N^α-(tert-butoxycarbonyl)-L-3-(3-N-ethylcarbazolyl)alanine | 145178-45-6

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吲哚及其衍生物
• 英文名称: N^α-(tert-butoxycarbonyl)-L-3-(3-N-ethylcarbazolyl)alanine
• 英文别名: (2S)-3-(9-ethylcarbazol-3-yl)-2-[(2-methylpropan-2-yl)oxycarbonylamino]propanoic acid
• CAS: 145178-45-6
• 化学式: C₂₂H₂₆N₂O₄
• 分子量: 382.459
• InChiKey: MKMLRXFNHPGEPR-KRWDZBQOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.2
• 重原子数：
  28
• 可旋转键数：
  7
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.36
• 拓扑面积：
  80.6
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  N^α-(tert-butoxycarbonyl)-L-3-(3-N-ethylcarbazolyl)alanine 、 1-aza-13,14-dithiacyclopentacosane 在 N,N-二异丙基乙胺 、 N-[(dimethylamino)-3-oxo-1H-1,2,3-triazolo[4,5-b]pyridin-1-yl-methylene]-N-methylmethanaminium hexafluorophosphate 作用下， 以 氯仿 为溶剂， 反应 12.0h， 生成 [(S)-2-(1,2-Dithia-14-aza-cyclopentacos-14-yl)-1-(9-ethyl-9H-carbazol-3-ylmethyl)-2-oxo-ethyl]-carbamic acid tert-butyl ester
  参考文献：
  名称：

  Photocurrent Generation under a Large Dipole Moment Formed by Self-Assembled Monolayers of Helical Peptides Having an N-Ethylcarbazolyl Group

  摘要：

  Self-assembled monolayers (SAMs) of alpha-helical peptides carrying an N-ethylcarbazolyl (ECz) group were prepared. The helical peptide SAMs on a gold surface were characterized by quartz crystal microbalance measurements, cyclic voltammetry, and impedance spectroscopy, showing that a tridecapeptide SAM with the N-terminal binding to gold was packed more densely than that with the C-terminal binding. The helix tilt angles from the surface normal in these peptide SAMs were found to be about 40 degrees on the basis of Fourier transform infrared reflection-absorption spectroscopy. Photocurrent generation of these peptide SAMs in an aqueous solution was investigated by photoexcitation of ECz groups either in the presence of an electron donor or acceptor. In the presence of methyl viologen (electron acceptor), electron donation from a gold surface to an ECz group was observed upon photoexcitation. On the other hand, in the presence of triethanolamine or ethylenediaminetetraacetic acid (electron donor), the direction of photocurrent was reversed. In the case of the anodic photocurrent generation using triethanoamine, the electron donation from an ECz group to a gold surface was accelerated by the helix dipole moment directing toward a gold surface. Furthermore, the electronic coupling between an ECz group and a gold surface through the peptide molecule was found to occur more strongly than that through a saturated hydrocarbon. The helical peptides were therefore shown to be an excellent medium for electron transfer.

  DOI：

  10.1021/ja992769l
• 作为产物：
  描述：

  二碳酸二叔丁酯 、 L-3-(3-N-ethylcarbazolyl)alanine 在 碳酸氢钠 作用下， 以 1,4-二氧六环 为溶剂， 反应 6.0h， 以46.9%的产率得到N^α-(tert-butoxycarbonyl)-L-3-(3-N-ethylcarbazolyl)alanine
  参考文献：
  名称：

  Photocurrent Generation under a Large Dipole Moment Formed by Self-Assembled Monolayers of Helical Peptides Having an N-Ethylcarbazolyl Group

  摘要：

  Self-assembled monolayers (SAMs) of alpha-helical peptides carrying an N-ethylcarbazolyl (ECz) group were prepared. The helical peptide SAMs on a gold surface were characterized by quartz crystal microbalance measurements, cyclic voltammetry, and impedance spectroscopy, showing that a tridecapeptide SAM with the N-terminal binding to gold was packed more densely than that with the C-terminal binding. The helix tilt angles from the surface normal in these peptide SAMs were found to be about 40 degrees on the basis of Fourier transform infrared reflection-absorption spectroscopy. Photocurrent generation of these peptide SAMs in an aqueous solution was investigated by photoexcitation of ECz groups either in the presence of an electron donor or acceptor. In the presence of methyl viologen (electron acceptor), electron donation from a gold surface to an ECz group was observed upon photoexcitation. On the other hand, in the presence of triethanolamine or ethylenediaminetetraacetic acid (electron donor), the direction of photocurrent was reversed. In the case of the anodic photocurrent generation using triethanoamine, the electron donation from an ECz group to a gold surface was accelerated by the helix dipole moment directing toward a gold surface. Furthermore, the electronic coupling between an ECz group and a gold surface through the peptide molecule was found to occur more strongly than that through a saturated hydrocarbon. The helical peptides were therefore shown to be an excellent medium for electron transfer.

  DOI：

  10.1021/ja992769l

文献信息

• Photocurrent Generation under a Large Dipole Moment Formed by Self-Assembled Monolayers of Helical Peptides Having an <i>N</i>-Ethylcarbazolyl Group
  作者：Tomoyuki Morita、Shunsaku Kimura、Shiro Kobayashi、Yukio Imanishi

  DOI：10.1021/ja992769l

  日期：2000.3.1

  Self-assembled monolayers (SAMs) of alpha-helical peptides carrying an N-ethylcarbazolyl (ECz) group were prepared. The helical peptide SAMs on a gold surface were characterized by quartz crystal microbalance measurements, cyclic voltammetry, and impedance spectroscopy, showing that a tridecapeptide SAM with the N-terminal binding to gold was packed more densely than that with the C-terminal binding. The helix tilt angles from the surface normal in these peptide SAMs were found to be about 40 degrees on the basis of Fourier transform infrared reflection-absorption spectroscopy. Photocurrent generation of these peptide SAMs in an aqueous solution was investigated by photoexcitation of ECz groups either in the presence of an electron donor or acceptor. In the presence of methyl viologen (electron acceptor), electron donation from a gold surface to an ECz group was observed upon photoexcitation. On the other hand, in the presence of triethanolamine or ethylenediaminetetraacetic acid (electron donor), the direction of photocurrent was reversed. In the case of the anodic photocurrent generation using triethanoamine, the electron donation from an ECz group to a gold surface was accelerated by the helix dipole moment directing toward a gold surface. Furthermore, the electronic coupling between an ECz group and a gold surface through the peptide molecule was found to occur more strongly than that through a saturated hydrocarbon. The helical peptides were therefore shown to be an excellent medium for electron transfer.