Employing Spectroscopic, Electrochemical, and In Silico Research to Investigate the Interaction of Ofloxacin, Antibacterial Drug With the Haemoglobin

Abstract

Understanding the intricate interplay between proteins and ligands is pivotal for rational drug development. This study investigates the binding of Ofloxacin to Hb using diverse biophysical techniques: fluorescence spectroscopy, UV‐visible spectroscopy, molecular docking, molecular dynamics simulations, and electrochemical analysis. Spectrophotometric data confirm a static quenching mechanism in ofloxacin‐Hb binding. Notably, ofloxacin‐Hb binding exhibits a significant change in free energy (−17.134 kJ/mol) and strong affinity via molecular docking was also observed (−8.2 kcal/mol). Molecular dynamics simulations validated these results, showing a change in free energy of −91.093 kJ/mol with minimal error of 13.508 kJ/mol, supporting a plausible interaction. Additionally, cyclic voltammetry elucidated dynamic interactions between Hb and ofloxacin. This comprehensive approach provides insights into drug‐protein binding dynamics, crucial for refining drug development strategies.