3-(N-tert-butoxycarbonylamino)-5-aminobenzoic acid ethyl ester | 341925-61-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 3-(N-tert-butoxycarbonylamino)-5-aminobenzoic acid ethyl ester
• 英文别名: ethyl-3-amino-5-((tert-butoxycarbonyl)amino)benzoate；3-Amino-5-Boc-amino-benzoic acid ethyl ester；ethyl 3-amino-5-[(2-methylpropan-2-yl)oxycarbonylamino]benzoate
• CAS: 341925-61-9
• 化学式: C₁₄H₂₀N₂O₄
• 分子量: 280.324
• InChiKey: IWXSDUBAVTZQPH-UHFFFAOYSA-N

物化性质

• 沸点：
  390.1±32.0 °C(Predicted)
• 密度：
  1.192±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2
• 重原子数：
  20
• 可旋转键数：
  6
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  90.6
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  3-(N-tert-butoxycarbonylamino)-5-aminobenzoic acid ethyl ester 在 盐酸 、 1-羟基苯并三唑 、 三乙胺 、 N,N'-二环己基碳二亚胺 作用下， 以 1,4-二氧六环 、 氯仿 、 N,N-二甲基甲酰胺 为溶剂， 反应 45.0h， 生成 3-[N-(N-tert-butoxycarbonyl-L-alanyl)amino]-5-(N'-palmitoylamino)benzoicacid ethyl ester
  参考文献：
  名称：

  Molecular Design and Synthesis of Artificial Ion Channels Based on Cyclic Peptides Containing Unnatural Amino Acids

  摘要：

  A series of novel cyclic. peptides composed of 3 to 5 dipeptide units with alternating natural-unnatural amino acid units, have been designed and synthesized, employing 5-(N-alkanoylamino)-3-aminobenzoic acid with a long alkanoyl chain as the unnatural amino acid. All cyclic peptides with systematically varying pore size, shape, and lipophilicity are found to form ion channels with a conductance of ca. 9 pS in aqueous KCl (500 mM) upon examination by the voltage clamp method. These peptide channels are cation selective with the permeability ratio PCl-/PK+ of around 0.17. The ion channels formed by the neutral, cationic, and anionic cyclic peptides containing L-alanine, L-lysine, and L-aspartate, respectively, show the monovalent cation selectivity with the permeability ratio PNa+,/PK+ of ca. 0.39. On the basis of structural information provided by voltage-dependent blockade of the single channel current of all the tested peptides by Ca2+, we inferred that each channel is formed from a dimer of the peptide with its peptide ring constructing the channel entrance and its alkanoyl chains lining across the membrane to build up the channel pore. The experimental results are consistent with an idea that the rate of ion conduction is determined by the nature of the hydrophobic alkanoyl chain region, which is common to all the channels.

  DOI：

  10.1021/jo001079t
• 作为产物：
  描述：

  3,5-二氨基苯甲酸 在 氯化亚砜 、 三乙胺 作用下， 以 1,4-二氧六环 、 乙醇 、 水 为溶剂， 生成 3-(N-tert-butoxycarbonylamino)-5-aminobenzoic acid ethyl ester
  参考文献：
  名称：

  Factors Influencing the Activity of Nanozymes in the Cleavage of an RNA Model Substrate

  摘要：

  一系列经不同硫醇保护的2纳米金纳米颗粒被制备并研究其在裂解RNA模型底物2-羟基丙基对硝基苯磷酸酯中的效率。通过动力学分析（迈克尔斯-门特恩曲线、pH依赖性和动力学同位素效应）阐明了它们各自的催化来源。数据表明存在两种不同的作用机制：一种涉及两个锌（II）络合物，另一种涉及单个锌（II）络合物和一个侧链胍基阳离子。基于双核催化位点的机制似乎比基于金属络合物和胍基之间的协同作用更有效。

  DOI：

  10.3390/molecules24152814

文献信息

• Factors Influencing the Activity of Nanozymes in the Cleavage of an RNA Model Substrate
  作者：Czescik、Zamolo、Darbre、Mancin、Scrimin

  DOI：10.3390/molecules24152814

  日期：——

  A series of 2-nm gold nanoparticles passivated with different thiols all featuring at least one triazacyclonanone-Zn(II) complex and different flanking units (a second Zn(II) complex, a triethyleneoxymethyl derivative or a guanidinium of arginine of a peptide) were prepared and studied for their efficiency in the cleavage of the RNA-model substrate 2-hydroxypropyl-p-nitrophenyl phosphate. The source of catalysis for each of them was elucidated from the kinetic analysis (Michaelis–Menten profiles, pH dependence and kinetic isotope effect). The data indicated that two different mechanisms were operative: One involving two Zn(II) complexes and the other one involving a single Zn(II) complex and a flanking guanidinium cation. The mechanism based on a dinuclear catalytic site appeared more efficient than the one based on the cooperativity between a metal complex and a guanidinium.

  一系列经不同硫醇保护的2纳米金纳米颗粒被制备并研究其在裂解RNA模型底物2-羟基丙基对硝基苯磷酸酯中的效率。通过动力学分析（迈克尔斯-门特恩曲线、pH依赖性和动力学同位素效应）阐明了它们各自的催化来源。数据表明存在两种不同的作用机制：一种涉及两个锌（II）络合物，另一种涉及单个锌（II）络合物和一个侧链胍基阳离子。基于双核催化位点的机制似乎比基于金属络合物和胍基之间的协同作用更有效。
• Molecular Design and Synthesis of Artificial Ion Channels Based on Cyclic Peptides Containing Unnatural Amino Acids
  作者：Hitoshi Ishida、Zhi Qi、Masahiro Sokabe、Kiyoshi Donowaki、Yoshihisa Inoue

  DOI：10.1021/jo001079t

  日期：2001.5.1

  A series of novel cyclic. peptides composed of 3 to 5 dipeptide units with alternating natural-unnatural amino acid units, have been designed and synthesized, employing 5-(N-alkanoylamino)-3-aminobenzoic acid with a long alkanoyl chain as the unnatural amino acid. All cyclic peptides with systematically varying pore size, shape, and lipophilicity are found to form ion channels with a conductance of ca. 9 pS in aqueous KCl (500 mM) upon examination by the voltage clamp method. These peptide channels are cation selective with the permeability ratio PCl-/PK+ of around 0.17. The ion channels formed by the neutral, cationic, and anionic cyclic peptides containing L-alanine, L-lysine, and L-aspartate, respectively, show the monovalent cation selectivity with the permeability ratio PNa+,/PK+ of ca. 0.39. On the basis of structural information provided by voltage-dependent blockade of the single channel current of all the tested peptides by Ca2+, we inferred that each channel is formed from a dimer of the peptide with its peptide ring constructing the channel entrance and its alkanoyl chains lining across the membrane to build up the channel pore. The experimental results are consistent with an idea that the rate of ion conduction is determined by the nature of the hydrophobic alkanoyl chain region, which is common to all the channels.