N-(tert-butoxycarbonyl)-3-(3-[4-(dimethylamino)phenyl]prop-2-enoyl)-L-tyrosine | 1508268-93-6

• 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: N-(tert-butoxycarbonyl)-3-(3-[4-(dimethylamino)phenyl]prop-2-enoyl)-L-tyrosine
• CAS: 1508268-93-6
• 化学式: C₂₅H₃₀N₂O₆
• 分子量: 454.523
• InChiKey: TUQDKSKVIKMSEA-FQEVSTJZSA-N

物化性质

• 沸点：
  690.2±55.0 °C(predicted)
• 密度：
  1.243±0.06 g/cm3(Temp: 20 °C; Press: 760 Torr)(predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.87
• 重原子数：
  33.0
• 可旋转键数：
  8.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.32
• 拓扑面积：
  116.17
• 氢给体数：
  3.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  N-(tert-butoxycarbonyl)-3-(3-[4-(dimethylamino)phenyl]prop-2-enoyl)-L-tyrosine 在 双氧水 、 sodium hydroxide 作用下， 以 乙醇 为溶剂， 反应 6.0h， 以33%的产率得到N-(tert-butoxycarbonyl)-3-(2-[4-(dimethylamino)phenyl]-3-hydroxy-4-oxo-4H-chromen-6-yl)-L-alanine
  参考文献：
  名称：

  Dual-Fluorescence l-Amino Acid Reports Insertion and Orientation of Melittin Peptide in Cell Membranes

  摘要：

  Monitoring insertion and orientation of peptides in situ on cell membranes remains a challenge. To this end, we synthesized an L-amino acid (AFaa) containing a dual-fluorescence dye of the 3-hydroxyflavone family, as a side chain. In contrast to other labeling approaches using a flexible linker, the AFaa fluorophore, introduced by solid phase synthesis into desired position of a peptide, is attached closely to its backbone with well-defined orientation, and, therefore, could reflect its localization in the membrane. This concept was validated by replacing the leucine-9 (L9) and tryptophan-19 (W19) residues by AFaa in melittin, a well-studied membrane-active peptide. Due to high sensitivity of AFaa dual emission to the environment polarity, we detected a much deeper insertion of L9 peptide position into the bilayer, compared to the W19 position. Moreover, using fluorescence microscopy with a polarized light excitation, we found different orientation of AFaa at L9 and W19 positions of melittin in the bilayers of giant vesicles and cellular membranes. These results suggested that in the natural membranes, similarly to the model lipid bilayers, melittin is preferentially oriented parallel to the membrane surface. The developed amino acid and the proposed methodology will be of interest to study other membrane peptides.

  DOI：

  10.1021/bc400325n
• 作为产物：
  描述：

  L-酪氨酸 在 aluminum (III) chloride 、 sodium hydroxide 作用下， 以 乙醇 、 水 、 硝基苯 为溶剂， 生成 N-(tert-butoxycarbonyl)-3-(3-[4-(dimethylamino)phenyl]prop-2-enoyl)-L-tyrosine
  参考文献：
  名称：

  Dual-Fluorescence l-Amino Acid Reports Insertion and Orientation of Melittin Peptide in Cell Membranes

  摘要：

  Monitoring insertion and orientation of peptides in situ on cell membranes remains a challenge. To this end, we synthesized an L-amino acid (AFaa) containing a dual-fluorescence dye of the 3-hydroxyflavone family, as a side chain. In contrast to other labeling approaches using a flexible linker, the AFaa fluorophore, introduced by solid phase synthesis into desired position of a peptide, is attached closely to its backbone with well-defined orientation, and, therefore, could reflect its localization in the membrane. This concept was validated by replacing the leucine-9 (L9) and tryptophan-19 (W19) residues by AFaa in melittin, a well-studied membrane-active peptide. Due to high sensitivity of AFaa dual emission to the environment polarity, we detected a much deeper insertion of L9 peptide position into the bilayer, compared to the W19 position. Moreover, using fluorescence microscopy with a polarized light excitation, we found different orientation of AFaa at L9 and W19 positions of melittin in the bilayers of giant vesicles and cellular membranes. These results suggested that in the natural membranes, similarly to the model lipid bilayers, melittin is preferentially oriented parallel to the membrane surface. The developed amino acid and the proposed methodology will be of interest to study other membrane peptides.

  DOI：

  10.1021/bc400325n