Interaction of a cobalt(III) complex containing β-amino alcohol with human serum albumin (HSA): Spectroscopic and molecular docking methods

Abstract

The current work aimed to explore the binding interaction of cobalt(III) complex containing [2-[(E)-({2-[(2-hydroxy ethyl) amino] ethyl} imino) methyl] phenol] ligand with human serum albumin (HSA) in simulative physiological condition (pH 7.4) based on multi-spectroscopic and molecular docking methods. By adding cobalt(III) complex, the HSA absorption was decreased which is a reason for interaction between them. Fluorescence studies and the calculated Ksv and Kq values confirmed that the quenching process is static. Thermodynamic data (ΔH°, and ΔS°) showed that the nature of the interaction forces are hydrophobic and Van der Waals types. A negative sign of Gibbs free energy also indicates the spontaneity of the reaction. The displacement experiments using the site probes warfarin and ibuprofen substantiated that cobalt(III) complex could bind to site I of HSA (subdomain IIA).