H-Ala-Gly-Val-Ser-Gly-His-Gly-Gln-His-Gly-Val-His-Gly-OH | 1225278-93-2

• 分子结构分类: 有机化合物 - 有机聚合物 - 多肽
• 英文名称: H-Ala-Gly-Val-Ser-Gly-His-Gly-Gln-His-Gly-Val-His-Gly-OH
• 英文别名: [Ala(1)]-alloferon；AGVSGHGQHGVHG
• CAS: 1225278-93-2
• 化学式: C₄₉H₇₄N₂₀O₁₆
• 分子量: 1199.25
• InChiKey: HAYYXHDQMNTMKE-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30%的产率得到H-Ala-Gly-Val-Ser-Gly-His-Gly-Gln-His-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

• Studies of insect peptides alloferon, <i>Any</i> -GS and their analogues. Synthesis and antiherpes activity
  作者：Mariola Kuczer、Katarzyna Dziubasik、Anna Midak-Siewirska、Renata Zahorska、Mirosław Łuczak、Danuta Konopińska

  DOI：10.1002/psc.1219

  日期：2010.4

  The subject of these studies was synthesis and determination of biological properties of a series of insect peptides, such as alloferon, Any‐GS and their analogues. The synthesis of 14 peptides was performed by the solid‐phase method. Biological effect of these peptides was evaluated by the antiviral test against Human Herpes Virus type 1 (HHV‐1) in vitro using a Vero cell line. It was found that the

  这些研究的主题是一系列昆虫肽的合成和生物学特性的测定，例如Alloferon，Any- GS及其类似物。14种肽的合成通过固相方法进行。通过使用Vero细胞系在体外针对1型人类疱疹病毒（HHV-1）进行的抗病毒测试，评估了这些肽的生物效应。发现所研究的肽抑制了Vero细胞中HHV-1的复制。版权所有©2010欧洲肽协会和John Wiley＆Sons，Ltd.。