Glu(OtBu)-Ala-OMe | 42538-76-1

• 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: Glu(OtBu)-Ala-OMe
• 英文别名: γ-tert-butyl-L-glutamyl-L-alanine methyl ester
• CAS: 42538-76-1
• 化学式: C₁₃H₂₄N₂O₅
• 分子量: 288.344
• InChiKey: GXJJFZOUNTUQKB-IUCAKERBSA-N

物化性质

• 沸点：
  430.8±45.0 °C(Predicted)
• 密度：
  1.106±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.11
• 重原子数：
  20.0
• 可旋转键数：
  6.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.77
• 拓扑面积：
  107.72
• 氢给体数：
  2.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  Glu(OtBu)-Ala-OMe 在 钯 氢气 、 一水合肼 、 溶剂黄146 、 三乙胺 作用下， 以 甲醇 、 乙酸乙酯 、 N,N-二甲基甲酰胺 为溶剂， 反应 65.0h， 生成 N-tert-butoxycarbonyl-O-benzyl-L-seryl-L-histidyl-L-leucyl-L-valyl-γ-tert-butyl-L-glutamyl-L-alanine hydrazide
  参考文献：
  名称：

  Kolomeitseva, L. A.; Kocharova, N. A.; Ibragimova, L. D., Journal of general chemistry of the USSR, 1982, vol. 52, # 2, p. 372 - 377

  摘要：

  DOI：
• 作为产物：
  描述：

  Z-Glu(O-t-Bu)-Ala-OMe 在 palladium on activated charcoal 盐酸 、 氢气 作用下， 以 甲醇 为溶剂， 生成 Glu(OtBu)-Ala-OMe
  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

文献信息

• Macrocyclization of Peptide Side Chains by the Ugi Reaction: Achieving Peptide Folding and Exocyclic <i>N</i>-Functionalization in One Shot
  作者：Aldrin V. Vasco、Carlos S. Pérez、Fidel E. Morales、Hilda E. Garay、Dimitar Vasilev、José A. Gavín、Ludger A. Wessjohann、Daniel G. Rivera

  DOI：10.1021/acs.joc.5b00858

  日期：2015.7.2

  The cyclization of peptide side chains has been traditionally used to either induce or stabilize secondary structures (beta-strands, helices, reverse turns) in short peptide sequences. So far, classic peptide coupling, nucleophilic substitution, olefin metathesis, and click reactions have been the methods of choice to fold synthetic peptides by means of macrocyclization. This article describes the utilization of the Ugi reaction for the side chain-to-side chain and side chain-to-termini macrocydization of peptides, thus enabling not only access to stable folded structures but also the incorporation of exocydic functionalities as N-substituents. Analysis of the NMR-derived structures revealed the formation of helical turns, beta-bulges, and a-turns in cyclic peptides cross-linked at i, i + 3 and i, i + 4 positions, proving the folding effect of the multicomponent Ugi macrocyclization. Molecular dynamics simulation provided further insights on the stability and molecular motion of the side chain cross-linked peptides.