(E)-17-[N-(9-fluorenylmethoxycarbonyl)-O-tert-butyl-L-threonyloxy]-4,7,10,13-tetraoxa-15-heptadecenoic acid phenacyl ester | 186021-16-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: (E)-17-[N-(9-fluorenylmethoxycarbonyl)-O-tert-butyl-L-threonyloxy]-4,7,10,13-tetraoxa-15-heptadecenoic acid phenacyl ester
• 英文别名: [(E)-4-[2-[2-[2-(3-oxo-3-phenacyloxypropoxy)ethoxy]ethoxy]ethoxy]but-2-enyl] (2S,3R)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-[(2-methylpropan-2-yl)oxy]butanoate
• CAS: 186021-16-9
• 化学式: C₄₄H₅₅NO₁₂
• 分子量: 789.92
• InChiKey: YCEJEMGZANLJOS-WYQOFZERSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.2
• 重原子数：
  57
• 可旋转键数：
  29
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.45
• 拓扑面积：
  154
• 氢给体数：
  1
• 氢受体数：
  12

反应信息

• 作为反应物：
  描述：

  (E)-17-[N-(9-fluorenylmethoxycarbonyl)-O-tert-butyl-L-threonyloxy]-4,7,10,13-tetraoxa-15-heptadecenoic acid phenacyl ester 在 溶剂黄146 、 锌 作用下， 反应 2.0h， 以97%的产率得到(E)-17-[N-(9-fluorenylmethoxycarbonyl)-O-tert-butyl-L-threonyloxy]-4,7,10,13-tetraoxa-15-heptadecenoic acid
  参考文献：
  名称：

  HYCRON, an Allylic Anchor for High-Efficiency Solid Phase Synthesis of Protected Peptides and Glycopeptides

  摘要：

  The recently developed allylic HYCRON anchor(1) exhibits excellent properties for the solid phase synthesis of protected peptides and glycopeptides. Model reactions with analogous low molecular weight compounds assessed the acid- and base-stability of the polar and flexible HYCRON linkage. The new anchor is available in a two-step synthesis and allows the use of both the Boc- and the Fmoc-strategy, which can even be combined within one synthesis. Protected glycopeptides are released under almost neutral conditions, taking advantage of the Pd(O)-catalyzed allyl transfer to a weakly basic nucleophile such as N-methylaniline. The highly efficient synthesis of O-alpha GalNAc-(T-N)-peptides of the MUC-1 repeating unit is described. Acid- and base-stability of the allyl ester linkage enabled the synthesis of an O-glucosylated peptide by first removing a threonine tert-butyl group on the solid phase and subsequently glycosylating the liberated resin-bound hydroxyl component.

  DOI：

  10.1021/jo960743w
• 作为产物：
  描述：

  3-(2-{2-[2-(4-bromo-but-2-enyloxy)-ethoxy]-ethoxy}-ethoxy)-propionic acid 在 potassium fluoride 、 四丁基溴化铵 、 碳酸氢钠 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 0.75h， 生成 (E)-17-[N-(9-fluorenylmethoxycarbonyl)-O-tert-butyl-L-threonyloxy]-4,7,10,13-tetraoxa-15-heptadecenoic acid phenacyl ester
  参考文献：
  名称：

  HYCRON, an Allylic Anchor for High-Efficiency Solid Phase Synthesis of Protected Peptides and Glycopeptides

  摘要：

  The recently developed allylic HYCRON anchor(1) exhibits excellent properties for the solid phase synthesis of protected peptides and glycopeptides. Model reactions with analogous low molecular weight compounds assessed the acid- and base-stability of the polar and flexible HYCRON linkage. The new anchor is available in a two-step synthesis and allows the use of both the Boc- and the Fmoc-strategy, which can even be combined within one synthesis. Protected glycopeptides are released under almost neutral conditions, taking advantage of the Pd(O)-catalyzed allyl transfer to a weakly basic nucleophile such as N-methylaniline. The highly efficient synthesis of O-alpha GalNAc-(T-N)-peptides of the MUC-1 repeating unit is described. Acid- and base-stability of the allyl ester linkage enabled the synthesis of an O-glucosylated peptide by first removing a threonine tert-butyl group on the solid phase and subsequently glycosylating the liberated resin-bound hydroxyl component.

  DOI：

  10.1021/jo960743w

文献信息

• HYCRON, an Allylic Anchor for High-Efficiency Solid Phase Synthesis of Protected Peptides and Glycopeptides
  作者：Oliver Seitz、Horst Kunz

  DOI：10.1021/jo960743w

  日期：1997.2.1

  The recently developed allylic HYCRON anchor(1) exhibits excellent properties for the solid phase synthesis of protected peptides and glycopeptides. Model reactions with analogous low molecular weight compounds assessed the acid- and base-stability of the polar and flexible HYCRON linkage. The new anchor is available in a two-step synthesis and allows the use of both the Boc- and the Fmoc-strategy, which can even be combined within one synthesis. Protected glycopeptides are released under almost neutral conditions, taking advantage of the Pd(O)-catalyzed allyl transfer to a weakly basic nucleophile such as N-methylaniline. The highly efficient synthesis of O-alpha GalNAc-(T-N)-peptides of the MUC-1 repeating unit is described. Acid- and base-stability of the allyl ester linkage enabled the synthesis of an O-glucosylated peptide by first removing a threonine tert-butyl group on the solid phase and subsequently glycosylating the liberated resin-bound hydroxyl component.