Probing the interaction of cephalosporin antibiotic cefoperazone with lysozyme using spectroscopic and in silico methods: Effect of paracetamol on binding

The interaction of lysozyme with cefoperazone was studied by means of spectroscopic and computational ap-proaches. The change in the UV-visible spectrum of lysozyme in presence of cefoperazone was an indication of the complex formation between them. Fluorescence spectroscopy suggested that there was a fair interaction between the protein and drug which was taken place via dynamic quenching mechanism and the binding ratio was approximately 1:1. The binding was energetically feasible and principally supported by the hydrophobic forces. CD spectroscopic studies have shown that cefoperazone induced the secondary structure of lysozyme by increasing the & alpha;-helical contents of the latter. In silico studies revealed that the large nonpolar cavity was the preferred binding site of cefoperazone within lysozyme and the interaction was taken place mainly through hydrophobic forces with small involvement of hydrogen bonding and electrostatic interactions which is in good agreement with the experimental analyses. Effect of paracetamol was also seen on the binding and it was found that paracetamol had a negative influence on the binding between cefoperazone and lysozyme.

Automated summary

The interaction between lysozyme and cefoperazone was studied using spectroscopic and computational approaches. The UV-visible spectrum showed a change in lysozyme in the presence of cefoperazone, indicating complex formation. Fluorescence spectroscopy suggested a fair interaction via dynamic quenching, with a binding ratio of approximately 1:1. In silico studies revealed that hydrophobic forces played a major role in the interaction, with some involvement of hydrogen bonding and electrostatic interactions.