摘要
采用荧光猝灭光谱（FS）、圆二色光谱（CD）、红外光谱（IR）研究了鹅掌楸碱（LA）与牛血清白蛋白（BSA）的结合反应。通过研究发现,鹅掌楸碱和BSA的相互作用机制为静态猝灭。计算了不同温度下的结合常数、结合位点及热力学参数,根据热力学参数推断静电作用力是维系复合物稳定的主要作用力;通过探针反应判断结合位点在SiteⅠ处。根据F9ster荧光共振能量转移理论,计算结合距离r=2.58 nm,说明二者之间形成了LA-BSA配合物。通过同步荧光、圆二色及红外光谱证实了鹅掌楸碱的结合导致了BSA的构象发生了改变。红外曲线拟合定量计算结果显示,BSA的α-螺旋百分含量由50.8%降低到46.5%,表明药物的存在明显改变了BSA的二级结构。
The interaction between liriodenine（ LA） and bovine serum albumin（ BSA） was investigated by fluorescence spectroscopy（ FS）,circular dichroism spectrum（ CD） and IR spectroscopy.The results indicate that the combination reaction of LA with BSA is a static quenching process.The binding constants,the number of binding sites,and corresponding thermodynamic parameters were calculated,respectively.Based on the thermodynamic parameters,it is speculated that the electrostatic forces play a main role in maintenance stability of complex.Binding site is in the site Ⅰ judged by the probe reaction. The binding distance is 2. 58 nm calculated by the foster fluorescence resonance energy transfer theory.The results show that the conformation of BSA changed due to the interaction of LA.The quantitative calculation of infrared curve fitting shows that the percentage of BSA α-helix decreases from 50. 8% to 46. 5%,which suggests that the presence of LA significantly changes the secondary structure of BSA.
作者
石婧楠
温毛桂
于青
白丽娟
边贺东
刘延成
陈振锋
SHI Jing-nan;WEN Mao-gui;YU Qing;BAI Li-juan;BIAN He-dong;LIU Yan-cheng;CHEN Zhen-feng(Guaugxi Key Laboratory of Chemistry and Engineering of Forest Products, School of Chemistry and Chemical Engineering, Guangxi University for Nationalities, Nanning 530000, China;State Key Labora- tory for Chemistry and Moleculor Engineering of Medical Resources, Guangxi Normal University, Guilin 541004, China)
出处
《化学试剂》
CAS
北大核心
2018年第6期513-517,559,共6页
Chemical Reagents
基金
国家自然科学基金资助项目(21361003,21101035)
广西自然科学基金资助项目(2016GXNSFDA-380005,2011GXNSFC018009,2012GXNSFAA053035)
广西新世纪“十百千”人才计划资助项目(2014)
广西民族大学自然科学基金项目(2015)
广西民族大学研究生教育创新计划资助项目(gxun-chxzs2017120)
关键词
鹅掌楸碱
牛血清白蛋白
荧光光谱
红外光谱
圆二色光谱
liriodenine
bovine serum albumin
fluorescence spectroscopy
IR spectroscopy
circular dichroism spectroscopy
