物理化学学报 >> 2016, Vol. 32 >> Issue (1): 274-282.doi: 10.3866/PKU.WHXB201511021

论文 上一篇    下一篇

吡虫啉与人血清白蛋白相互作用热力学行为

郭清莲1,潘凌立2,杨立云3,何欢3,张业中3,刘义3,*()   

  1. 1 武汉大学中南医院,武汉 430071
    2 黄石市中心医院,湖北黄石 435002
    3 武汉大学化学与分子科学学院化学系,武汉430072
  • 收稿日期:2015-09-21 发布日期:2016-01-13
  • 通讯作者: 刘义 E-mail:yiliuchem@whu.edu.cn
  • 基金资助:
    湖北省卫生计生委重点项目(WJ2015MB097);武汉黄鹤英才(科技)计划(2014[10])

Thermodynamics of the Interaction of Imidacloprid with Human Serum Albumin

Qing-Lian GUO1,Ling-Li PAN2,Li-Yun YANG3,Huan HE3,Ye-Zhong ZHANG3,Yi LIU3,*()   

  1. 1 Zhongnan Hospital, Wuhan University, Wuhan 430071, P. R. China
    2 Center Hospital of Huangshi City, Huangshi 435002, Hubei Province, P. R. China
    3 Department of Chemistry, College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, P. R. China
  • Received:2015-09-21 Published:2016-01-13
  • Contact: Yi LIU E-mail:yiliuchem@whu.edu.cn
  • Supported by:
    the Key Project of Health and Family Planning Commission of Hubei Province, China(WJ2015MB097);WuhanYellow Crane Talents Program for Science and Technology, China(2014[10])

摘要:

在模拟人体生理条件下,综合利用荧光光谱、紫外吸收光谱、圆二色谱和分子模拟等方法,研究了吡虫啉(IMI)和人血清白蛋白(HSA)相互作用的热力学行为。荧光光谱和紫外吸收光谱的分析表明:吡虫啉能有效猝灭HSA的内源荧光,猝灭机制为静态猝灭;通过所获取的相互作用热力学参数,可知两者之间的相互作用是一个吉布斯自由能降低的自发过程,且二者之间的主要作用力为氢键和范德华力。位点竞争实验和分子模拟的结果表明:吡虫啉在HSA的主要结合位置为位点?。圆二色谱、同步荧光光谱和三维荧光的分析发现:吡虫啉引起HSA的构象发生改变,其α-螺旋含量降低,无规卷曲含量升高,肽链结构在吡虫啉的作用下有所伸展。

关键词: 吡虫啉, 人血清白蛋白, 相互作用, 热力学参数

Abstract:

The thermodynamics of the interaction between human serum albumin (HSA) and imidacloprid (IMI) was investigated using fluorescence, UV-Vis absorbance, and circular dichroism spectroscopy, in addition to molecular modeling under physiological conditions. The fluorescence quenching of HSA by IMI was a static process, which was confirmed by the UV-Vis absorption spectra. The calculated enthalpy (ΔH) and entropy (ΔS) changes implied that hydrogen bonds and van der Waals forces played a predominant role in the binding process. Site marker competitive experiments along with molecular docking indicated that the binding of IMI to HSA took place primarily in site?. The circular dichroism and synchronous fluorescence spectroscopy demonstrated that the secondary structure of HSA changed after its interaction with IMI, causing the α-helix content to decrease with an increase in anunordered structure. The peptide structure extended after binding with IMI.

Key words: Imidacloprid, Human serum albumin, Interaction, Thermodynamics parameter

MSC2000: 

  • O642