1,1-Dimethyl-4-phenyl-2-phenylcarboxamidopentanoic anhydride

• 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: 1,1-Dimethyl-4-phenyl-2-phenylcarboxamidopentanoic anhydride
• 英文别名: (3-benzamido-2,2-dimethyl-5-phenylpentanoyl) 3-benzamido-2,2-dimethyl-5-phenylpentanoate
• 化学式: C₄₀H₄₄N₂O₅
• 分子量: 632.8
• InChiKey: AZTARPFJXYNPTC-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  8.3
• 重原子数：
  47
• 可旋转键数：
  16
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  102
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  3-Benzoylamino-2,2-dimethyl-5-phenyl-pentanoic acid 在 三乙胺 、 bromo-tris(1-pyrrolidinyl)phosphonium hexafluorophosphate 作用下， 以 二氯甲烷 为溶剂， 反应 3.0h， 生成 1,1-Dimethyl-4-phenyl-2-phenylcarboxamidopentanoic anhydride
  参考文献：
  名称：

  Symmetrical anhydride-type serine protease inhibitors: Structure-activity relationship studies of human chymase inhibitors

  摘要：

  We prepared a potent and relatively selective human chymase inhibitor 9 (-), based on the study of SAR of a symmetrical anhydride-type serine protease inhibitor 1. Kinetic studies suggested that 9 (-) reacts with the Ser residue at the active site of the enzyme, forming a stable acyl enzyme complex. We also showed the importance of the tri-substituted beta-amino acid structure for the potent anti-enzymatic activity, (C) 1999 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(99)00012-8

文献信息

• Symmetrical anhydride-type serine protease inhibitors: Structure-activity relationship studies of human chymase inhibitors
  作者：Kiyoko Iijima、Jun Katada、Yoshio Hayashi

  DOI：10.1016/s0960-894x(99)00012-8

  日期：1999.2

  We prepared a potent and relatively selective human chymase inhibitor 9 (-), based on the study of SAR of a symmetrical anhydride-type serine protease inhibitor 1. Kinetic studies suggested that 9 (-) reacts with the Ser residue at the active site of the enzyme, forming a stable acyl enzyme complex. We also showed the importance of the tri-substituted beta-amino acid structure for the potent anti-enzymatic activity, (C) 1999 Elsevier Science Ltd. All rights reserved.