HSA and DNA binding analysis of antiviral drug cidofovir: Spectroscopic and molecular docking techniques

[Display omitted] •The interaction of cidofovir with ct-DNA and HSA was investigated.•This study combined a variety of spectroscopic techniques with molecular docking simulation.•The binding constant and binding site have been determined.•The interaction mode between cidofovir and ct-DNA was groove binding.•The findings revealed that cidofovir binds to subdomain IIIA, specifically Sudlow’s site II of HSA. This article discusses the interaction of antiviral drug cidofovir (CDV) with biomolecules (HSA and DNA) under simulated physiological conditions (pH 7.4). The binding propensity of CDV with DNA was assessed through UV–visible absorption spectroscopy, fluorescence spectroscopy, and molecular docking. The results of fluorescence spectroscopy indicated that the binding of CDV to DNA induced fluorescence quenching through a static quenching mechanism, with a binding constant of 1.03 × 103 M−1 at 293 K. The groove mode of CDV binding to calf thymus DNA (ct-DNA) was validated using dye displacement assays. The results from molecular docking confirmed the binding mode and supported the findings obtained through spectroscopic techniques. Furthermore, the binding propensity of CDV with HSA was assessed through fluorescence spectroscopy, UV–visible absorption spectroscopy, and docking simulation. The fluorescence data indicated that CDV quenches the intrinsic fluorescence of the protein through a static quenching process, with a binding constant of 5.60 × 103 M−1 at 293 K. Meanwhile, the results of docking simulation confirmed our spectroscopic findings.