• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>RSC Advances >Characterizing the binding interaction of astilbin with bovine serum albumin: a spectroscopic study in combination with molecular docking technology
【24h】

Characterizing the binding interaction of astilbin with bovine serum albumin: a spectroscopic study in combination with molecular docking technology

机译：表征曲霉菌素与牛血清白蛋白的结合相互作用：结合分子对接技术的光谱研究

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

摘要

Astilbin (ASN) is a flavonoid compound isolated from the rhizome of Smilax china L. (Smilacaceae). It has many bioactivities, such as selective immunosuppression, antioxidant, anti-hepatic injury, etc. , and is widely used in traditional Chinese medical treatments. The interaction of ASN with bovine serum albumin (BSA) was studied in a physiological buffer (pH = 7.40) using multi-spectroscopic techniques in combination with molecular docking methods. UV-vis absorption measurements proved that a ASN–BSA complex could be formed. Fluorescence data revealed that ASN could strongly quench the intrinsic fluorescence of BSA in terms of a static quenching procedure. The process of binding was spontaneous and the binding occurred mainly through hydrogen bonding and van der Waals forces. The distance r between donor (BSA) and acceptor (ASN) was calculated to be 4.80 nm based on F?rster's non-radiative energy transfer theory. The binding constant ( K _(a) = 7.31 × 10 ~(4) mol L ~(?1) ) and the number of binding sites ( n ≈ 1) at 298 K suggested that ASN only occupied one site in BSA with high affinity. Moreover, the results of molecular docking indicated that ASN was more likely to be located in site I (sub-domain IIA) of BSA. The results of synchronous fluorescence and three-dimensional fluorescence spectra showed that ASN induced conformational changes of BSA. The findings would be beneficial for research on the transportation, distribution and some important bioactivities of ASN in the human body.
机译：曲霉菌素（ASN）是一种从S（Smilax china L。）（S科）的根茎中分离出来的类黄酮化合物。它具有多种生物活性，如选择性免疫抑制，抗氧化剂，抗肝损伤等，被广泛用于中医治疗中。使用多光谱技术结合分子对接方法，在生理缓冲液（pH = 7.40）中研究了ASN与牛血清白蛋白（BSA）的相互作用。紫外可见吸收测量证明可以形成ASN-BSA复合物。荧光数据表明，按照静态猝灭程序，ASN可以强烈猝灭BSA的固有荧光。结合过程是自发的，结合主要通过氢键和范德华力发生。根据弗斯特非辐射能量转移理论，施主（BSA）与受主（ASN）之间的距离r为4.80 nm。结合常数（K _（a）= 7.31×10〜（4）mol L〜（？1））和298 K处的结合位点数目（n≈1）表明ASN仅在BSA中占据一个高位点亲和力。此外，分子对接的结果表明，ASN更有可能位于BSA的I位（亚域IIA）。同步荧光和三维荧光光谱结果表明，ASN诱导了BSA的构象变化。这些发现将有助于研究ASN在人体中的运输，分布和一些重要的生物活性。

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