Analysis on the interaction and binding properties of daphnoretin and human serum albumin in the presence of cisplatin: multi-spectroscopic methods and docking simulation

• DOI: 10.1016/j.ejps.2021.105723
• Publication Date: 2021-01-19T16:33:51Z
• Authors: Yuanhao Liang; Liang Xu; Hongtian Yang; Wenli Xu; Ruixue Hu; Xiaoying Fan; Yufeng Liu
• Keywords: Molecular Docking Simulation; 0303 health sciences; 03 medical and health sciences; Binding Sites; Spectrometry, Fluorescence; Coumarins; Circular Dichroism; Humans; Thermodynamics; Serum Albumin, Human; Cisplatin; Protein Binding

The interaction between anticancer drugs and HSA may have a significant impact on the pharmacology and efficacy of drugs. Drugs change the binding properties of HSA by regulating the quenching mechanism, binding mode and binding affinity. In this study, the interactions of cisplatin (cDDP), HSA, and daphnoretin were elucidated by multi-spectroscopic analyses and docking simulation. Fluorescence quenching showed that cDDP could not change the static quenching mechanism of HSA-daphnoretin, but could enhance their binding affinity. Site competition experiments revealed that daphnoretin and cDDP both bound to site I, which was consistent with the results of molecular docking. Thermodynamic date indicated that cDDP and daphnoretin formed a more stable complex with HSA via hydrophobic, van der Waals interaction and hydrogen bond. Three-dimensional fluorescence and circular dichroism spectra showed that cDDP changed the conformation and micro-environment of HSA induced by daphnoretin. This work could provide valuable information for the binding properties and interaction among cDDP, daphnoretin and HSA, and put forward the possibility of using HSA as a multidrug carrier.