N-(O3-acetyl-betulinyl)-β-alanine t-butyl ester | 1426661-52-0

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 异戊烯醇脂质
• 英文名称: N-(O3-acetyl-betulinyl)-β-alanine t-butyl ester
• 英文别名: N-[(3β)-3-(acetyloxy)-28-oxolup-20(29)-en-28-yl]-β-alanine 1-(1,1-dimethylethyl) ester；tert-butyl 3-[[(1R,3aS,5aR,5bR,7aR,9S,11aR,11bR,13aR,13bR)-9-acetyloxy-5a,5b,8,8,11a-pentamethyl-1-prop-1-en-2-yl-1,2,3,4,5,6,7,7a,9,10,11,11b,12,13,13a,13b-hexadecahydrocyclopenta[a]chrysene-3a-carbonyl]amino]propanoate
• CAS: 1426661-52-0
• 化学式: C₃₉H₆₃NO₅
• 分子量: 625.933
• InChiKey: XBRIBNDJLWLWDM-JCPXNNEOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  9.3
• 重原子数：
  45
• 可旋转键数：
  9
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.87
• 拓扑面积：
  81.7
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  N-(O3-acetyl-betulinyl)-β-alanine t-butyl ester 在 4-二甲氨基吡啶 、 sodium hydroxide 作用下， 以 四氢呋喃 、 吡啶 、 甲醇 、 水 为溶剂， 反应 30.0h， 生成 N-[3β-(3-carboxy-3-methylbutanoyloxy)lup-20,29-en-28-oyl]-β-alanine
  参考文献：
  名称：

  Synthesis and biological evaluation of a new derivative of bevirimat that targets the Gag CA-SP1 cleavage site

  摘要：

  Bevirimat (2), the first-in-class HIV-1 maturation inhibitor, shows a low efficacy due essentially to the natural polymorphism of its target, the CA-SP1 junction. Moreover, its low hydrosolubility makes it difficult to study its interaction with the CA-SP1 junction. We have synthesized new derivatives of bevirimat by adding different hydrophilic substituents at the C-28 position to improve their hydrosolubility and perform the structural study of a complex by NMR. Synthesis of the new derivatives, the effect of substituents at the C-28 position and their hydrosolubility are discussed. The ability of these molecules to inhibit viral infection and their cytotoxicity is assessed. Compared to the well-known bevirimat (2), one of our compounds (16) shows a higher hydrosolubility associated with a 2.5 fold increase in activity, a higher selectivity index and a better antiviral profile. Moreover, for the first time a direct interaction between a derivative of bevirimat (16) and the domain CA-SP1 NC is shown by NMR. Information from this study should allow us to decipher the mechanism by which bevirimat inhibits HIV-1 maturation and how the natural polymorphism of the spacer peptide SP1 triggers resistance to inhibitors. (C) 2013 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2013.01.013
• 作为产物：
  描述：

  白桦脂酸 在 (benzotriazol-1-yloxy)tripyrrolodinophosphonium hexafluorophosphate 、 N,N-二异丙基乙胺 作用下， 以 吡啶 、 N,N-二甲基甲酰胺 为溶剂， 反应 72.0h， 生成 N-(O3-acetyl-betulinyl)-β-alanine t-butyl ester
  参考文献：
  名称：

  Synthesis and biological evaluation of a new derivative of bevirimat that targets the Gag CA-SP1 cleavage site

  摘要：

  Bevirimat (2), the first-in-class HIV-1 maturation inhibitor, shows a low efficacy due essentially to the natural polymorphism of its target, the CA-SP1 junction. Moreover, its low hydrosolubility makes it difficult to study its interaction with the CA-SP1 junction. We have synthesized new derivatives of bevirimat by adding different hydrophilic substituents at the C-28 position to improve their hydrosolubility and perform the structural study of a complex by NMR. Synthesis of the new derivatives, the effect of substituents at the C-28 position and their hydrosolubility are discussed. The ability of these molecules to inhibit viral infection and their cytotoxicity is assessed. Compared to the well-known bevirimat (2), one of our compounds (16) shows a higher hydrosolubility associated with a 2.5 fold increase in activity, a higher selectivity index and a better antiviral profile. Moreover, for the first time a direct interaction between a derivative of bevirimat (16) and the domain CA-SP1 NC is shown by NMR. Information from this study should allow us to decipher the mechanism by which bevirimat inhibits HIV-1 maturation and how the natural polymorphism of the spacer peptide SP1 triggers resistance to inhibitors. (C) 2013 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2013.01.013