Electrochemical Studies and Molecular Docking Applications for the Interactions of a Riminophenazine Antibiotic Clofazimine With Serum Albumins (HSA and BSA) and Calf-Thymus DNA

Abstract

The interactions of clofazimime (CLF) with human serum albumin (HSA), bovine serum albumin (BSA) and calf thymus DNA (ct-DNA) were studied by square-wave voltammetry (SWV) at physiological pH. The cyclic voltammogram of CLF gave three reversible redox peak couples in the studied medium. SWV data showed that the cathodic current of CLF decreased by adding of HSA, BSA and ct-DNA owing to the molecular binding interactions. For these binding processes, thermodynamic quantities (Delta G degrees, Delta H degrees and Delta S degrees) and binding constants (K) were obtained and calculated from voltammetry data in the temperature range 295-310 K. Also, the molecular docking studies were carried out to obtain theoretical information about the interactions of CLF with A-DNA, B-DNA and serum albumins. The results of docking applications showed that CLF had the highest binding affinity (BA) for BSA.