Chinese Journal of Applied Chemistry ›› 2020, Vol. 37 ›› Issue (5): 604-610.DOI: 10.11944/j.issn.1000-0518.2020.05.190303

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Interaction Mechanism Between Thiourea Aryl Iridium Anticancer Complex and Bovine Serum Albumin

XIE Xingqin()   

  1. Department of Metallurgy and Resource Engineering,Nanning Campus, Guilin University of Technology,Chongzuo,Guangxi 532100,China
  • Received:2019-11-14 Accepted:2020-02-20 Published:2020-05-01 Online:2020-04-29
  • Supported by:
    Supported by the Guangxi University Young Teachers Basic Ability Promotion Project(No.2019KY0288)

Abstract:

In this paper, the interaction between thiourea aryl iridium and bovine serum albumin (BSA) was studied by ultraviolet-visible spectroscopy (UV-Vis) and fluorescence spectroscopy under physiological conditions. The mechanism of action was determined, the type of binding force was discussed, and the activation energy of the reaction of thiourea aryl iridium anticancer compound with bovine serum albumin was calculated. The experimental results show that m-methoxybenzaldehyde 4-phenyl-3-thiourea aryl iridium (TSC-Ir-6) complex has a quenching effect on endogenous fluorescence of bovine serum albumin, and the quenching type is static quenching. Through the fixed Stern-Volmer equations and apparent binding constant, the thermodynamic parameters calculated by the formula, it is concluded that the combination of TSC-Ir-6 and BSA is a spontaneous process (ΔG<0), and the interaction forces are hydrogen bonding and van der Waals force. The number of binding sites is about one. With the presence of coexisting ions, the binding constant between TSC-Ir-6 and BSA is significantly increased, the binding force is stronger, and the retention time of TSC-Ir-6 in plasma is improved, which may lead to a better therapeutic effect.

Key words: thiourea aryl iridium complex, bovine serum albumin, ultraviolet-visible spectroscopy, fluorescent spectrometry, interaction