Acta Phys. -Chim. Sin. ›› 2016, Vol. 32 ›› Issue (1): 274-282.doi: 10.3866/PKU.WHXB201511021

• ARTICLE • Previous Articles     Next Articles

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
  • 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])


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


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