• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Separate molecular determinants in amyloidogenic and antimicrobial peptides
【24h】

Separate molecular determinants in amyloidogenic and antimicrobial peptides

机译：淀粉样蛋白和抗菌肽中的单独分子决定因素

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

Several amyloid-forming and antimicrobial peptides (AMYs and AMPs) have the ability to bind to and damage cell membranes. In addition, some AMYs possess antimicrobial activity and some AMPs form amyloid-like fibrils, relating the two peptide types and their properties. However, a comparison of their sequence characteristics reveals important differences. The high β-strand and aggregation propensities typical of AMYs are largely absent in α-helix-forming AMPs, which are instead marked by a strong amphipathic moment not generally found in AMYs. Although a few peptides, for example, islet amyloid polypeptide and dermaseptin S9, combine some determinants of both groups, the structural distinctions suggest that antimicrobial activity and amyloid formation are separate features not generally associated.
机译：几种淀粉样蛋白和抗菌肽（AMY和AMP）具有结合并破坏细胞膜的能力。另外，一些AMY具有抗菌活性，一些AMP形成淀粉样蛋白原纤维，这与两种肽类型及其性质有关。然而，对其序列特征的比较揭示了重要的差异。在形成α-螺旋的AMPs中基本上不存在AMYs的典型高β链和聚集倾向，而是由AMYs中通常不存在的强两亲性矩来标记。尽管一些肽（例如，胰岛淀粉样蛋白多肽和dermaseptin S9）结合了两组的某些决定因素，但结构上的区别表明，抗菌活性和淀粉样蛋白的形成是通常不相关的独立特征。

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