• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>BioTechnology: An Indian Journal >Comparative Investigation on the Interaction of Cefonicid Sodium with Bovine Transferrin and Bovine Serum Albumin by Multi-Spectroscopy
【24h】

Comparative Investigation on the Interaction of Cefonicid Sodium with Bovine Transferrin and Bovine Serum Albumin by Multi-Spectroscopy

机译：多重光谱法比较头孢尼丁钠与牛转铁蛋白和牛血清白蛋白的相互作用

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The reaction mechanisms of cefonicid sodium to bovine serum albumin and bovine transferrin were studied by multi-spectroscopy methods. The results demonstrated that new complexes were formed between cefonicid sodium and the two proteins, which resulted in a static quenching of fluorescence of the two proteins. And the numbers of binding sites in the two systems were approximately equal to 1. In the reaction system, the drug binds with the two proteins mainly through electrostatic force. It also showed that in the two systems the hydrophobic environment around amino acid residues changed, and the primary binding sites for cefonicid sodium were both closer to tryptophan residues. Circular dichroism spectroscopy showed that the secondary structures of the two proteins were changed. The values of Hill's coefficients indicating that there were negative co-operativities in the interaction between subsequent ligands and the two proteins. In addition, the studies have showed that the binding between bovine serum albumin and cefonicid sodium was stronger. However, cefonicid sodium had larger influences on the microenvironment of bovine transferrin. The interaction between cefonicid sodium and different proteins will be helpful for extracting the common features, applying the unique characteristic of drug-proteins systems.
机译：采用多光谱法研究了头孢烯啶钠与牛血清白蛋白和牛转铁蛋白的反应机理。结果表明，头孢尼考钠和两种蛋白之间形成了新的复合物，导致两种蛋白的荧光静态猝灭。并且两个系统中结合位点的数目大约等于1。在反应系统中，药物主要通过静电力与两种蛋白质结合。还表明在这两个系统中，氨基酸残基周围的疏水环境发生了变化，头孢尼丁钠的主要结合位点都更靠近色氨酸残基。圆二色光谱表明，两种蛋白质的二级结构均发生了变化。希尔系数的值表明随后的配体与两种蛋白质之间的相互作用中存在负协同作用。此外，研究表明，牛血清白蛋白和头孢尼西汀钠之间的结合更强。然而，头孢尼西钠对牛转铁蛋白的微环境影响较大。头孢烯啶钠与不同蛋白质之间的相互作用将有助于提取共同特征，并利用药物-蛋白质系统的独特特征。

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