Boc-Pro-Pro-Pro-OBzl | 29776-72-5

• 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: Boc-Pro-Pro-Pro-OBzl
• CAS: 29776-72-5
• 化学式: C₂₇H₃₇N₃O₆
• 分子量: 499.607
• InChiKey: IZTJHHXWPMLDFU-FKBYEOEOSA-N

物化性质

• 沸点：
  669.6±55.0 °C(Predicted)
• 密度：
  1.250±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.11
• 重原子数：
  36.0
• 可旋转键数：
  5.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.63
• 拓扑面积：
  96.46
• 氢给体数：
  0.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  Boc-Pro-Pro-Pro-OBzl 在 palladium 10% on activated carbon 、 氢气 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 N,N-二异丙基乙胺 作用下， 以 甲醇 、 乙腈 为溶剂， 20.0 ℃ 、101.33 kPa 条件下， 生成
  参考文献：
  名称：

  Factors Affecting the Stabilization of Polyproline II Helices in a Hydrophobic Environment

  摘要：

  Several parameters have a critical importance for the stabilization of either polyproline I (PPI) or polyproline II (PPII) helices in a hydrophobic environment. Among them, it was found out that the concentration is crucial as polyprolines at 3 mM concentration stably fold in PPII helices, that are organized in aggregates stable even after several days and are detectable by dynamic light scattering analysis. In more diluted concentration the same molecules stably fold in PPI helices, and no aggregates are found. In contrast, the introduction of a (4S,5R)-4-carboxy-5-methyloxazolidin-2-one ((L)-Oxd) moiety always inhibits the formation of the PPI helix, regardless of the (L)-Oxd position and the solution concentration.

  DOI：

  10.1021/acs.orglett.6b00532
• 作为产物：
  描述：

  Boc-Pro-Pro-OBzl 在 palladium 10% on activated carbon 、 氢气 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 N,N-二异丙基乙胺 作用下， 以 甲醇 、 乙腈 为溶剂， 20.0 ℃ 、101.33 kPa 条件下， 生成 Boc-Pro-Pro-Pro-OBzl
  参考文献：
  名称：

  Factors Affecting the Stabilization of Polyproline II Helices in a Hydrophobic Environment

  摘要：

  Several parameters have a critical importance for the stabilization of either polyproline I (PPI) or polyproline II (PPII) helices in a hydrophobic environment. Among them, it was found out that the concentration is crucial as polyprolines at 3 mM concentration stably fold in PPII helices, that are organized in aggregates stable even after several days and are detectable by dynamic light scattering analysis. In more diluted concentration the same molecules stably fold in PPI helices, and no aggregates are found. In contrast, the introduction of a (4S,5R)-4-carboxy-5-methyloxazolidin-2-one ((L)-Oxd) moiety always inhibits the formation of the PPI helix, regardless of the (L)-Oxd position and the solution concentration.

  DOI：

  10.1021/acs.orglett.6b00532

文献信息

• Zand L.; Tsai, F.-H.; Overberger, C. G., Bulletin des Societes Chimiques Belges, 1991, vol. 100, # 1, p. 35 - 47
  作者：Zand L.、Tsai, F.-H.、Overberger, C. G.

  DOI：——

  日期：——
• Otagiri, Ken; Nosho, Yasuharu; Shinoda, Ichizo, Agricultural and Biological Chemistry, 1985, vol. 49, # 4, p. 1019 - 1026
  作者：Otagiri, Ken、Nosho, Yasuharu、Shinoda, Ichizo、Fukui, Hiroshi、Okai, Hideo

  DOI：——

  日期：——
• The ferrocene moiety as a structural probe: redox and structural properties of ferrocenoyl-oligoprolines FcPronOBzl (n=1–4) and FcPro2PheOBzl
  作者：Heinz-Bernhard Kraatz、Donald M Leek、Abdelaziz Houmam、Gary D Enright、Janusz Lusztyk、Danial D.M Wayner

  DOI：10.1016/s0022-328x(99)00300-9

  日期：1999.10

  The preparations of the five ferrocenoyl-oligopeptides, Fc-Pro-OBzl (1), Fc-Pro(2)-OBzl (2), Fc-Pro(3)-OBzl (3), Fc-Pro(4)-OBzl (4) and Fc-Pro(2)-Phe-OBzl (5) are described. Crystallographic studies show that the Fc-oligoprolines 1-4 adopt a helical polyproline II structure having all prolines in a mutually tl ans-conformation. This structure is maintained in MeCN and CHCl3 solutions, as was shown by NMR methods. Chemical and magnetic similarities among the proline residues render spectral assignment by conventional 1D H-1-NMR spectroscopy impossible. However, a combination of 2D NMR techniques allowed us to unequivocally assign all signals. The redox potential of the Fc-group attached to the oligoproline chain is sensitive to the sequence and length of the oligopeptide. With growing peptide length, the molecule becomes easier to oxidize. (C) 1999 Elsevier Science S.A. All rights reserved.