• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>RSC Advances >Binding interaction of an anionic amino acid surfactant with bovine serum albumin: physicochemical and spectroscopic investigations combined with molecular docking study
【24h】

Binding interaction of an anionic amino acid surfactant with bovine serum albumin: physicochemical and spectroscopic investigations combined with molecular docking study

机译：阴离子氨基酸表面活性剂与牛血清白蛋白的结合相互作用：物理化学和光谱研究结合分子对接研究

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

The interaction of a synthesised amino acid surfactant, sodium-N-dodecanoylphenylalaninate (AAS) with a transport protein, bovine serum albumin (BSA) has been uncovered employing various physicochemical and spectroscopic techniques like tensiometry, electro kinetic potential measurements, steady-state fluorometry, time-resolved measurements and circular dichroism (CD) at physiological pH and 298 K. The difference in tensiometric responses of AAS in the absence and presence of BSA indicates a significant interaction operative between them. The zeta (xi) potential measurements have been taken into account in assigning the type of binding interaction between them. The steady-state fluorescence study reveals the sequential unfolding of BSA with stepwise addition of AAS. Stern-Volmer and modified Stern-Volmer plots, Scatchard plots and thermodynamic parameters have been employed to find the type of binding of AAS to BSA. Life-time measurements have been carried out to shed light on the relative amplitude of binding of AAS to the two Trp residues of BSA namely Trp-134 and Trp-213. The changes in protein secondary structure induced by AAS are unveiled by CD measurements. Quantum mechanical calculations involving density functional theory (DFT) and molecular docking analysis have been undertaken to highlight the interactive phenomenon between the two. Thus this work shows a total inspection of an amino acid surfactant-BSA interaction.
机译：的相互作用的合成氨基酸表面活性剂，钠-N-dodecanoylphenylalaninate（AAS）带的输送蛋白，牛血清白蛋白（BSA）已经发现了使用各种物理化学和技术，如张力测量光谱，电动势的测量，稳态荧光，生理pH和298k时的时间分辨测量和圆形二色性（CD）。在没有和存在BSA的情况下AA的张力反应的差异表明它们之间的显着相互作用。在分配它们之间的绑定相互作用时已经考虑了Zeta（Xi）潜在测量。稳态荧光研究揭示了BSA的顺序展开，逐步添加AAS。已采用船尾波尔和改进的船尾波尔图，Scatchard图和热力学参数来找到AA与BSA的结合类型。寿命时间测量已经进行了对与BSA的两个色氨酸残基即TRP-134和Trp-213 AAS结合的相对振幅线索。 AA诱导的蛋白质二级结构的变化通过CD测量推出。已经进行了涉及密度泛函理论（DFT）和分子对接分析的量子力学计算，以突出两者之间的互动现象。因此，该工作显示了氨基酸表面活性剂-BSA相互作用的总检测。

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