H-Gly-Cys(Acm)-Phe-Val-Pro-Cys(Fm)-Gly-OH | 118972-75-1

• 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: H-Gly-Cys(Acm)-Phe-Val-Pro-Cys(Fm)-Gly-OH
• CAS: 118972-75-1
• 化学式: C₄₆H₅₈N₈O₉S₂
• 分子量: 931.147
• InChiKey: YSIAXPNSLSIYAR-RHLPRWGDSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.35
• 重原子数：
  65.0
• 可旋转键数：
  23.0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  258.23
• 氢给体数：
  8.0
• 氢受体数：
  11.0

反应信息

• 作为反应物：
  描述：

  H-Gly-Cys(Acm)-Phe-Val-Pro-Cys(Fm)-Gly-OH 在 哌啶 、 2-巯基乙醇 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 2.0h， 以84%的产率得到H-Gly-Cys(Acm)-Phe-Val-Pro-Cys-Gly-OH
  参考文献：
  名称：

  Unequivocal synthesis and characterization of a parallel and an antiparallel bis-cystine peptide

  摘要：

  Using an unambiguous methodology we have synthesized the two topological isomers (parallel and antiparallel) of a cyclic peptide dimer containing two disulfide bridges, and we have characterized them spectroscopically using circular dichroism and NMR. We have shown that the interactions between the two chains play a dominant role in determining the different conformational properties of both dimers. Although both molecules are flexible, the ensemble of conformations available to them is clearly different: the antiparallel dimer gives extended structures while the parallel dimer gives mainly folded conformations. Interchain NOEs between symmetry-related residues could be differentiated from the trivial intraresidue NOE using a selective TOCSY-NOESY experiment, and this assignment was in agreement with the predictions made from a conformational search using molecular dynamics without experimental constraints.

  DOI：

  10.1021/jo00075a027

文献信息

• Uteroglobin-like peptide cavities I. Synthesis of antiparallel and parallel dimers of bis-cysteine peptides
  作者：M. Ruiz-Gayo、F. Albericio、M. Pons、M. Royo、E. Pedroso、E. Giralt

  DOI：10.1016/s0040-4039(00)82130-9

  日期：1988.1