(S)-2-((S)-2-tert-Butoxycarbonylamino-propionylamino)-propionic acid dodecyl ester | 171671-73-1

• 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-((S)-2-tert-Butoxycarbonylamino-propionylamino)-propionic acid dodecyl ester
• CAS: 171671-73-1
• 化学式: C₂₃H₄₄N₂O₅
• 分子量: 428.613
• InChiKey: UMSXOAFRCCRIDL-OALUTQOASA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.87
• 重原子数：
  30.0
• 可旋转键数：
  15.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.87
• 拓扑面积：
  93.73
• 氢给体数：
  2.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  (S)-2-((S)-2-tert-Butoxycarbonylamino-propionylamino)-propionic acid dodecyl ester 在 氰基磷酸二乙酯 、 氢溴酸 、 溶剂黄146 、 三乙胺 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 反应 7.0h， 生成 (S)-2-{(S)-2-[(S)-2-(11-Bromo-undecanoylamino)-propionylamino]-propionylamino}-propionic acid dodecyl ester
  参考文献：
  名称：

  Regulation of β-Sheet Structures within Amyloid-Like β-Sheet Assemblage from Tripeptide Derivatives

  摘要：

  N-(11-Trimethylammonioundecanoyl)-O,O'-didodecyl tripeptide bromides and N-(11-trimethylammonioundecanyl)-O-dodecyl tripeptide bromides formed a parallel P-sheet structure when they aggregated in water and in CCl4. The parallel beta-sheet was distinguished from the antiparallel counterpart by Fourier transform infrared spectroscopy because the former lacks a weak band at about 1690 cm(-1) that is characteristic for the latter. The FT-IR spectra of the aggregate in CCl4 remained unchanged if the solution was diluted to 0.01 mM, condensed to dryness, or heated to 60 degrees C, and hence, the beta-sheet was easily formed and thermodynamically stable. The parallel beta-sheet was also possible to transform into an antiparallel beta-sheet, for example, by mixing with another tripeptide-containing amphiphile whose tripeptide part had an opposite direction. Transmission electron microscope (TEM) and atomic force microscope (AFM) pictures revealed that the aggregate in CCl4 is a bundle of small filaments whose diameters are 70-80 Angstrom. Developed interpeptide hydrogen bonding should be formed along the long axis of the filament. The, morphological structures and stable peptide arrangements of the present assemblages are similar to those of the amyloid fiber whose accumulation causes fatal diseases.

  DOI：

  10.1021/ja981363q
• 作为产物：
  描述：

  N-叔丁氧羰基-L-丙氨酸 、 L-alanine hydrochloride dodecyl ester 在 氰基磷酸二乙酯 、 三乙胺 作用下， 以 四氢呋喃 为溶剂， 生成 (S)-2-((S)-2-tert-Butoxycarbonylamino-propionylamino)-propionic acid dodecyl ester
  参考文献：
  名称：

  Regulation of β-Sheet Structures within Amyloid-Like β-Sheet Assemblage from Tripeptide Derivatives

  摘要：

  N-(11-Trimethylammonioundecanoyl)-O,O'-didodecyl tripeptide bromides and N-(11-trimethylammonioundecanyl)-O-dodecyl tripeptide bromides formed a parallel P-sheet structure when they aggregated in water and in CCl4. The parallel beta-sheet was distinguished from the antiparallel counterpart by Fourier transform infrared spectroscopy because the former lacks a weak band at about 1690 cm(-1) that is characteristic for the latter. The FT-IR spectra of the aggregate in CCl4 remained unchanged if the solution was diluted to 0.01 mM, condensed to dryness, or heated to 60 degrees C, and hence, the beta-sheet was easily formed and thermodynamically stable. The parallel beta-sheet was also possible to transform into an antiparallel beta-sheet, for example, by mixing with another tripeptide-containing amphiphile whose tripeptide part had an opposite direction. Transmission electron microscope (TEM) and atomic force microscope (AFM) pictures revealed that the aggregate in CCl4 is a bundle of small filaments whose diameters are 70-80 Angstrom. Developed interpeptide hydrogen bonding should be formed along the long axis of the filament. The, morphological structures and stable peptide arrangements of the present assemblages are similar to those of the amyloid fiber whose accumulation causes fatal diseases.

  DOI：

  10.1021/ja981363q