H-His-Gly-Val-Ser-Gly-His-Gly-Gln-Ala-Gly-Val-His-Gly-OH | 1620150-28-8

• 分子结构分类: 有机化合物 - 有机聚合物 - 多肽
• 英文名称: H-His-Gly-Val-Ser-Gly-His-Gly-Gln-Ala-Gly-Val-His-Gly-OH
• 英文别名: [Ala⁹]-alloferon；HGVSGHGQAGVHG
• CAS: 1620150-28-8
• 化学式: C₄₉H₇₄N₂₀O₁₆
• 分子量: 1199.25
• InChiKey: VSKGOIDKBQJJIN-MYJLPPCUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -9.14
• 重原子数：
  85.0
• 可旋转键数：
  37.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  561.88
• 氢给体数：
  19.0
• 氢受体数：
  19.0

反应信息

• 作为产物：
  描述：

  Fmoc-gly-wang resin 、 Fmoc-甘氨酸 、 Fmoc-L-缬氨酸 、 Fmoc-L-丝氨酸 、 Fmoc-L-谷氨酰胺 、 N-芴甲氧羰基-L-组氨酸 在 哌啶 、 1-羟基苯并三唑 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 以36%的产率得到H-His-Gly-Val-Ser-Gly-His-Gly-Gln-Ala-Gly-Val-His-Gly-OH
  参考文献：
  名称：

  Copper(II) complexes of alloferon 1 with point mutations (H1A) and (H9A) stability structure and biological activity

  摘要：

  Mono- and polynuclear copper(II) complexes of the alloferon 1 with point mutations (H1A) A(1)GVSGH(6)GQH(9) GVH(12)G (Allo1A) and (H9A) H(1)GVSGH(6)GQA(9)GVH(12)G (Allo9A) have been studied by potentiometric, UV-visible, CD, EPR spectroscopic and mass spectrometry (MS) methods. To obtain a complete complex speciation different metal-to-ligand molar ratios ranging from 1:1 to 4:1 for Allo1A and to 3:1 for Allo9A were studied. The presence of the His residue in first position of the peptide chain changes the coordination abilities of the Allo9A peptide in comparison to that of the Allo1A.Imidazole-N3 atom of N-terminal His residue of the Allo9A peptide forms stable 6-membered chelate with the terminal amino group. Furthermore, the presence of two additional histidine residues in the Allo9A peptide (H-6,H-12) leads to the formation of the CuL complex with 4N {NH2,N-Im-H-1,N-Im-H-6,N-Im-H-12} binding site in wide pH range (5-8). For the Cu(II)-Allo1A system, the results demonstrated that at physiological pH 7.4 the predominant complex the CuH-L-1 consists of the 3N {NH2,N-,CO3NIm} coordination mode. The inductions of phenoloxidase activity and apoptosis in vivo in Tenebrio molitor cells by the ligands and their copper(II) complexes at pH 7.4 were studied. The Allo1A, Allo1K peptides and their copper(II) complexes displayed the lowest hemocytotoxic activity while the most active was the Cu(II)-Allo9A complex formed at pH 7.4. The results may suggest that the N-terminal-His(1) and His(6) residues may be more important for their proapoptotic properties in insects than those at positions 9 and 12 in the peptide chain. (C) 2014 Elsevier Inc. All rights reserved.

  DOI：

  10.1016/j.jinorgbio.2014.05.012

文献信息

• Novel analogs of alloferon: Synthesis, conformational studies, pro-apoptotic and antiviral activity
  作者：Mariola Kuczer、Elżbieta Czarniewska、Anna Majewska、Maria Różanowska、Grzegorz Rosiński、Marek Lisowski

  DOI：10.1016/j.bioorg.2016.03.002

  日期：2016.6

  Vero cells. [Ala9]-alloferon exhibits the strongest antiviral activity among the analyzed compounds. However, no cytotoxic activity against Vero cell line was observed for all the studied peptides. In vivo assays with hemocytes of T. molitor showed that [Lys9]-, [Phg9]-, [Lys12]-, and [Phe12]-alloferon exhibit a twofold increase in caspases activity in comparison with the native peptide. The CD conformational

  在这项研究中，我们报告了昆虫肽Alloferon（H-His-Gly-Val-Ser-Gly-His-Gly-Gln-His-Gly-Val-His-Gly-OH）的新型衍生物的构效关系。 。通过将位置9或12的His交换为天然或非天然氨基酸，可以修饰肽的结构。在使用Vero细胞系针对人疱疹病毒1 MCIntrie株（HHV-1 MC）进行的抗病毒体外测试中确定了这些肽的生物学特性。还评估了该肽在体内对黄粉虫甲虫血细胞的促凋亡作用。另外，通过在水和甲醇中的圆二色性检查了Alloferon类似物的结构性质。发现大多数评估的肽可以降低Vero细胞中的HHV-1滴度。在所分析的化合物中，[Ala 9 ]-别洛佛隆显示出最强的抗病毒活性。然而，对于所有研究的肽，未观察到针对Vero细胞系的细胞毒性活性。用T. molitor血细胞进行的体内分析显示[Lys 9 ]-，[Phg 9 ]-，[Lys 12