Z(OMe)-Lys(Z)-Pro-OH | 51165-28-7

• 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: Z(OMe)-Lys(Z)-Pro-OH
• CAS: 51165-28-7
• 化学式: C₂₈H₃₅N₃O₈
• 分子量: 541.601
• InChiKey: SICCARCXABUGDN-ZEQRLZLVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.46
• 重原子数：
  39.0
• 可旋转键数：
  13.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  143.5
• 氢给体数：
  3.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  H-Asp(OBzl)-Gln-Phe-Val-Gly-Leu-Met-NH2 、 Z(OMe)-Lys(Z)-Pro-OH 在 1-羟基苯并三唑 、 三乙胺 、 N,N'-二环己基碳二亚胺 作用下， 以 二甲基亚砜 、 N,N-二甲基甲酰胺 为溶剂， 生成 Z(OMe)-Lys(Z)-Pro-Asp(OBzl)-Gln-Phe-Val-Gly-Leu-Met-NH2
  参考文献：
  名称：

  Studies on peptides. CXIV. Synthesis of hylambates-kassinin, a frog skin tachykinin peptide.

  摘要：

  Hylambates-kassinin是一种新的两栖动物皮肤十二肽，属于速激肽家族。它采用传统方法合成，使用了以硫醚为介质的去保护反应，辅以三氟甲烷磺酸。合成的Hylambates-kassinin在孤立的豚鼠十二指肠中的收缩效力是合成的kassinin的1.4倍。

  DOI：

  10.1248/cpb.31.4259

文献信息

• Synthesis of the Pentadecapeptide corresponding to the Entire Amino Acid Sequence of Salmon α-Melanotropin II (α-MSH II)
  作者：KENJI OKAMOTO、KOICHI YASUMURA、NOBUHIRO YAMAMURA、SHINICHI SHIMAMURA、KENJI MIYATA、AKIRA TANAKA、MASUHISA NAKAMURA、HIROSHI KAWAUCHI、HARUAKI YAJIMA

  DOI：10.1248/cpb.30.2595

  日期：——

  The pentadecapeptide corresponding to the entire amino acid sequence of α-MSH II, isolated from salmon pituitary gland, was synthesized by a conventional procedure. The synthetic peptide exhibited in vitro melanocyte-stimulating activity of 1.66×1010 MSH U/g.

  采用传统方法合成了与α-MSH II 全部氨基酸序列相对应的十胜五肽，该肽是从鲑鱼垂体中分离出来的。合成肽的体外黑色素细胞刺激活性为 1.66×1010 MSH U/g。
• Tuftsin analogs: synthesis, structure-function relationships, and implications for specificity of tuftsin's bioactivity
  作者：Shlomo Dagan、Philip Gottlieb、Esther Tzehoval、Michael Feldman、Mati Fridkin、Koichi Yasumura、Kenji Okamoto、Haruaki Yajima

  DOI：10.1021/jm00160a027

  日期：1986.10

  Thirteen analogues of the natural macrophage activator peptide tuftsin, ten of which are novel, were synthesized with the aim of exploring the relation between their biological potency and their capacity to attach specifically to cellular tuftsin's receptors. The analogues representing modifications and chain extensions at various parts of the parent tuftsin molecule can be classified as N-terminal analogues, C-terminal analogues, "within-chain" derivatives, or dimers of tuftsin and retrotuftsin. The various synthetic routes employed to prepare the analogues are described. A direct correlation was found between the ability of analogues to inhibit [3H-Arg4]tuftsin specific binding to mice peritoneal macrophages and their capacity to enhance phagocytosis or to inhibit tuftsin-mediated phagocytosis by the cells and to potentiate the cell's immune response.