Boc-Tyr-c[D-Cys-Gly-Phe-NH-NH<-Phe<-Gly<-D-Cys]<-Tyr-Boc | 873684-55-0

• 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: Boc-Tyr-c[D-Cys-Gly-Phe-NH-NH<-Phe<-Gly<-D-Cys]<-Tyr-Boc
• CAS: 873684-55-0
• 化学式: C₅₆H₇₀N₁₀O₁₄S₂
• 分子量: 1171.36
• InChiKey: PGPYVOBQJYYZSY-WGXSSYHUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.87
• 重原子数：
  82.0
• 可旋转键数：
  14.0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.39
• 拓扑面积：
  349.92
• 氢给体数：
  12.0
• 氢受体数：
  16.0

反应信息

• 作为反应物：
  描述：

  Boc-Tyr-c[D-Cys-Gly-Phe-NH-NH<-Phe<-Gly<-D-Cys]<-Tyr-Boc 、 三氟乙酸 以 二氯甲烷 为溶剂， 反应 0.5h， 生成 Tyr-c[Cys-Gly-Phe-NH-NH<-Phe<-Gly<-Cys]<-Tyr bis(trifluoroacetic acid salt)
  参考文献：
  名称：

  Synthesis and biological activity of the first cyclic biphalin analogues

  摘要：

  Biphalin is a linear octapeptide with strong opioid activity. Its structure is based on two identical sequences derived from enkephalins joined C-terminal to C-terminal by an hydrazide bridge (Tyr-D-Ala-Gly-Phe-NH-NH <- Phe <- Gly <- D-Ala <- Tyr). In this study we present the design, synthesis, and biological evaluation of the first cyclic biphalin analogues. D-Alanine residues in positions 2, 2' of the parent peptide were replaced by D- and L-cysteine and an intramolecular disulfide bond between the cysteine thiol groups was introduced. We obtained two cyclic analogues with quite different biological profiles. (c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2005.09.080
• 作为产物：
  描述：

  Boc-Tyr-D-Cys(Acm)-Gly-Phe-NH-NH<-Phe<-Gly<-D-Cys(Acm)<-Tyr-Boc 在 碘 、 溶剂黄146 作用下， 以 二甲基亚砜 为溶剂， 反应 3.0h， 以40%的产率得到Boc-Tyr-c[D-Cys-Gly-Phe-NH-NH<-Phe<-Gly<-D-Cys]<-Tyr-Boc
  参考文献：
  名称：

  Synthesis and biological activity of the first cyclic biphalin analogues

  摘要：

  Biphalin is a linear octapeptide with strong opioid activity. Its structure is based on two identical sequences derived from enkephalins joined C-terminal to C-terminal by an hydrazide bridge (Tyr-D-Ala-Gly-Phe-NH-NH <- Phe <- Gly <- D-Ala <- Tyr). In this study we present the design, synthesis, and biological evaluation of the first cyclic biphalin analogues. D-Alanine residues in positions 2, 2' of the parent peptide were replaced by D- and L-cysteine and an intramolecular disulfide bond between the cysteine thiol groups was introduced. We obtained two cyclic analogues with quite different biological profiles. (c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2005.09.080