(S)-2-[(R)-2-(Trityl-amino)-3-tritylsulfanyl-propionylamino]-succinamic acid tert-butyl ester | 31945-78-5

• 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: (S)-2-[(R)-2-(Trityl-amino)-3-tritylsulfanyl-propionylamino]-succinamic acid tert-butyl ester
• CAS: 31945-78-5
• 化学式: C₄₉H₄₉N₃O₄S
• 分子量: 776.012
• InChiKey: HBPGPZMIVUTDKP-MJPWBCPGSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  8.36
• 重原子数：
  57.0
• 可旋转键数：
  16.0
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.2
• 拓扑面积：
  110.52
• 氢给体数：
  3.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  (S)-2-[(R)-2-(Trityl-amino)-3-tritylsulfanyl-propionylamino]-succinamic acid tert-butyl ester 在 溶剂黄146 作用下， 生成 H-Cys(Trt)-Asn-OtBu
  参考文献：
  名称：

  Die Synthese von Insulinfragmenten mit intakter interchenarer Disulfidbrücke A²⁰-B¹⁹

  摘要：

  AbstractThe synthesis of six insulin fragments is described, in which various sequences of the two chains are linked by the disulfide bridge between A20 and B19. The fragments in question are: A20–21–B19–21, A20–21–B18–21, A20–21–B17–21, A19–21–B19–21, A16–21–B18–21 and A20–21–B12–21.In order to build up the simpler fragments the disulfide bridge was established by oxidation with iodine of two S‐trityl cysteine peptides in which the carboxyl and amino groups were protected by the t‐butyl and t‐butyloxycarbonyl residue. From the mixture obtained the unsymmetrical cystine peptide was separated in all cases from the two symmetrical ones by counter‐current distribution.In the synthesis of the more complex fragments advantageous use was made of smaller unsymmetrical fragments prepared as above but having one amino group protected by the N‐trityl residue. After selective elimination of this group it was possible to lengthen the peptide chain at this position.The free peptides were obtained by removal of the protecting groups with strong acids, in particular concentrated hydrochloric acid. While in this deprotecting step the disulfide bond was stable, conditions are discussed under which disproportionation was observed.None of the six synthetic insulin fragments showed activity in stimulating rat adipose tissue to convert 14C‐labelled glucose to CO2 in vitro.

  DOI：

  10.1002/hlca.19710540143
• 作为产物：
  描述：

  Z-L-天冬酰胺叔丁酯 在 palladium on activated charcoal 氢气 、 N,N'-二环己基碳二亚胺 作用下， 以 乙酸乙酯 为溶剂， 生成 (S)-2-[(R)-2-(Trityl-amino)-3-tritylsulfanyl-propionylamino]-succinamic acid tert-butyl ester
  参考文献：
  名称：

  Die Synthese von Insulinfragmenten mit intakter interchenarer Disulfidbrücke A²⁰-B¹⁹

  摘要：

  AbstractThe synthesis of six insulin fragments is described, in which various sequences of the two chains are linked by the disulfide bridge between A20 and B19. The fragments in question are: A20–21–B19–21, A20–21–B18–21, A20–21–B17–21, A19–21–B19–21, A16–21–B18–21 and A20–21–B12–21.In order to build up the simpler fragments the disulfide bridge was established by oxidation with iodine of two S‐trityl cysteine peptides in which the carboxyl and amino groups were protected by the t‐butyl and t‐butyloxycarbonyl residue. From the mixture obtained the unsymmetrical cystine peptide was separated in all cases from the two symmetrical ones by counter‐current distribution.In the synthesis of the more complex fragments advantageous use was made of smaller unsymmetrical fragments prepared as above but having one amino group protected by the N‐trityl residue. After selective elimination of this group it was possible to lengthen the peptide chain at this position.The free peptides were obtained by removal of the protecting groups with strong acids, in particular concentrated hydrochloric acid. While in this deprotecting step the disulfide bond was stable, conditions are discussed under which disproportionation was observed.None of the six synthetic insulin fragments showed activity in stimulating rat adipose tissue to convert 14C‐labelled glucose to CO2 in vitro.

  DOI：

  10.1002/hlca.19710540143