3-[N-(N-tert-butoxycarbonyl-O-β-benzyl-L-aspartyl)amino]-5-(N'-hexadecanoylamino)benzoic acid | 341925-70-0

• 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: 3-[N-(N-tert-butoxycarbonyl-O-β-benzyl-L-aspartyl)amino]-5-(N'-hexadecanoylamino)benzoic acid
• 英文别名: 3-(hexadecanoylamino)-5-[[(2S)-2-[(2-methylpropan-2-yl)oxycarbonylamino]-4-oxo-4-phenylmethoxybutanoyl]amino]benzoic acid
• CAS: 341925-70-0
• 化学式: C₃₉H₅₇N₃O₈
• 分子量: 695.897
• InChiKey: BDVYHDHCYSCPRO-XIFFEERXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  9.2
• 重原子数：
  50
• 可旋转键数：
  26
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  160
• 氢给体数：
  4
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  3-[N-(N-tert-butoxycarbonyl-O-β-benzyl-L-aspartyl)amino]-5-(N'-hexadecanoylamino)benzoic acid 以3.2%的产率得到cyclo{-tetra[3-(N-(O-β-benzyl-L-aspartyl)amino)-5-(N'-palmitoyl-amino)phenylcarbonyl]-}
  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：

  Boc-L-天冬氨酸 4-苄酯 在 1-羟基苯并三唑 、 溶剂黄146 、 三乙胺 、 N,N'-二环己基碳二亚胺 、 锌 作用下， 以 氯仿 、 水 为溶剂， 反应 22.0h， 生成 3-[N-(N-tert-butoxycarbonyl-O-β-benzyl-L-aspartyl)amino]-5-(N'-hexadecanoylamino)benzoic acid
  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

文献信息

• 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.