(S)-2-amino-N^α-(tert-butyloxycarbonyl)-6-(6'-aminopyrimidine-2',4'-dion-N-yl)hexanoic acid tert-butyl ester | 218966-05-3

• 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: (S)-2-amino-N^α-(tert-butyloxycarbonyl)-6-(6'-aminopyrimidine-2',4'-dion-N-yl)hexanoic acid tert-butyl ester
• 英文别名: tert-butyl (2S)-6-[(2,4-dioxo-1H-pyrimidin-6-yl)amino]-2-[(2-methylpropan-2-yl)oxycarbonylamino]hexanoate
• CAS: 218966-05-3
• 化学式: C₁₉H₃₂N₄O₆
• 分子量: 412.486
• InChiKey: YWGHSCLQFOQJQR-LBPRGKRZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.9
• 重原子数：
  29
• 可旋转键数：
  12
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.68
• 拓扑面积：
  135
• 氢给体数：
  4
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  (S)-2-amino-N^α-(tert-butyloxycarbonyl)-6-(6'-aminopyrimidine-2',4'-dion-N-yl)hexanoic acid tert-butyl ester 在 三氟乙酸 作用下， 以 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 15.0h， 生成 (S)-2-amino-6-(8'-O-benzyl-5'-carbaisoalloxazin-10'-yl)hexanoic acid trifluoroacetate
  参考文献：
  名称：

  Efficient Syntheses of a Flavin and an 8-Hydroxy-5-deazaflavin Amino Acid and Their Incorporation into Oligopeptides

  摘要：

  We report a convenient synthesis for the cofactor amino acids (S)-3 and (S)-4 in which the C-5-ribose chain of the original riboflavin and ribo-5-deazaflavin cofactors is replaced by a C-5-amino acid side chain. Both cofactor amino acids are available in enantiomerically pure form in gram quantities and can be incorporated into oligopeptides using a standard Fmoc-based solid-phase peptide synthesis protocol. The benzyl-protecting group of the 8-hydroxy-5-deazaflavin can be cleaved by hydrogenolysis directly on the peptide. This allows the investigation of the properties of the peptide bound redox active OH- and the deprotonated O--form of the deazaflavin. Due to the electron- and energy-transfer properties of both cofactors, applications of both amino acid in the preparation of peptide- and protein-based biosensors, of catalytically active peptides, or as chemical rulers for distance measurements in biopolymers based on the fluorescence resonance energy-transfer technology can be envisaged.

  DOI：

  10.1021/jo980643l
• 作为产物：
  描述：

  6-氯尿嘧啶 、 (S)-6-氨基-2-((叔丁氧基羰基)氨基)己酸叔丁酯 以 正丁醇 为溶剂， 反应 5.0h， 以49%的产率得到(S)-2-amino-N^α-(tert-butyloxycarbonyl)-6-(6'-aminopyrimidine-2',4'-dion-N-yl)hexanoic acid tert-butyl ester
  参考文献：
  名称：

  Efficient Syntheses of a Flavin and an 8-Hydroxy-5-deazaflavin Amino Acid and Their Incorporation into Oligopeptides

  摘要：

  We report a convenient synthesis for the cofactor amino acids (S)-3 and (S)-4 in which the C-5-ribose chain of the original riboflavin and ribo-5-deazaflavin cofactors is replaced by a C-5-amino acid side chain. Both cofactor amino acids are available in enantiomerically pure form in gram quantities and can be incorporated into oligopeptides using a standard Fmoc-based solid-phase peptide synthesis protocol. The benzyl-protecting group of the 8-hydroxy-5-deazaflavin can be cleaved by hydrogenolysis directly on the peptide. This allows the investigation of the properties of the peptide bound redox active OH- and the deprotonated O--form of the deazaflavin. Due to the electron- and energy-transfer properties of both cofactors, applications of both amino acid in the preparation of peptide- and protein-based biosensors, of catalytically active peptides, or as chemical rulers for distance measurements in biopolymers based on the fluorescence resonance energy-transfer technology can be envisaged.

  DOI：

  10.1021/jo980643l

文献信息

• Efficient Syntheses of a Flavin and an 8-Hydroxy-5-deazaflavin Amino Acid and Their Incorporation into Oligopeptides
  作者：Thomas Carell、Holger Schmid、Markus Reinhard

  DOI：10.1021/jo980643l

  日期：1998.11.1

  We report a convenient synthesis for the cofactor amino acids (S)-3 and (S)-4 in which the C-5-ribose chain of the original riboflavin and ribo-5-deazaflavin cofactors is replaced by a C-5-amino acid side chain. Both cofactor amino acids are available in enantiomerically pure form in gram quantities and can be incorporated into oligopeptides using a standard Fmoc-based solid-phase peptide synthesis protocol. The benzyl-protecting group of the 8-hydroxy-5-deazaflavin can be cleaved by hydrogenolysis directly on the peptide. This allows the investigation of the properties of the peptide bound redox active OH- and the deprotonated O--form of the deazaflavin. Due to the electron- and energy-transfer properties of both cofactors, applications of both amino acid in the preparation of peptide- and protein-based biosensors, of catalytically active peptides, or as chemical rulers for distance measurements in biopolymers based on the fluorescence resonance energy-transfer technology can be envisaged.