：10.1016/j.ejmech.2014.04.009

  日期：2014.5

  Insulin degrading enzyme (IDE) is a highly conserved zinc metalloprotease that is involved in the clearance of various physiologically peptides like amyloid-beta and insulin. This enzyme has been involved in the physiopathology of diabetes and Alzheimer's disease. We describe here a series of small molecules discovered by screening. Co-crystallization of the compounds with IDE revealed a binding both at the permanent exosite and at the discontinuous, conformational catalytic site. Preliminary structure activity relationships are described. Selective inhibition of amyloid-beta degradation over insulin hydrolysis was possible. Neuroblastoma cells treated with the optimized compound display a dose-dependent increase in amyloid-beta levels. (c) 2014 Elsevier Masson SAS. All rights reserved.