...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >Nuclear Magnetic Resonance-Based Structural Characterization and Backbone Dynamics of Recombinant Bee Venom Melittin
【24h】

Nuclear Magnetic Resonance-Based Structural Characterization and Backbone Dynamics of Recombinant Bee Venom Melittin

机译：基于核磁共振的基于结构特征和骨干动力学的重组蜂毒素

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

In recent years, there has been a resurgence of interest in melittin and its variants as their therapeutic potential has become increasingly evident. Melittin is a 26-residue peptide and a toxic component of honey bee venom. The versatility of melittin in interacting with various biological substrates, such as membranes, glycosaminoglycans, and a variety of proteins, has inspired a slew of studies that aim to improve our understanding of the structural basis of such interactions. However, these studies have largely focused on melittin solutions at high concentrations (>1 mM), even though melittin is generally effective at lower (micromolar) concentrations. Here we present high-resolution nuclear magnetic resonance studies in the lower-concentration regime using a novel method to produce isotope-labeled (~(15)N and ~(13)C) recombinant melittin. We provide residue-specific structural characterization of melittin in dilute aqueous solution and in 2,2,2-trifluoroethanol/water mixtures, which mimic melittin structure–function and interactions in aqueous and membrane-like environments, respectively. We find that the cis–trans isomerization of Pro14 is key to changes in the secondary structure of melittin. Thus, this study provides residue-specific structural information about melittin in the free state and in a model of the substrate-bound state. These results, taken together with published work from other laboratories, reveal the peptide’s structural versatility that resembles that of intrinsically disordered proteins and peptides.
机译：近年来，由于其治疗潜力越来越明显，穆丁汀的兴趣及其变体具有重新疗效。 Melittin是一种26-残基肽和蜂蜜蜂毒液的毒性组分。 Melittin与各种生物基质相互作用的多功能性，例如膜，糖胺聚糖和各种蛋白质，启发了一种研究的旨在改善我们对这种相互作用的结构基础的理解。然而，这些研究在很大程度上集中于高浓度（> 1mm）的蛋白溶胶溶液，即使熔融素在较低（微摩尔）浓度下是有效的。在这里，我们使用一种新的方法在低浓度方案中呈现高分辨率核磁共振研究，以产生同位素标记的（〜（15）n和〜（13）c）重组茂热素。我们提供稀溶液中熔融素的残留物特异性结构表征，并分别在2,2,2-三氟乙醇/水混合物中，其分别模拟熔融素结构 - 功能和相互作用的水性和膜状环境。我们发现Pro14的 CIS-Trans异构化是Melittin二次结构变化的关键。因此，该研究提供了关于自由状态下的熔体素的残留物特异性结构信息和基板结合状态的模型。这些结果与其他实验室的公开工作一起揭示了肽的结构多功能性，类似于内在紊乱的蛋白质和肽。

著录项

  • 来源
    《Biochemistry》 |2018年第19期|共11页
  • 作者

    Lisa Ramirez; Alexander Shekhtman; Jayanti Pande;

  • 作者单位

    Department of Chemistry University at Albany State University of New York Albany New York 12222 United States;

    Department of Chemistry University at Albany State University of New York Albany New York 12222 United States;

    Department of Chemistry University at Albany State University of New York Albany New York 12222 United States;

  • 收录信息
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 生物化学;
  • 关键词

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