Abstract
The quality and strength of drug and albumin interaction affecting the drug-free concentration and physiological activity are important issues in pharmacokinetic research. In the present study, not only did we evaluate the binding strength of ceftriaxone and ceftizoxime to bovine serum albumin (BSA), but we also investigated the kinetic and thermodynamic parameters including KD, KA, ΔS, and ΔH. We applied in vitro optical fluorescence spectroscopy and surface plasmon resonance (SPR) sensing approaches as well as molecular docking analyses. The kinetic and thermodynamic investigations were done using different concentrations of drugs at three temperatures. Thermodynamic parameters visibly demonstrated that the binding was an exothermic and spontaneous process. The obtained negative values of both enthalpy change (ΔH) and entropy change (ΔS) in fluorescence and SPR and also molecular docking investigations showed that the major binding force involved in the complexation of drugs to BSA was hydrogen bonding. Static quenching was the foremost fluorescence quenching mechanism between them. Furthermore, the results of ΔG and KD values proved that the interaction of ceftriaxone-BSA was stronger than ceftizoxime-BSA. Finally, molecular docking confirmed that the preferable binding sites of ceftizoxime and ceftriaxone were site IIA and site IB of albumin, respectively.
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Acknowledgements
The authors are grateful for the financial support (grant no: IR.ARUMS.REC.1399.021) from the Ardabil University of Medical Sciences.
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This paper was supported by the Ardabil University of Medical Sciences (grant no: IR.ARUMS.REC.1399.021).
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F Fathi studied conception and design, performed SPR experiments, prepared draft manuscript, and co-wrote the paper; H Monirinasab performed spectral experiments and co-wrote the paper; M Zakariazadeh performed docking analyses; H Kohestani analyzed data and co-wrote the paper; and Morteza Kouhestani analyzed and interpreted the results.
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Monirinasab, H., Zakariazadeh, M., Kohestani, H. et al. Study of β-lactam-based drug interaction with albumin protein using optical, sensing, and docking methods. J Biol Phys 48, 177–194 (2022). https://doi.org/10.1007/s10867-021-09599-0
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DOI: https://doi.org/10.1007/s10867-021-09599-0