tert-butyl 4-acetyl-3-aminobenzoate

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: tert-butyl 4-acetyl-3-aminobenzoate
• 英文别名: tert-Butyl 4-acetyl-3-aminobenzoate
• 化学式: C₁₃H₁₇NO₃
• 分子量: 235.283
• InChiKey: JPUHDYIKZGUKCU-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.6
• 重原子数：
  17
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  69.4
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  tert-butyl 4-acetyl-3-aminobenzoate 在 N-甲基吗啉 、 potassium carbonate 、 二乙胺 、 氯甲酸异丁酯 作用下， 以 N,N-二甲基甲酰胺 、 乙腈 为溶剂， 反应 26.5h， 生成 (S)-tert-butyl 1-(4-cyclohexylbenzyl)-3,5-dimethyl-2-oxo-2,3-dihydro-1H-benzo[e][1,4]diazepine-8-carboxylate
  参考文献：
  名称：

  Synthetic, structural mimetics of the β-hairpin flap of HIV-1 protease inhibit enzyme function

  摘要：

  Small-molecule mimetics of the beta-hairpin flap of HIV-1 protease (HIV-1 PR) were designed based on a 1,4-benzodiazepine scaffold as a strategy to interfere with the flap-flap protein-protein interaction, which functions as a gated mechanism to control access to the active site. Michaelis-Menten kinetics suggested our small-molecules are competitive inhibitors, which indicates the mode of inhibition is through binding the active site or sterically blocking access to the active site and preventing flap closure, as designed. More generally, a new bioactive scaffold for HIV-1PR inhibition has been discovered, with the most potent compound inhibiting the protease with a modest K-i of 11 mu M. (C) 2015 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2015.09.002
• 作为产物：
  描述：

  对乙基苯甲酸 在 chromium(VI) oxide 、 4-二甲氨基吡啶 、 硫酸 、 palladium on carbon 、 氢气 、 硝酸 、 高碘酸 、 N,N'-二环己基碳二亚胺 作用下， 以 甲醇 、 二氯甲烷 、 乙腈 为溶剂， 反应 21.0h， 生成 tert-butyl 4-acetyl-3-aminobenzoate
  参考文献：
  名称：

  Synthetic, structural mimetics of the β-hairpin flap of HIV-1 protease inhibit enzyme function

  摘要：

  Small-molecule mimetics of the beta-hairpin flap of HIV-1 protease (HIV-1 PR) were designed based on a 1,4-benzodiazepine scaffold as a strategy to interfere with the flap-flap protein-protein interaction, which functions as a gated mechanism to control access to the active site. Michaelis-Menten kinetics suggested our small-molecules are competitive inhibitors, which indicates the mode of inhibition is through binding the active site or sterically blocking access to the active site and preventing flap closure, as designed. More generally, a new bioactive scaffold for HIV-1PR inhibition has been discovered, with the most potent compound inhibiting the protease with a modest K-i of 11 mu M. (C) 2015 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2015.09.002

文献信息

• 1,3,5,8-Tetrasubstituted 1,3,4-Benzotriazepin-2-one Scaffolds for β-Turn Mimicry without Stereogenic Carbon Centers: Synthesis and Conformational Analysis
  作者：Xiaozheng Wei、Antoine Douchez、William D. Lubell

  DOI：10.1021/acs.joc.3c00113

  日期：——

  carbon center, the scaffold could serve as type I and I′ β-turn mimics, because pyramidalization of the N3-nitrogen in the benzotriazepin-2-one provides potential for adoptive chirality. 1,3,5,8-Tetrasubstituted 1,3,4-benzotriazepin-2-one scaffolds offer interesting potential for the cost-effective synthesis of nonpeptide β-turn surrogates for peptide mimicry in various recognition events.

  已使用 1,3,5,8-四取代的 1,3,4-苯并三氮卓-2-一支架研究了肽 β-转角二级结构的拓扑拟态。基于氮杂氨基酸化学和不同的正交保护策略，构思了从 4-乙酰基-3-氨基苯甲酸酯合成四取代苯并三氮杂酮的方法。在芳环上安装 8 位羧酸盐可以引入多种取代基以模拟i位残基。Benzotriazepin-2-one 结晶和 X 射线分析表明，尽管不存在立体异构碳中心，但支架可以作为 I 型和 I' 型 β-转角模拟物，因为 N 3 的金字塔化-benzotriazepin-2-one 中的氮提供了过继手性的潜力。1,3,5,8-四取代的 1,3,4-苯并三氮卓-2-一支架为在各种识别事件中模拟肽的非肽 β-转角替代物的经济高效合成提供了有趣的潜力。
• Synthetic, structural mimetics of the β-hairpin flap of HIV-1 protease inhibit enzyme function
  作者：Jay Chauhan、Shen-En Chen、Katherine J. Fenstermacher、Aurash Naser-Tavakolian、Tali Reingewertz、Rosene Salmo、Christian Lee、Emori Williams、Mithun Raje、Eric Sundberg、Jeffrey J. DeStefano、Ernesto Freire、Steven Fletcher

  DOI：10.1016/j.bmc.2015.09.002

  日期：2015.11

  Small-molecule mimetics of the beta-hairpin flap of HIV-1 protease (HIV-1 PR) were designed based on a 1,4-benzodiazepine scaffold as a strategy to interfere with the flap-flap protein-protein interaction, which functions as a gated mechanism to control access to the active site. Michaelis-Menten kinetics suggested our small-molecules are competitive inhibitors, which indicates the mode of inhibition is through binding the active site or sterically blocking access to the active site and preventing flap closure, as designed. More generally, a new bioactive scaffold for HIV-1PR inhibition has been discovered, with the most potent compound inhibiting the protease with a modest K-i of 11 mu M. (C) 2015 Elsevier Ltd. All rights reserved.