(R)-3-hydroxymethyl-5-methyl-1,3-dihydrobenzo[e][1,4]diazepin-2-one | 1310683-94-3

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯二氮卓类
• 英文名称: (R)-3-hydroxymethyl-5-methyl-1,3-dihydrobenzo[e][1,4]diazepin-2-one
• 英文别名: (3R)-3-(hydroxymethyl)-5-methyl-1,3-dihydro-1,4-benzodiazepin-2-one
• CAS: 1310683-94-3
• 化学式: C₁₁H₁₂N₂O₂
• 分子量: 204.228
• InChiKey: LSNGVRBLROMLJC-SNVBAGLBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.7
• 重原子数：
  15
• 可旋转键数：
  1
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  61.7
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  (R)-3-hydroxymethyl-5-methyl-1,3-dihydrobenzo[e][1,4]diazepin-2-one 在 咪唑 、 Hoveyda-Grubbs catalyst second generation 、 四丁基氟化铵 、 sodium hydride 、 Methanaminium,N-[(dimethylamino)(3H-1,2,3-triazolo[4,5-b]pyridin-3-yloxy)methylene]-N-methyl-, hexafluorophosphate(1-) 、 lithium hydroxide 作用下， 以 四氢呋喃 、 甲醇 、 二氯甲烷 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 49.0h， 生成 (4-chloro-2-trifluoromethyl-phenyl)-carbamic acid 5-methyl-2-oxo-1-[(4-oxo-pent-2-enylcarbamoyl)-methyl]-2,3-dihydro-1H-benzo[e][1,4]diazepin-3-ylmethyl ester
  参考文献：
  名称：

  Peptidomimetics containing a vinyl ketone warhead as falcipain-2 inhibitors

  摘要：

  The design, chemical synthesis, and enzymatic activity evaluation of a set of falcipain-2 inhibitors are reported. These compounds contain a proven peptidomimetic recognition motif based on a benzo[1,4] diazepin-2-one (1,4-BDZ) framework built on a dipeptide sequence, and a Michael acceptor terminal moiety capable of deactivating the cysteine protease active site. Our goal is to modify the P-3 site of this motif in order to identify the structural requirements for the interaction with the target. (C) 2011 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2011.02.058
• 作为产物：
  描述：

  tert-butyl (4R)-4-[(2-acetylphenyl)carbamoyl]-2,2-dimethyl-1,3-oxazolidine-3-carboxylate 在 盐酸 、 碳酸氢钠 作用下， 以 甲醇 、 水 为溶剂， 反应 17.0h， 以92%的产率得到(R)-3-hydroxymethyl-5-methyl-1,3-dihydrobenzo[e][1,4]diazepin-2-one
  参考文献：
  名称：

  Peptidomimetics containing a vinyl ketone warhead as falcipain-2 inhibitors

  摘要：

  The design, chemical synthesis, and enzymatic activity evaluation of a set of falcipain-2 inhibitors are reported. These compounds contain a proven peptidomimetic recognition motif based on a benzo[1,4] diazepin-2-one (1,4-BDZ) framework built on a dipeptide sequence, and a Michael acceptor terminal moiety capable of deactivating the cysteine protease active site. Our goal is to modify the P-3 site of this motif in order to identify the structural requirements for the interaction with the target. (C) 2011 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2011.02.058