H-D-Tyr(t-Bu)-Arg(Pbf)-Arg(Pbf)-Nal-Gly-aldoxime | 1292807-45-4

• 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-D-Tyr(t-Bu)-Arg(Pbf)-Arg(Pbf)-Nal-Gly-aldoxime
• CAS: 1292807-45-4
• 化学式: C₆₆H₉₀N₁₂O₁₂S₂
• 分子量: 1307.65
• InChiKey: FRKXMYLMVMYJAH-IBDQIQQUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.0
• 重原子数：
  92.0
• 可旋转键数：
  26.0
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  366.8
• 氢给体数：
  12.0
• 氢受体数：
  16.0

反应信息

• 作为反应物：
  描述：

  H-D-Tyr(t-Bu)-Arg(Pbf)-Arg(Pbf)-Nal-Gly-aldoxime 在 N-氯代丁二酰亚胺 、 氢气 、 溶剂黄146 作用下， 以 甲醇 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 2.0h， 生成 cyclo[-D-Tyr(t-Bu)-Arg(Pbf)-Arg(Pbf)-Nal-Gly-ψ[C(=NH)-NH]-]
  参考文献：
  名称：

  Potent CXCR4 Antagonists Containing Amidine Type Peptide Bond Isosteres

  摘要：

  A series of FC131 [cyclo(-D-Tyr-Arg-Arg-Nal-Gly-)] analogues containing amidine type peptide bond isosteres were synthesized as selective CXC chemokine receptor type 4 (CXCR4) antagonists. An isosteric amidine substructure was constructed by a macrocyclization process using nitrile oxide-mediated C-N bond formation. All of the amidine-containing FC131 analogues exhibited potent SDF-1 binding inhibition to CXCR4. The Nal-Gly-substituted analogue was characterized as one of the most potent cyclic pentapeptide-based CXCR4 antagonists reported to date. The improved activity against human immunodeficiency virus (HIV) type-1 X4 strains suggested that addition of another basic amidine group to the peptide backbone effectively increases the selective binding of the peptides to CXCR4 receptor.

  DOI：

  10.1021/ml200047e
• 作为产物：
  描述：

  (9H-芴-9-基)-2-氧代乙基氨基甲酸甲酯 、 Fmoc-O-叔丁基-D-酪氨酸 、 Fmoc-3-(2-萘基)-L-丙氨酸 、 Fmoc-Pbf-L-精氨酸 在 5-Chloro-2,3-bis(4-chlorophenyl)-pyrazine 、 溶剂黄146 、 原甲酸三甲酯 、 哌啶 作用下， 以 1,2-二氯乙烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 2.0h， 生成 H-D-Tyr(t-Bu)-Arg(Pbf)-Arg(Pbf)-Nal-Gly-aldoxime
  参考文献：
  名称：

  Potent CXCR4 Antagonists Containing Amidine Type Peptide Bond Isosteres

  摘要：

  A series of FC131 [cyclo(-D-Tyr-Arg-Arg-Nal-Gly-)] analogues containing amidine type peptide bond isosteres were synthesized as selective CXC chemokine receptor type 4 (CXCR4) antagonists. An isosteric amidine substructure was constructed by a macrocyclization process using nitrile oxide-mediated C-N bond formation. All of the amidine-containing FC131 analogues exhibited potent SDF-1 binding inhibition to CXCR4. The Nal-Gly-substituted analogue was characterized as one of the most potent cyclic pentapeptide-based CXCR4 antagonists reported to date. The improved activity against human immunodeficiency virus (HIV) type-1 X4 strains suggested that addition of another basic amidine group to the peptide backbone effectively increases the selective binding of the peptides to CXCR4 receptor.

  DOI：

  10.1021/ml200047e