...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Synthesis, solution structure analysis and antibody binding of cyclic epitope peptides from glycoprotein D of Herpes simplex virus type I
【24h】

Synthesis, solution structure analysis and antibody binding of cyclic epitope peptides from glycoprotein D of Herpes simplex virus type I

机译：单纯疱疹病毒I型糖蛋白D的环状表位肽的合成，溶液结构分析和抗体结合

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Two cyclic peptides with a thioether bond have been synthesised corresponding to the 9-22 ((9)LKMADPNRFRGKDL(22)) sequence of glycoprotein D (gD-1) of Herpes simplex virus. The role of the secondary structure in protein-specific monoclonal antibody recognition was investigated. The sequence selected for this study comprises a strongly antigenic site adopting a beta-turn at residues (14)Pro-(15)Asn. Thioether bond was formed between the free thiol group of cysteine or homocysteine inserted in position 11 and the chloroacetylated side chain of lysine in position 18. We report here the preparation of cyclic peptides containing Cys or Hcy in position 11, differing only in one methylene group. The linear precursor peptides were synthesised by Boc/Bzl strategy on MBHA resin, and the cyclisation was carried out in alkaline solution. The secondary structure of the peptides was studied by CD, FT-IR and NMR spectroscopy. The CD and FT-IR data have revealed fundamental changes in the solution conformation of the two compounds. The CH, group difference significantly resulted in the altered turn structure at the 12 Ala and (13)Asp as identified by NMR spectroscopy. The antibody binding properties of the cyclopeptides studied by gD-specific monoclonal antibody (A16) in direct and competition enzyme-linked immunosorbent assay (ELISA) were also not the same. We found that peptide LK[HcyADPNRFK]GKDL exhibited higher affinity to Mab A16 than peptide LK[CADPNRFK]GKDL, however, their reactivity was significantly lower compared to the linear ones. Our results clearly show the importance of secondary structure in an antibody binding and demonstrate that even a slight modification of the primary structure dramatically could influence the immune recognition of the synthetic antigens. (C) 2003 Elsevier B.V. All rights reserved. [References: 38]
机译：已合成了两个带有硫醚键的环肽，分别对应于单纯疱疹病毒糖蛋白D（gD-1）的9-22（（9）LKMADPNRFRGKDL（22））序列。研究了二级结构在蛋白质特异性单克隆抗体识别中的作用。选择用于该研究的序列包含在残基（14）Pro-（15）Asn处采用β转角的强抗原位点。在位置11插入的半胱氨酸或高半胱氨酸的游离巯基与位置18赖氨酸的氯乙酰化侧链之间形成硫醚键。我们在此报告在位置11包含Cys或Hcy的环状肽的制备，仅一个亚甲基不同。通过Boc / Bzl策略在MBHA树脂上合成线性前体肽，并在碱性溶液中进行环化。通过CD，FT-IR和NMR光谱研究了肽的二级结构。 CD和FT-IR数据揭示了这两种化合物溶液构象的根本变化。 CH，基团的差异显着导致通过NMR光谱法鉴定的在12 Ala和（13）Asp处的转向结构改变。用gD特异性单克隆抗体（A16）在直接和竞争酶联免疫吸附测定（ELISA）中研究的环肽的抗体结合特性也不相同。我们发现，肽LK [HcyADPNRFK] GKDL对Mab A16的亲和力比肽LK [CADPNRFK] GKDL高，但与线性酶相比，它们的反应性低得多。我们的结果清楚地表明了二级结构在抗体结合中的重要性，并表明即使一级结构的微小修饰也可以显着影响合成抗原的免疫识别。 （C）2003 Elsevier B.V.保留所有权利。 [参考：38]

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号