Characterizing the interaction between oridonin and bovine serum albumin by a hybrid spectroscopic approach

Oridonin is an effective anticancer drug which has high potency and low systemic toxicity. In this study, the interaction between oridonin and bovine serum albumin (BSA) was investigated by several spectroscopic approaches for the first time. The binding characteristics of oridonin and BSA were determined by fluorescence emission spectra and resonance light scattering spectra. It is showed that the oridonin quenches the fluorescence of BSA and the static quenching constant KSV is 1.30×104 L mol−1 at 298 K. Moreover, oridonin and BSA form a 1:1 complex with a binding constant of 0.62×104 L mol−1. On the other hand, the thermodynamic parameters indicate that the binding process was a spontaneous molecular interaction procedure, in which hydrophobic forces played a major role. The structure analysis indicates that oridonin binding results in an increased hydrophobicity around the tryptophan residues of BSA. Additionally, as shown by the UV–vis absorption, synchronous fluorescence and three-dimensional fluorescence results, oridonin could lead to conformational and some microenvironmental changes of BSA. The work provides accurate and full basic data for clarifying the binding mechanism of oridonin with BSA in vitro and is helpful for understanding its effect on protein function during its transportation and distribution in blood. - Highlights: ► Interaction between oridonin and BSA was evaluated by multi-spectroscopic methods. ► Binding constant, number of binding sites and thermodynamic parameters were calculated. ► Oridonin binds to Subdomain II site in BSA and form a 1:1 complex with it. ► Oridonin-BSA complex is stabilized mainly by hydrophobic force. ► Oridonin binding induces conformational and microenvironmental changes in BSA.