cis-1-(1,1-dimethylethyoxycarbonyl)-4-(6-(2,5-dihydro-2,5-dioxo-1H-pyrrolo-1)-hexanamido)-L-proline | 171110-73-9

• 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: cis-1-(1,1-dimethylethyoxycarbonyl)-4-(6-(2,5-dihydro-2,5-dioxo-1H-pyrrolo-1)-hexanamido)-L-proline
• 英文别名: (2S,4S)-4-[6-(2,5-dioxopyrrol-1-yl)hexanoylamino]-1-[(2-methylpropan-2-yl)oxycarbonyl]pyrrolidine-2-carboxylic acid
• CAS: 171110-73-9
• 化学式: C₂₀H₂₉N₃O₇
• 分子量: 423.466
• InChiKey: OHWNEZGWNYXENC-KBPBESRZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.05
• 重原子数：
  30.0
• 可旋转键数：
  8.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.65
• 拓扑面积：
  133.32
• 氢给体数：
  2.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  BOC-L-脯氨酸 、 乙酸酐 、 BOC-脯氨酸基-脯氨酸 、 cis-1-(1,1-dimethylethyoxycarbonyl)-4-(6-(2,5-dihydro-2,5-dioxo-1H-pyrrolo-1)-hexanamido)-L-proline 在 N-甲基吗啉 、 氢氟酸 、 (benzotriazo-1-yloxy)tris(dimethylamino)phosphonium hexafluorophosphate 、 1-羟基苯并三唑 、 N,N'-二环己基碳二亚胺 、 三氟乙酸 作用下， 生成
  参考文献：
  名称：

  Engineering of a 129-residue tripod protein by chemoselective ligation of proline-II helices

  摘要：

  A 129-residue tripod protein was designed, synthesized, and biophysically characterized. This receptor-adhesive modular protein contained three 30-residue proline-II helices linked to a 9-residue proline-II helix through thioether bonds. Coupling of 6-maleimidohexanoic acid succinimido ester to cis-N-alpha-Boc-4-amino-L-proline furnished in 77% yield the maleimido ac id cis-N-Boc-4-(6-maleimidohexanamido)-L-proline (Boc-Prm), which was used in the solid-phase synthesis of the linker peptide CH3-CO-Pro(3)-Prm(3)-Pro(3)-NH2. The leg peptide, the 40-residue thiol Gly-Arg-Gly-Asp-Ser-Pro-Gly-Tyr-Gly-Pro(30)-Cys-NH2, was also made by solid-phase synthesis. The tripod protein was prepared by Michael addition of the thiol groups of three leg peptides to the three maleimide groups of the linker peptide. By C-13 NMR spectrometry, the linker peptide was a proline-II helix, as indicated by the presence of only trans Pro-Pro resonances for its beta and gamma carbons. By circular dichroic spectroscopy, the model peptide CH3-CO-Pro(9)-NH2, the linker peptide, the leg peptide, and the tripod protein each contained substantial proline-II helix, as indicated by a strong negative band at 205 nm and a weak positive band at 226 nm. Since the Pro(30) proline-II helix of each leg is about 93 Angstrom long, two Arg-Gly-Asp sites on different legs of the tripod protein could be as much as similar to 250 Angstrom apart.

  DOI：

  10.1016/0040-4020(95)00592-v
• 作为产物：
  描述：

  6-(马来酰亚胺基)己酸琥珀酰亚胺酯 、 (2S,4S)-4 -氨基- 1 -(叔丁氧羰基)吡咯烷二羧酸 在 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 以77%的产率得到cis-1-(1,1-dimethylethyoxycarbonyl)-4-(6-(2,5-dihydro-2,5-dioxo-1H-pyrrolo-1)-hexanamido)-L-proline
  参考文献：
  名称：

  Engineering of a 129-residue tripod protein by chemoselective ligation of proline-II helices

  摘要：

  A 129-residue tripod protein was designed, synthesized, and biophysically characterized. This receptor-adhesive modular protein contained three 30-residue proline-II helices linked to a 9-residue proline-II helix through thioether bonds. Coupling of 6-maleimidohexanoic acid succinimido ester to cis-N-alpha-Boc-4-amino-L-proline furnished in 77% yield the maleimido ac id cis-N-Boc-4-(6-maleimidohexanamido)-L-proline (Boc-Prm), which was used in the solid-phase synthesis of the linker peptide CH3-CO-Pro(3)-Prm(3)-Pro(3)-NH2. The leg peptide, the 40-residue thiol Gly-Arg-Gly-Asp-Ser-Pro-Gly-Tyr-Gly-Pro(30)-Cys-NH2, was also made by solid-phase synthesis. The tripod protein was prepared by Michael addition of the thiol groups of three leg peptides to the three maleimide groups of the linker peptide. By C-13 NMR spectrometry, the linker peptide was a proline-II helix, as indicated by the presence of only trans Pro-Pro resonances for its beta and gamma carbons. By circular dichroic spectroscopy, the model peptide CH3-CO-Pro(9)-NH2, the linker peptide, the leg peptide, and the tripod protein each contained substantial proline-II helix, as indicated by a strong negative band at 205 nm and a weak positive band at 226 nm. Since the Pro(30) proline-II helix of each leg is about 93 Angstrom long, two Arg-Gly-Asp sites on different legs of the tripod protein could be as much as similar to 250 Angstrom apart.

  DOI：

  10.1016/0040-4020(95)00592-v