| Rosuvastatin (ROS) is an anti-cholesterol drug belonging to statin drugs. A multi-spectroscopic approach combined with a molecular modeling technique was used to assess ROS association with human serum albumin
(HSA). Besides, an HSA immobilized surface plasmon resonance (SPR) chip was used to obtain kinetic parameters
(ka, kd, and KD). Fluorescence quenching titrations revealed that ROS interacts with HSA via a dynamic,
exothermic, enthalpy-driven mechanism. Hydrogen bonds and van der Waals interactions as the most prevalent
bonding forces contribute to ROS-HSA complex formation. ROS binding to HSA alters HSA conformation. The
SPR results indicated that ROS and HSA have a strong interaction possessing an equilibrium constant (KD) of
1.55 × 10− 8 M at 298 K. A competitive analysis of site markers showed that ROS has a higher tendency to bind to
the warfarin binding site (site IIA), which may explain why warfarin has a higher anticoagulant effect in ROS
users. FRET analysis indicated that non-radiation energy transfer occurred between ROS and HSA. According to
molecular docking studies, ROS prefers binding sites IB and IIA while the ROS-HSA complex stabilizes due to the
hydrogen bond and π-π interaction. The presence of hydrogen-bond donors and acceptors, as well as aromatic
ROS moieties, facilitates such interactions. |